Review

Received: 21 February 2021 Revised: 29 March 2021 Accepted article published: 1 April 2021 Published online in Wiley Online Library: 16 April 2021

(wileyonlinelibrary.com) DOI 10.1002/jctb.6745

Insights into polyester plastic biodegradation

by carboxyl ester hydrolases
Alisa Gricajeva,a Ashok Kumar Naddab* and Renata Gudiukaitea*

Abstract
Environmental pollution caused by polyesters has become a major ecological safety concern that needs to be managed
urgently. One way to resolve this problem is giving the spotlight to current emerging research of microbial biocatalysts. During
the last two decades many researchers have reported the ability to break down and modify natural and synthetic polyesters
using different microbial carboxyl ester hydrolases (lipases, esterases, cutinases, PETases, etc.) also called polyesterases, and
contribution of these enzymes towards the reduction of plastic levels in the future. Continuous search of such lipolytic bioca-
talysts and their improvement via protein engineering strategies results in beneficial findings making the use of polyesterases
in the biodegradation of plastics increasingly more realistic. The present review provides a comprehensive insight into the
structural properties enabling microbial lipolytic-type carboxyl ester hydrolases to effectively catalyze the cleavage of ester
linkages in different polyester plastics. Moreover, the management of extensively used polyester plastics using different lipo-
lytic enzymes as an innovative eco-friendly solution is presented in this report. Furthermore, improvement of polyesterases via
protein engineering for the development of more effective and suitable polyester-degrading lipolytic biocatalysts is summa-
rized in this review as well.
© 2021 Society of Chemical Industry (SCI).

Keywords: lipolytic enzymes; cutinases; polyester biodegradation; plastic waste

PTT poly(trimethylene terephthalate)

ABBREVIATIONS PUR polyurethane
3PET bis(benzoyloxyethyl) terephthalate PVA/PVAc polyvinyl acetate
aa amino acids PVC polyvinyl chloride
BHET bis(2-hyroxyethyl) terephthalate SBG substrate-binding groove
DB disulfide bonds/bridges Tg glass transition temperature
EG ethylene glycol Tm melting temperature
MHET mono(2-hydroxyethyl) terephthalate TPA terephthalic acid
MW molecular weight
OxH oxyanion hole
PA polyamines
PBAT poly(butylene adipate-co-butylene INTRODUCTION
terephthalate) Earth has been severely affected by plastic-based pollutants and
PBS polybutylene succinate every domain of biotic and abiotic components have been devas-
PBSA polybutylene succinate–co-adipate tatingly exposed. There are various forms of plastics that are being
PBST poly(butylene succinate-co-terephthalate) used in our day-to-day life, such as polyethylene-terephthalate
PCL poly(ε-caprolactone) (PET), polyamines (PA), polystyrene (PS), polyvinyl chloride (PVC),
PE polyethylene poly(ε-caprolactone) (PCL), polyurethane (PUR) and many more.
PEA poly(ethylene adipate) Due to their favorable mechanical and thermal properties, cheap
PEF polyethylene furanoate manufacture, stability and durability, they have been widespread
PEG polyethylene glycol
PES poly(ethylene succinate)
PET polyethylene-terephthalate * Correspondence to: R Gudiukaite, Institute of Biosciences, Life Sciences Center,
PHA polyhydroxyalkanoate Vilnius University, Sauletekis Avenue 7, 10257 Vilnius, Lithuania. E-mail: renata.
PHB polyhydroxy-butyrate gudiukaite@gf.vu.lt; or AK Nadda, Department of Biotechnology and Bioinfor-
matics, Jaypee University of Information Technology, Waknaghat, Solan,
PHBV poly(3-hydroxybutyrate-co-3-hydroxyvalerate) Himachal Pradesh, 173 234, India. E-mail: ashok.kumar@juit.ac.in
PLA/PLLA poly(L-lactic acid)
PoE polyester a Department of Microbiology and Biotechnology, Institute of Biosciences, Life
PoEs polyesters Sciences Center, Vilnius University, Vilnius, Lithuania
PPDO poly(p-dioxanone)
b Department of Biotechnology and Bioinformatics, Jaypee University of Infor-
359

PS polystyrene mation Technology, Solan, India

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and used for packaging, building materials and commodity as
well as hygiene products.1–5 Usually, most of the synthetic polyes-
ter (PoE) plastics (polyethylene (PE), PS, PVC and PET) are defined
as non-biodegradable, contrary to PCL, polyhydroxy-butyrate
(PHB) and its copolymer, poly(L-lactic acid) (PLA or PLLA) and ali-
phatic polyesters (PoEs) from different lactic acid derivatives.6,7
Approximately 100 million tons of plastics are produced each year
and within a short period of time almost half of them are disposed
to the environment.6 In fact, 93% of generated plastic wastes are
disposed of in landfill and oceans each year.8 Approximately, 12
billion tons of plastic waste are expected to accumulate in the
environment by 2050.9 Thus pollution from PoEs has become a
major environmental concern that needs urgent solutions.
The question arises regarding the fate of the PoE fibers that are
being released or accumulating in the environment. Unfortu-
nately, the effects of discarded PoEs on the environment, human
and animal health are not well known. Some plastics can be harm-
ful by mimicking hormones. One such example is vinyl chloride,
which is carcinogenic to humans and animals.10 When PoE- or
polyamide-based products are exposed to the external environ-
ment, they partially deteriorate, crack into pieces and eventually
form microplastics. One of the serious issues of the micro- and
nanoplastic formation is that these particles can easily enter the
marine ecosystem and cell membranes; moreover, these toxic
compounds can accumulate in fish.11 It was recently reported that
microplastics were detected for the first time in human placenta.12
The unsustainable use of PoE-based fabrics can be controlled by
developing new approaches preventing the release of fibers and
particles into the environment. To encourage their recycling and
reuse to a greater extent is a crucial step in managing this waste.
Moreover, to overcome the plastic-induced pollution, alternative
biodegradable plastics have gained much attention. Most of the
biodegradable PoE-type plastics have properties (good tenacity,
elasticity, etc.) comparable to conventional plastics; therefore,
these polymers are being intensively used in industry as an alter-
native to conventional plastics. The term ‘bioplastic’ can refer
either to bio-based plastics synthesized from biomass and renew-
able resources (e.g. PLA, polyhydroxyalkanoate (PHA)) or plastics
that are produced from fossil fuels (e.g. polybutylene succinate
(PBS)). Both types can serve as a substrate for microorganisms.7,8,13
7,8,13
When biodegradable plastics are assimilated by microorgan-
isms, they can be decomposed into CO2, CH4, H2O, inorganic com-
pounds or biomass.2,8,14–17 Thus plastic degradation mediated by
microbial enzymes is considered to be a promising solution to deal
with this environmental issue.2,7,14,18
During the last two decades many researchers have reported the
ability to break down and modify synthetic PoEs using microbial
enzymes and the contribution of these enzymes towards the reduc-
tion of plastic levels in the future.2,19–30 PoEs are dominant biode-
gradable polymers which can be affected by some microbial
carboxyl ester hydrolase (EC 3.1.1)-subclass enzymes. This review
therefore focuses on discussion and consideration of the role and
importance of PoE plastic degradation by microbial lipases
(EC 3.1.1.3), carboxylesterases or true esterases (EC 3.1.1.1) and cuti-
nases (EC 3.1.1.74), as well as highly related enzymes such as
PETases (EC 3.1.1.101) and PHA depolymerases (EC 3.1.1.75 and EC
3.1.1.76), which altogether can be called polyesterases.31–34 This arti-
cle provides a comprehensive insight into the structural properties
enabling lipases, esterases, cutinases (lipolytic enzymes),35–37 PET-
hydrolyzing enzymes (cutinases and PETases)38 and PHA depoly-
merases39 to effectively cleave ester linkages of different PoE plas-
360
tics. Furthermore, management of different PoEs using lipolytic
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A Gricajeva, AK Nadda, R Gudiukaite
enzymes and improvement of polyesterases via protein engineer-
ing for the development of more effective and suitable PoE-
degrading lipolytic biocatalysts are summarized and discussed
herein as well.
A SHORT DESCRIPTION OF NON-
BIOLOGICAL METHODS USED FOR
POLYESTER DEGRADATION
There are several physicochemical methods such as thermal, pho-
tochemical treatment, pyrolytic degradation, and photodegrada-
tion used for the conversion and reutilization of PoEs.40–44
However, the bioprocess economy, harsh degradation conditions
and formation of several by-products and harmful gases are the
major challenges that need to be overcome.
Photocatalytic degradation of the polyesters
Different PoEs are sensitive to UV radiation and photocatalytic oxi-
dation, which results in the production of free radicals. UV absorp-
tion occurs due to the presence of various hydroxyl groups –
additive impurities in the molecular structure of PoEs.45 The
photocatalytic oxidation of PoEs like PET is attributed to Norrish
type I and Norrish type II reactions.46 In the type I reaction splitting
of the molecule occurs near the carbonyl bond and results in the
formation of ketone, alkyl or aryl radicals around the ester linkage.
Norrish type II involves intramolecular reaction with cyclic six-
membered translation species, resulting in carboxylic end groups
and alkenes. Thus Norrish I degrades PoE by photoionization
whereas Norrish II degrades them via chain hydrolysis. In a recent
study, under artificial weather conditions, degradation of PoE
coating was studied at the nanoscale level. Results indicated an
increase in the band formation in gauche conformer as compared
to the trans conformer of PoE, which indicated the photocatalytic
degradation of PoEs in open surfaces.47 During certain photode-
gradation processes, yellowing of the PoE is observed due to
light-induced reactions as a result of the formation of conjugated
alkene48 or quinone derivatives.49,50 A wide range of synthetic
and natural polymers retain UV radiation and go through photo-
lytic, photooxidative and thermo-oxidative responses that lead
to their defragmentation.51
Photodegradation is carried out by the retention of photons.
Various types of electromagnetic radiation can also accelerate
the process of photodegradation. These processes also incorpo-
rate photo-dissociation and atomic separation into smaller units
by the photons.52 UV radiation, however, leads to photo-oxidative
degradation, which causes the separation of the polymer chains,
decreases in atomic weight and changes in mechanical proper-
ties, and leading to a non-usable material.53 The longer time
required for the photodegradative reaction of PoE is one of the
major drawbacks of this process.
Thermal degradation of polyesters
PoEs can be also decomposed by thermal degradation. During
high-temperature treatment PoEs tend to lose their polymeric
nature and original conformation. The depolymerization occurs
by defragmentation of primary chains that gives transitional-
stage, monomer units by an unzipping process. Thus, during this
process, the chemical nature of the substituent is changed,
whereas the structure of the chain remains unaltered.54 During
pyrolytic degradation the depolymerization occurs primarily due
to breakage of the ⊎ hydrogen bond55–57 and secondarily due to
hydrolysis of ⊍ hydrogen bonds. Allyl and diallyl compounds with
J Chem Technol Biotechnol 2022; 97: 359–380

Polyester plastic biodegradation
carboxylic acids and hydrides predominate in PoEs and are prom-
inent products along with aldehydes and hydrocarbons at the
end of the degradation. A known disadvantage of thermal degra-
dation is a requirement for extreme/harsh temperature condi-
tions for complete degradation.58,59 The byproducts or gases
released during thermal degradation of PET include CO, CO2, ben-
zoic acid and benzoic acid derivatives, which can be harmful to
the environment. It has been reported that conventional utiliza-
tion of plastic wastes may enhance net CO2 emissions. Moreover,
a huge amount of ash and slag containing hazardous and toxic
compounds are produced, which can cause other serious environ-
mental problems.8
Hydrolytic degradation of polyesters
Different types of hydrolytically degradable PoEs are preferred to
replace non-hydrolytically degradable petroleum-based PoEs.60
Techniques such as hydrolytic depolymerization are considered
to be very effective for chemical recycling of polymers and recov-
ery of monomers.43,61 It was found that molecular weight
(MW) and crystallinity have a large impact on PoE degradation.
An increase in MW and crystallinity of PoE causes hinderance to
hydrolytic degradation since H2O is not in proximity to the poly-
mer backbone.62–65 When excess of H2O is forced on it leads to
ester hydrolysis and breaks the ester bonds in acidic conditions
that are characteristic of some PoEs like PLA.66,67 For the basic sys-
tems, formation of stable carboxylate anions acts as a driving
force for the hydrolytic degradation. Hence the process of hydro-
lytic degradation of PoE is simple, where, in the first step, uptake
of H2O by the PoE occurs. The second step involves cleavage of
the ester bond and diffusion of the low-MW products out of the
polymer.60,68,69 If it is a large polymer, then the diffusion of degra-
dation product is slow, and the number of end groups increases,
causing autocatalysis and faster degradation of the interior of
the polymer. Thus, though being a simple degradation method,
one of its disadvantages is slow and time-consuming degradation
of large PoEs.
Despite some advantages of non-biological methods, such deg-
radation of PoE plastics is a harsh process consuming much
energy. Furthermore, the radiation used in some non-biological
PoE degradation strategies can be harmful to humans since it
can cause skin burns or skin cancer. Thus environmentally friendly
and cheap alternative solutions are required. Biodegradation
involving natural catalysts such as enzymes are promising ways
to solve this problem. However, some physical pretreatment can
improve enzyme access and the biodegradation process.
CHARACTERIZATION OF LIPOLYTIC
ENZYMES INVOLVED IN POLYESTER
BIODEGRADATION
Enzymatic breakdown of PoEs is a rather green and promising
approach that can be used to convert plastic wastes. The advan-
tages of enzymatic biodegradation over conventional PoE degra-
dation methods include low energy consumption, mild reaction
conditions and environmentally friendly enzymatic repolymeriza-
tion of the resultant monomers.70 All of the PoEs polymers are
made of monomers that are linked into chains by ester bonds that
are the target of hydrolysis for some carboxyl ester hydrolases
such as lipolytic and lipase-/cutinase-like enzymes.
The natural function of esterases and lipases is the hydrolysis of
lipids. Usually, esterases hydrolyze short-chain (C < 10) water-
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soluble acyl esters, whereas lipases prefer long-chain (C > 10)
water-insoluble acyl esters. Cutinases naturally function as cutin-
degrading enzymes and are classified as an intermediate group
of lipolytic enzymes active usually towards short-to-medium-
chain (C2–C12) acyl esters.71,72 Nevertheless, lipolytic enzymes
are often described as rather promiscuous and versatile towards
substrates they can hydrolyze, and PoEs are discovered as one
of the suitable substrates for these enzymes.73 Moreover, some
recently discovered cutinase-like enzymes with unique prefer-
ence towards catalysis of aromatic polyester PET were placed in
a new family/group of enzymes called PETases.72 Some other
groups of carboxyl ester hydrolases that are proposed as indepen-
dent groups of PoE-degrading polyesterases are PHA depoly-
merases, which are recognized as enzymes specific for PHB and
PHBV hydrolysis,74 PBS-, PCL- and PLA-specific (lipase- or
protease-type) depolymerases and polyurethanases (PUases).75
All these lipolytic and lipase/cutinase-like enzymes have many
common features.
Common structural features of polyesterases
Despite little amino acid (aa) sequence similarity and different
molecular weights, the absolute majority of lipolytic enzymes
tested for PoE degradation, as well as PETases and PHA depoly-
merases, belong to a large structurally similar but functionally
diverse ⊍/⊎-hydrolase superfamily.37,76–79 All described polyes-
terases have the same catalytic Ser-Asp/Glu-His triad (Table 1),
which is typical for all the serine hydrolases; therefore all PoE-
degrading lipolytic enzymes and other similar polyesterases cata-
lyze PoE ester bond hydrolysis via the same mechanisms. Catalytic
nucleophilic Ser (nSer) is located in a highly conservative Gly-X-
Ser-X-Gly (where X is any aa) motif in the active center. The con-
servative motif makes up a distinctive structural element known
as a nucleophilic elbow.80 The ⊍/⊎-hydrolase fold is characterized
by a remarkable plasticity ensuring multifunctionality of the
superfamily enzymes, including lipolytic and lipase-/cutinase-like
enzymes, and their versatility towards different substrates.79
PoE-degrading lipases and esterases additionally to the main
⊍/⊎-hydrolase fold core domain have an adjacently located lid
domain that covers the active site. The lid domain has an essential
function during catalysis: it binds to the hydrophobic substrates,
including PoEs, and promotes catalysis by opening the active site,
consisting of a highly hydrophobic substrate-binding groove (SBG)
(also called channel, pocket, cleft) and, most importantly, the cata-
lytic triad. The lid domain of lipases and esterases can have differ-
ent complexities: from small structural elements made of two aa to
complex two to five amphiphilic ⊍-helices covering the active
site.70,81,82 After determination of crystal structures of some cuti-
nases and PETases, it was revealed that in their molecular struc-
tures the lid domain is absent (Table 1), with the single exception
of the mesophilic fungus Trichoderma reesei cutinase-like enzyme
having a lid made of N-terminal ⊍-helices.72 Notably, differences
detected in the structure of lid domains of lipolytic enzymes can
determine the substrate preferences of the enzymes.83
Another important structural feature leading to catalytic effi-
ciency is a common structure called the oxyanion hole (OxH).
OxH stabilizes the PoE hydrolysis reaction intermediate promot-
ing PoE hydrolysis.37 Stabilization is ensured by hydrogen bond-
ing between the oxygen of the carbonyl group of PoE and
enzymes' main chain amides belonging to variable aa forming
OxH. PoE-degrading lipolytic enzymes can have different OxH sig-
natures that can be critical to the PoE-degrading enzymes' sub-
361
strate specificity.84,85
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Table 1. Distinctive structural features of lipolytic and lipase-cutinase-like enzymes involved in degradation of different PoEs

PoE-degrading
enzymes:
important Esterases
characteristics Lipases (EC 3.1.1.3) (EC 3.1.1.1) Cutinases (EC 3.1.1.74) PETases (EC 3.1.1.101) PHA depolymerases (EC 3.1.1.75, EC 3.1.1.76) References

Superfamily ⊍/⊎-Hydrolases ⊍/⊎-Hydrolases; ⊍/⊎-Hydrolases ⊍/⊎-Hydrolases ⊍/⊎-Hydrolases 28, 71, 72, 75, 76, 83,
⊎-lactamase-like 87, 94–97
fold enzymes
www.soci.org

Lid-domain Present Present No lida No lid Present

Catalytic triad Different topologies of Ser-Asp/Glu-His
SBG Usually narrow/deep Usually narrow/ Wide/shallow Wide/shallow Usually narrow/deep
deep
DB − − + + −
Features Lid; hydrophobic Lid; hydrophobic Shallow/wide hydrophobic SBG; neutral Shallow/wide C-terminal substrate-binding domain;
important for active site; SBG and active site; SBG surface charge around active site; open hydrophobic SBG, hydrophobic active site; SBG and its forms;
PoE its forms; unique and its forms; active site; ‘lady-bug’-like enzyme form; W156 wobbling surface loops needed for dimer formation:
degradation Trp residues in the unique Trp thermostability ensured by: Pro important for PET flexibility of these loops can promote PoE

© 2021 Society of Chemical Industry (SCI).

active site residues in the residues; –S–S– bridges; Ca2+/Mg2+ binding; –S–S– binding; unique Trp residues in the active
active site bridges; SBG subsite site
II

Abbreviations: DB, disulfide bridge; SBG, substrate-binding groove.

a
An exception is a cutinase-like enzyme from T. reesei.72

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Polyester plastic biodegradation
Even though all enzymes tested for PoE hydrolysis have the
same catalytic triad determining the mechanism of the catalysis,
the form, depth and surroundings of the catalytic center differ sig-
nificantly.86 The active site of polyesterases is located at the apex
of the central ⊎-sheet within a specific structural pocket, called the
substrate-binding groove (SBG) or site. The edges of the latter
mainly consist of hydrophobic aa residues which upon enzyme-
substrate binding ensure crucial interactions with the hydropho-
bic substrate. SBGs of lipolytic enzymes can vary in their radius,
shape, size, depth and physicochemical properties of the hydro-
phobic interaction region (Table 1), which often ensure different
substrate specificity of different lipolytic enzymes.80 Some PoE
plastics or their various forms, e.g. plastic films, have extremely
low proximity/contact efficacy with enzyme molecules, which
negatively hinders the breakdown process. Polyesterases prefer-
entially attach the amorphous region of the biodegradable
PoE.86 Certain exceptional structural properties (hydrophobic
SBG or ‘crowning area’ around the active site, lid domain) enable
polyesterases to adsorb to the surface of PoEs rather effec-
tively.71,73,86,87 There are also some studies showing less effective
activity towards semicrystalline PoEs as well.88 Various studies
have shown polyesterases to act on PoEs through a random-
chain-scission mechanism, where ester bonds are usually prefer-
entially degraded in endo positions; therefore, PoE-degrading
polyesterases are in most cases endo-type hydrolases.71,89 How-
ever, exo-type cleavage has also been reported.90 The catalytic
hydrolysis mechanism of PoEs corresponds to a classical serine
hydrolase hydrolysis mechanism and has been well discussed
previously.70,72,91–93 Some remarkable specific insights into PCL,
PET and PLA degradation mechanisms have also been presented
in previous studies.28,76,90,91,93 Although the main structural fea-
tures, e.g. core fold, catalytic triad, OxH and catalytic mechanism
of polyesterases, can be rather similar, there are some specific
structural features that are distinct. Such structural differences
can be suggested to explain variations detected in the activities
and catalytic preferences of different polyesterases towards
different PoEs.
Specific structural peculiarities important
for the degradation of polymers
Lipases/esterases
The lid domain that is common to PoE-degrading lipases and
esterases is usually more complex (made of two or more ⊍-heli-
ces); therefore, upon the enzyme's adsorption on PoEs lid opening
can form a large hydrophobic area, ensuring better adsorption
onto hydrophobic PoEs. Highly hydrophobic SBG in lipases/ester-
ases is another prerequisite for the effective biodegradation of
various hydrophobic PoEs.71,72,98 It was shown that Clostridium
botulinum (Cbotu_EstA) truncated esterase, by the introduction
of an exposed hydrophobic patch (absent in the native enzyme),
possessed an enhanced hydrolytic activity towards PoE due to
facilitated enzyme adsorption to the polymer.75 However, a dee-
per and narrow SBG found in lipases and esterases restricts these
enzymes from a more effective degradation of aromatic or ali-
phatic and aromatic co-polyesters. Therefore, microbial lipases
and some esterases usually display low activity towards PET and
other aromatic PoEs due to their lid domain covering the deep-
seated hydrophobic active site.71,99 Fungal and bacterial cutinases
lack the lid and have an exposed catalytic site that is located close
to the protein surface, increasing enzyme accessibility to the PoEs.
Lipases and esterases have been mentioned to modify the
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hydrophobic PET of different crystallinity and in this regard are
proposed to be classified as PET-modifying enzymes.71,100
Cutinases/PETases
Although cutinases as well as other lipases and esterases have
been determined to catalyze the hydrolysis of a broad range of
both emulsified and solid PoEs substrates, such as PLA, PCL, PET,
poly(ethylene adipate) (PEA) and poly(butylene adipate-co-
butylene terephthalate) (PBAT), these enzymes have a higher
potential to degrade the inner PET building block.71 The higher
cutinase activity towards efficient degradation of PET inner ester
bonds can be majorly attributed to the thermal stability of these
enzymes, which are usually isolated from thermophilic microor-
ganisms and used either as indigenous or in recombinant
form.72,101 Thermal stability of PoE-degrading enzymes is favor-
able for PET degradation since this polymer in H2O solutions has
a glass transition temperature (Tg) of 65–70 °C, at which it
becomes more flexible, and becomes sensitive and responsive
to enzymatic biodegradation.72,102 Higher stability of cutinases
favoring activity at high temperatures can be at most attributed
to the disulfide bonds/bridges (DB) that are stabilizing the tertiary
structure of the protein (bacterial cutinases usually have two, and
fungal from two to three DB)37,72 and neutral charge in the crown-
ing area of the active site.73 It was shown that introduction of
additional DB into the structure of Cut190* resulted in remarkably
increased melting temperature (Tm) of the mutant enzyme.103
Besides the overall neutral surface charge around the active site
and characteristic DB, an important mode of cutinase stabilization
can be attributed to divalent metal cations such as Ca2+ and Mg2
+ 71
. Some cutinases (Thermobifida alba cutinase Est119/Ta-cut)
can have multiple (up to four) Ca2+-binding sites; upon binding,
these divalent ions stabilize the loop structures of the enzyme.87
It was shown that activity and thermostability of cutinases can
increase with the increase of Ca2+ in the reaction media,92,104,105
and some cutinases (Cut190) are even inactive without Ca2+.71
Proline residues in the loop regions carrying catalytic aa have also
been detected as important determinants of the thermal stability
of some cutinases.106,107 Additionally, the unique resemblance of
T. alba Est119 cutinase, which is similar to a ‘lady beetle’, where
the active site groove is located ‘at the tip of the belly-like side just
like a head’, may be favorable for adhering to the PLA polymer
film surface.87 Some studies have also shown that the change in
charged surface aa of some cutinases to neutral can enhance their
activity towards some PoEs. Therefore, the reason for different
hydrolytic activities of cutinases towards PoEs can be partially
explained by their distinctive electrostatic and hydrophobic sur-
face characteristics as well.72 Furthermore, by investigating struc-
tural and biochemical features of Aspergillus oryzae (CutL1) and
Fusarium solani (FsC) cutinases having similar fold, it was revealed
that CutL1 enhanced the thermostability, and remarkable activity
towards PCL degradation was favored not only because of an
additional DB in the structure, but also because of a topologically
more favored catalytic triad with a continuous and deep
groove.75,108 Therefore, the difference in various cutinases that
are active towards a specific PoE (PLA, PET or PCL) can be attrib-
uted to individual structural peculiarities of the enzymes. Such
insights into the structural characteristics of cutinases can be used
as targets for re-engineering of these highly promising enzymes
with improved function and stability for a wide range of PoE
biodegradations.
A breakthrough in PET degradation was made a few years ago
363
following the discovery of PETase enzymes. The first PETase was
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reported in Ideonella sakaiensis 201-F6 and was isolated from a
plastic-bottle recycling factory in Japan.109 It is now proposed that
PETase is a member of the cutinase group (∼50% aa identity with
Thermobifida fusca TfCut2, Saccharomonospora viridis SvCut and
T. alba TaCut cutinases),76 which is not fully evolutionarily opti-
mized for PET degradation.110 PET hydrolases (cutinases and
cutinase-like PETases) must possess thermal stability, a wide/shal-
low open active site accessible to the solvent and a hydrophobic
SBG of the active site that can accommodate bulky aromatic moi-
eties of the polymer.71,76 However, I. sakaiensis PETase, which has
been proposed as a unique enzyme in its ability to catalyze the
hydrolysis of recalcitrant PET (1.9% degraded crystallinity
PET),109 has been shown to be less active than some cutinases
(Cut190*, LC-cutinase (LCC)), which are able to degrade more
effectively inner blocks of PET having higher crystallinity.71,111
On the other hand, Joo et al.76 have determined that I. sakaiensis
PETase can be more active towards PET in comparison to Tfcut2
cutinase due to higher stability conditioned by higher number
of DB and differences in the form SBG subsite II, resulting in better
accommodation of the appropriate substrate.76 Furthermore, a
phenomenon known as ‘W156 wobbling’ (W156 is a highly con-
served Trp156 aa residue found across all homologous enzymes)
has been attributed uniquely to PETases. The W156 wobbling/
rotation/flexibility phenomenon in PETases was determined to
be promoted by Ser185, which is replaced by His in other homol-
ogous enzymes. Thus W156 wobbling is stated to be crucial for
substrate binding and product release.112 PETases and cutinases
are now one of the most extensively studied polyesterases for
understanding their activity mechanisms and enhancing their
capability towards recalcitrant and extensively used PoE
PET.76,110,112–119
PHA depolymerases and other polyesterases
PHB and PHBV depolymerases are recognized as enzymes specific
for PHB and PHBV hydrolysis that have the same catalytic triad, lid
domain and hydrolysis mechanism as all serine hydrolases,
including lipolytic enzymes and closely related cutinase-like
PETases.78,86,120,121 Generally, PHA depolymerases consist of three
domains: (i) a catalytic domain consisting of a catalytic triad; (ii) a
linking domain between the catalytic domain and the C-terminal
domain; and most importantly (iii) a C-terminal PHA-binding
domain.75 Analysis of the crystal structures of PHB depolymerases
revealed the presence of conserved Trp aa residues in their active
sites, which were determined to be important for PoE bind-
ing.70,122 However, the specific mechanism of PoE binding medi-
ated by these Trp residues in PHB hydrolysis has not yet been
demonstrated. The same Trp residues were detected in the active
sites of homologous PLA-hydrolyzing enzymes. Interestingly,
Hajighasemi et al.70 reported that such Trp residues were not
found in carboxylesterases and lipases that are not able to
degrade PLA. These findings suggest that Trp residues are
important for the PoE substrate coordination in the active site
and subsequent hydrolysis, at least in PHB depolymerases and
some PLA-degrading enzymes. Similarly positioned Trp residues
in the active sites of carboxyl ester hydrolases might indicate that
the enzyme has the potential for hydrolytic activity against PoEs.70
Since there is no other experiment-based clarification of the func-
tion of these conserved Trp residues in polyesterases, their role in
the hydrolysis of PoEs is to be investigated and verified.
Furthermore, carboxyl esterases such as aryl and sterol esterases
(EC 3.1.1.2 and EC 3.1.1.13, respectively) were also tested for the
364
PoE degradation. Aryl esterases have been shown to break down
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A Gricajeva, AK Nadda, R Gudiukaite
PBAT.71 Sterol esterases have been studied for the surface modifi-
cation of PET polyester to improve its characteristics favorable in
the textile industry.123 Therefore, exploration of different carboxyl
esterases can lead to the discovery of novel, unexplored and
effective polyesterases belonging to different types of carboxyl
esterase (EC 3.1.1.–) subclass.
Lipases, esterases, cutinases, PETases and PHA-depolymerases
are all important candidates representing a solution for effective
biological breakdown of different types of PoE. All discussed poly-
esterases can play a major role in biotransformation of PoEs. Gen-
erally, lipolytic enzymes, especially lipases and esterases, are more
active towards aliphatic PoE plastics. The most promising
enzymes for achieving progress in the most recalcitrant (aro-
matic/aliphatic–aromatic copolymer) PoE plastic biodegradation
are cutinases. The management of PoE plastics via lipolytic and
lipase-/cutinase-like enzymes will be comprehensively discussed
in the next section.
MANAGEMENT OF POLYESTER PLASTICS
USING POLYESTERASES
The most important factors that affect plastic biodegradation can
be: (i) the nature of the plastic–polyester (molecular weight, sur-
face area, chemical structure, availability of hydrolysable ester
bonds in the polymer chain, degree of polymer crystallinity, ste-
reoregularity, Tm, Tg and the complexity of the polymer formula);
(ii) the environment in which the polymers are placed or disposed
(pH, temperature, moisture and oxygen content).2,6–8,75,98,124–127
The high Tm, Tg and percentage crystallinity of many PoE plas-
tics128 are major limiting factors for effective biodegradation.
However, some lipolytic enzymes can modify the structure and
surface of PoEs (e.g. PET) and increase their hydrophilicity, avoid-
ing harsh chemicals and reducing energy consumption.72 The
most important studies regarding the biodegradation of PoEs
with lipases, esterases, cutinases, PETases and PHA depoly-
merases will be discussed in the following sections and are pre-
sented in Tables 2–5. Figure 1 summarizes the main products
obtained after enzymatic hydrolysis of different PoEs.
Enzymatic degradation of PET
PET is a linear polymer of ester-linked terephthalic acid (TPA) and
ethylene glycol (EG).129 It is the most popular plastic used around
the world because of its malleability, transparency and resistance
to natural degradation. When PET is hydrolyzed it produces bis
(2-hyroxyethyl) terephthalate (BHET), mono(2-hydroxyethyl) tere-
phthalate (MHET) and TPA monomers (Fig. 1). Microbial PETases
and cutinases in particular possess a remarkable capability to hydro-
lyze PET to its monomeric units. Müller et al.130 reported that
cutinase from T. fusca DSM 43793 was able to degrade aliphatic–
aromatic copolyesters and PET sheets. Several researchers have dis-
cussed applications of microbial cutinases19,131-142 and lipases143 to
PET fibers, oligomer decomposition and surface modification. It was
proposed that cutinases from T. fusca and F. solani pisi and lipase
from Thermomyces lanuginosus (Novozymes, Bagsværd, Denmark)
showed activity on PoE poly(trimethylene terephthalate) (PTT).143
The cutinase from T. fusca was found to release higher amounts of
hydrolysis products from PTT materials and was able to open and
hydrolyze a cyclic PTT dimer.143 Many studies have also indicated
that carboxylesterase from T. fusca KW3 can be active towards PET
and its derivatives.22,144–147 Thermobifida alba AHK119 possess the
ability to significantly hydrolyze aliphatic–aromatic copolyester film
through esterase activity.148 Several years later a new LC-cutinase
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Table 2. Biotransformation of PET using microbial lipolytic and lipase-/cutinase-like enzymes

Biocatalyst Findings of the study References

T. fusca KW3 carboxylesterase (TfCa)
Cutinase from T. alba (Tha_Cut1)
I. sakaiensis PETase
Carboxylesterase from T. fusca KW3
Cutinases from T. cellulosilytica DSM44535
(Thc_Cut1 and Thc_Cut2) and T. fusca
DSM44342 (Thf42_Cut1)
Carboxylesterase TfCa from T. fusca KW3, TfCut2
from T. fusca KW3 and LC-cutinase
16 commercial lipases and cutinases
CALB and H. insolens cutinase (HiC)
Four different cutinase variants from T.
cellulosilytica
PETase (BhrPETase) from bacterium HR29
p-Nitrobenzylesterase from Bacillus subtilis
Esterase from Thermobifida halotolerans
Putative polyester hydrolases Tcur1278 and
Tcur0390
Cutinase (Cut190) from S. viridis AHK190
Fusarium oxysporum recombinant cutinase
FoCut5a
Cutinase from F. oxysporum
T. cellulosilytica cutinase (Thc Cut1)
H. insolens cutinase (HiC)
Sub1, a suberinase encoded by Streptomyces
scabies
Release of 7 nmol TPA acid mL−1 by TfCa (0.01 mg mL−1) 22
PET surface-modifying hydrolysis leading to considerable improvement 23
in hydrophilicity
Effective conversion of PET to its monomers: TPA and EG 109
Hydrolysis of highly hydrophobic, synthetic cyclic PET trimers 146
Release of MHET, TPA and bis(benzoyloxyethyl) terephthalate (3PET) 147
Dual enzyme system (TfCa2 + LC-cutinase) produced a 2.4-fold higher 151
amount of degradation products compared to TfCut2 individual
enzyme
The most promising result was shown by H. insolens cutinase used solely 153
or in combination with C. antarctica lipase
HiC: limited last reaction step; CALB: complete conversion of BHET to 154
TPA, even at the highest substrate concentration investigated
(31 mmol L−1)
Hydrolysis of HMLS-PET cords, creating new carboxylic and hydroxyl 157
groups with distinct exo-/endo-wise selectivity
Breakdown of amorphous PET 158
During PET hydrolysis TPA, benzoic acid (BA), 2-hydroxyethyl benzoate 159
(HEB) and MHET were released
Hydrolysis of model substrate 3PET releasing TPA and MHET. No higher 160
oligomers like bis-(2-hydroxyethyl) terephthalate were detected
Tcur1278: superior thermal stability and high hydrolytic activity on PET. 161
Tcur0390: higher hydrolytic activity against PCL and PET nanoparticles
compared to Tcur1278
Efficient hydrolysis of various aliphatic and aliphatic-co-aromatic PoE 36, 37, 152, 162
films
Hydrolysis of PET model substrates and synthetic polymers 163
Modification of PET made textile surface without compromising 164
polymer's bulk properties, such as strength
Selective hydrolysis of PET moieties in packaging and bottles made of 20, 156, 165
PET and polyethylene (PE) or polyamide (PA) blends releasing TPA and
MHET
Hydrolysis yielded in 97% of pure TPA comparable with the commercial 166
synthesis-grade TPA (98%)
Release of TPA. Enhancing of Sub1 activity on PET and stability at 37 °C 167
for at least 20 days after addition of Triton

Studies covering the last decade are presented.

Abbreviations: 3PET, bis(benzoyloxyethyl) terephthalate; EG, ethylene glycol; HMLS-PET, high-modulus and low-shrinkage PET; MHET, mono(2-hydro-
xyethyl) terephthalate; TPA, terephthalic acid.

(LCC) was successfully isolated from a leaf–branch compost metage-
nomic library.149 LCC had the highest aa sequence identity (59.7%)
to Thermomonospora curvata lipase and has been studied exten-
sively as a promising biocatalyst for biodegradation of PET.149-151
The S. viridis AHK190 cutinase-like enzyme Cut190 was also charac-
terized as a PET-degrading enzyme with the potential for industrial
application in PoE degradation, monomer recycling and PET surface
modification.36,37,152 Several other studies suggested a cocktail
composed of microbial cutinase and lipase for more effective PET
degradation.153,154 Carniel et al.154 demonstrated remarkable syn-
ergy of C. antarctica lipase B (CALB) and Humicola insolens cutinase
(HiC) towards PET and its derivatives. The use of protein cocktails
composed of several different lipolytic enzymes can help to avoid
as MHET.151,155 In a dual enzymatic system based on TfCut2 and
LCC cutinases and carboxylesterase TfCa from T. fusca KW3, more
efficient degradation of PET films was also demonstrated.151 The
combination of TfCa and LCC or TfCut2 cutinases yielded a 104%
and 91% increase in the total amounts of products, respectively,
compared to enzymatic hydrolysis of PET films without addition of
TfCa.151 The promising results in PET moiety degradation was
shown also by Thermobifida cellulosilytica cutinase (Thc Cut1), which
acted on PET blended with PE or PA from packaging and bottles
without prior separation.156 Thc Cut1 cutinase selectively hydro-
lyzed PET moieties, releasing TPA and MHET.156 Vecchiato et al.157
analyzed four different T. cellulosilytica cutinase variants and dem-
onstrated their ability to hydrolyze HMLS-PET (high-modulus and
365

biodegradation inhibition by intermediate reaction products such low-shrinkage PET) cords, creating new carboxylic and hydroxyl

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Table 3. Biotransformation of PCL using microbial lipolytic enzymes

Biocatalyst Findings of the study References

Lipase from C. antarctica and cutinase from F. solani
F. solani and A. fumigatus cutinases
Cutinases from A. brassicicola (AbC), A. fumigatus
(AfC), A. oryzae (AoC), H. insolens (HiC) and F. solani
(FsC)
Extracellular cutinase of P. japonica Y7-09
Bacillus sp. KY0701 cutinase
Cutinase from M. thermophila
Lipase from P. cepacia and T. cellulosilytica cutinase
Thc_Cut1
Thermophilic esterase from the archaeon
Archaeoglobus fulgidus (AfEST)
Lipase-derived from probiotic Lactobacillus
plantarum
Novozyme®435 and Amano lipase PS
B. subtilis lipase (BSL), Burkholderia sp. lipase (BCL) and
Ophiostoma piceae sterol esterase (OPE)
Greater mass loss in PCL films by lipase rather than cutinase at the same 28
enzyme concentrations was achieved. Degradation mode of PCL films:
layered for cutinase and penetrated for lipase-catalyzed degradation
F. solani cutinase: PCL degradation and synthesis of polymer with a molecular 34
weight (MW) of 2300. A. fumigatus cutinase: complete degradation of PCL
and synthesis of molecules with a MW of 25 000
Highest activity by HiC cutinase was demonstrated/determined 73
93.33% degradation of PCL film after 15 days of incubation, 43.2% foam 174
plastic degradation after 30 days of incubation
Weight loss of PCL films in minimal salt medium 175
78.5% of PCL weight loss in 36 h. PVAc degradation 176
Lipase-catalyzed significant surface erosion and increase in crystallinity using 177
highest PEG amount. Thc_Cut1-catalyzed significant decrease in MW,
increase in dispersity and release of ε-caprolactone monomer units after
6 h incubation with PCL
Enzyme resistance to temperatures above glass transition of the plastic. 178
Achievement of thermal decomposition temperature decrease that is 179
needed for complete mass loss from 460 to 395° C
Higher Novozyme® 435 activity 180
Initiation reaction rates by BSL and BCL were determined to be 57 and 181
80 μg min−1 U−1, respectively. Low OPE activity towards PCL and high
activity towards PVAc

Studies covering the last decade are presented.

Abbreviations: PEG, polyethylene glycol; PVAc, polyvinyl acetate.

groups with distinct exo- and endo-wise selectivity.157 The newest
enzyme with promising activities towards PET was reported to be a
PETase (BhrPETase) from bacterium HR29. BhrPETase showed high
homology to LCC cutinase.158 Kawai et al.71 successfully summa-
rized the carboxyl ester hydrolases involved in PET management.
The authors indicated that hydrolases that led to successful PET
inner bond hydrolysis were cutinases, esterases and lipases capa-
ble of modifying PET. Recently, Tournier et al.111 demonstrated
LCC cutinase as at least 33 times more efficient for PET degrada-
tion than any other tested enzyme. Engineered enzyme was pre-
sented as suitable to degrade and recycle plastic bottles.
Ultimately, researchers purified TPA monomers, resulting after
breakdown, and used them for the synthesis of PET, which was
used to make bottles,111 which presented a great example of the
circular economy. The most relevant studies of the last decade
regarding PET hydrolysis and modification using lipolytic enzymes
are summarized in Table 2. The research interest towards PET bio-
degradation is resulting in the discovery of new lipolytic enzymes
and PETases suitable for PET management. Nevertheless, the reac-
tion conditions and target lipolytic enzyme characteristics (activity,
thermostability, substrate specificity, etc.) towards PET and other
PoE plastics can be improved in order to achieve more effective
management of the most abundant worldwide polymer.
Biodegradation of PCL and their derivatives
The biodegradation of PCL has been attempted for a long time.
One of the first studies of PCL biodegradation using microbial
366
Pseudomonas aeruginosa lipase can successfully catalyze PCL
hydrolysis, with the formation of dimeric ester of hydroxyhexano-
ate as the main reaction product.168 Further, it was shown that
Candida antarctica169 and Mucor miehei170 lipases can effectively
hydrolyze PCL in toluene at 40–60 °C. Tsuji and Ishizaka171
reported that Rhizopus arrhizus lipase can break down blends of
PCL and poly(L-lactide). Furthermore, it was shown that Pseudo-
monas lipase can degrade different PCL-based block copolymers
composed of PCL and poly(ethylene glycol),172 PCL and various
polylactide-based polymers,173 PCL and poly(p-dioxanone)
(PPDO).89 Baker et al.73 analyzed five cutinases from Alternaria
brassicicola (AbC), Aspergillus fumigatus (AfC), A. oryzae (AoC),
H. insolens (HiC), and F. solani (FsC). The most promising results
for PCL hydrolysis was demonstrated by HiC cutinase. The cuti-
nase from Pseudozyma japonica Y7-09 was successfully applied
to degradation of PCL and foam plastic.174 However, Ping et al.34
suggested that A. fumigatus cutinase showed more promising
results than F. solani cutinase for PCL degradation. The good per-
formance on PCL degradation was demonstrated by Bacillus
sp.,175 Myceliophthora thermophila,176 F. solani cutinases and
C. antarctica lipase.28 Important examples of PCL degradation
using lipolytic enzymes are presented in Table 3. Different scien-
tific data support the ability of various lipolytic enzymes to break
down PCL.
Enzymatic degradation of polyurethanes
PUR are one of the most common classes of polymers and are

polyesterases was conducted by Jaeger et al.168 It was shown that used in the medical, automotive and industrial fields.182 It is a

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Table 4. Biotransformation of PBS and its derivatives using microbial lipolytic enzymes

Polyester Biocatalyst Findings of the study References

PBS and PHBV Aliphatic PoEs cutinase 1
from T. cellulosilytica
(Thc_Cut1) expressed in P.
pastoris
PBS-co-diethylene glycol succinate) (PBS-co- Novozyme 435 (N435) lipase
DEGS) and PBS-co-butylene diglycolic acid)
(PBS-co-BDGA)
PBS-co-cyclohexane dimethanol succinate) (P Novozyme 435 (N435) lipase
(BS-co-CHDMS)) and PBS-co-butanediol
cyclohexanedicarboxylic acid) (P(BS-co-
BCHDA))
PBS, PBSA Lipase from yeast
Cryptococcus sp.
PBS Recombinant cutinase from
F. solani
PBS was blended with cellulose microcrystalline Recombinant F. solani
(CMC), cellulose acetate (CA) and cellulose cutinase
triacetate (CTA)
PBS Recombinant F. solani
cutinase
PBS, PBS-co-1,4-cyclohexane dimethanol) Immobilized Candida lipase
(PBS/CHDM), PBS-co-diglycolic acid (Novozyme 435)
(PBS/DGA)
PBS, PBSA Cutinase-like enzyme PaCLE1
from P. antarctica JCM
10317
PBAT C. botulinum ATCC 3502
esterases (Cbotu_EstA and
Cbotu_EstB)
PBAT Lipase from Pelosinus
fermentans
PBAT H. insolens (HiC) and T.
cellulosilytica (Thc_Cut1)
cutinases
PBAT P. pseudoalcaligenes
arylesterase (PpEst)
PBAT and oligomeric model substrate bis Polyesterase EstB3 and EstC7
[4-(benzoyloxy)butyl] terephthalate from Sphagnum
(BaBTaBBa) magellanicum
Poly(ethylene succinate) (PES), PBS and F. solani cutinase
poly(hexylene succinate) (PHS)
PBS-dilinoleic succinate) (PBS-DLS) copolymers C. antarctica lipase (CALB).
Higher preference towards PHBV 20
Biodegradation of PBS-co-DEGS and PBS-co- 26
BDGA copolymers with different DEG/DGA
content in THF/toluene mixed system in 30 h
Degradation rate of 67% for P(BS-co-CHDMS) 27
Complete degradation of PBS and PBSA films in 214
72 h and 16 h of the reaction, respectively
Complete degradation of PBS films in ∼6 h 216
Weight loss by 85% of PBS/CMC and PBS/CA 217
blends reached in 4 h
The weight loss achieved in the vicinity of 80– 218
90%
A series of low-MW PoEs were obtained 219
Degradation of solid films of PBS, PBSA, PCL and 213, 220,
PLLA. Highest degradation rates of PCL and 221
PBSA were achieved
Considerably higher activity of Cbotu_EstA was 222
demonstrated
Release of small PBAT building blocks 223
Thc_Cut1: more efficient PBAT breakdown, 224
resulting in up to 3-fold higher concentrations
of TPA. HiC: higher overall hydrolytic activity
Activity on both whole and milled PBAT film 225
releasing TPA and
4-(4-hydroxybutoxycarbonyl) benzoic acid
Outstanding activity and a strong preference for 226
PBAT
Biodegradation preference PHS > PBS > PES 227
Approx. 40% mass loss of fibrous materials 228
prepared from the PBS-DLS 70:30 copolymer.

Studies covering the last decade are presented.

Abbreviations: MHET, mono(2-hydroxyethyl) terephthalate; PBAT, poly(butylene adipate-co-butylene terephthalate); PBS, polybutylene succinate;
PBSA, polybutylene succinate–co-adipate; PEG, polyethylene glycol; TPA, terephthalic acid.

polymer of polyisocyanates and polyols that are linked with ure-
thane bonds. PUR is used as foam due to the presence of an isocy-
anate group because, when H2O reacts with the isocyanate group,
CO2 is produced.183 Commonly used polyisocyanates are tolylene
diisocyanate and diphenylmethane diisocyanate, and are based
on the type of polyols used; there are two types of PUR: polyester
and polyether urethane.183 The first detected PUR-degrading
chlororaphis.184–186 The respective genes of these lipases belong
to a large gene cluster, which can be responsible for mechanisms
of carbon catabolite control in Pseudomonas species.187,188 It is
also known that Comamonas acidovorans TB-35 esterase PudA
displayed PUR hydrolysis activity and released diethylene glycol
and adipic acid as biodegradation products.189,190 Bacillus subtilis
polyurethanase-lipase,191 Alicycliphilus sp. esterase,192 Candida
367

enzymes were PueB and PueA lipases from Pseudomonas rugosa lipase193 and CALB194 have been proposed as promising

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Table 5. Biotransformation of PoE plastics using microbial lipolytic enzymes

Polyester Biocatalyst Findings of the study References

Poly(DL-lactideco-glycolide)-block- Lipase from Pseudomonas sp. Immobilized-enzyme reactor capable of degrading 25

poly(ethyleneglycol)- block-poly
(DL-lactide-coglycolide) (PLGA-PEG-
PLGA)
Poly(oxyethylene terephthalate)
(PET-PEO); poly(oxyethylene
terephthalate) (PET-PEO)-based
polymer
Ionic phthalic acid-based PoEs
Poly(1,4-butylene
2,5-thiophenedicarboxylate)
(PBTF) and poly(1,4-butylene
2,5-furandicarboxylate) (PBF)
Poly(ethylene furanoate) (PEF)
PEF
Ionic phthalic acid-based PoEs
Polycarbonate poly(bisphenol-A
carbonate) (BPAPC)
Polyesters of 2,5-furandicarboxylic
acid (FDCA)
Esterase and cutinase from P.
pseudoalcaligenes; lipase from P.
pelagia
Cutinase from P. pseudoalcaligenes
(PpCutA) and a putative lipase
from Pseudomonas pelagia
(PpelaLip)
H. insolens (HiC) and T. cellulosilytica
(Cut) cutinases
Cutinase from T. cellulosilytica
T. cellulosilytica cutinase (Thc Cut1)
and H. insolens (HiC) cutinase
Arylesterase (PpEst) from P.
pseudoalcaligenes
Three different lipases from C.
antarctica (CAL), C. rugosa (CRL)
Cutinase 1 from T. cellulosilytica
(Thc_Cut1)
PLGA-PEG-PLGA nanoparticles within a residence
time of 2 min was analyzed
A slight synergistic effect of a combination of the 29
enzymes in terms of the hydrolysis products, TPA
MHET and bis(2-hydroxyethyl) terephthalate was
achieved
Faster hydrolysis of PoEs containing 1,2-ethanediol 32
rather than 1,8-octanediol.
In 72 h of incubation, weight losses of about 20% 90
have been reached, with PBF to be degraded
slightly faster than PBTF
Release of 2,5-furandicarboxylic acid and oligomers. 238
100% hydrolysis of PEF films was achieved after only 239, 240
72 h incubation with an HiC in 1 mol L−1 KPO
pH 8 at 65 °C
Effective hydrolysis of all 14 synthesized ionic 241
phthalic PoEs as indicated by TPA release
Degradation order of BPAPC in THF: 242
PPL > CAL > CRL, in CHCl3: CRL > CAL > PPL
Hydrolysis of all tested PoEs with preference for PoEs 243
containing 1,5-pentanediol and 1,9-nonanediol.
Enzyme activity increase when the linear diol
1,3-propanediol was replaced by the branched
analog 1,2-propanediol or ethoxy units were
introduced into the PoE chain

Studies covering the last decade are presented.

Abbreviations: MHET, mono(2-hydroxyethyl) terephthalate; PBS, polybutylene succinate; PBSA, polybutylene succinate–co-adipate; PEG, polyethyl-
ene glycol; PoEs, polyesters; TPA, terephthalic acid.

lipolytic enzymes in PUR biotransformation. During the last
decade, several reports suggested degradation of PUR by ester-
ases/lipases which were proposed to be named PUases.195 It
was also reported that the above-mentioned LCC, TfCut2,
Tcur1278 and Tcur0390 cutinases showed great potential not only
towards PET degradation but also displayed the ability to degrade
PUR.196 The observation that cutinases can be involved in decom-
position of several PoEs could be attributed to the promiscuous
nature of these enzymes.129 It was concluded that lipolytic
enzymes such as esterases or cutinases are versatile biocatalysts
and display a broad substrate preference.129,197 Islam et al.198
reported the fusion of the anchor peptide Tachystatin A2 to the
bacterial cutinase Tcur1278, which accelerated the degradation
of polyester–polyurethane nanoparticles. It is important to note
that despite biodegradation availability of polyester PUR the
decomposition of polyether PUR remains a major challenge in
the 21st century.
Enzymatic degradation of PHA and its derivates
PHA are biodegradable PoEs that are synthesized and accumulated
intracellularly during unbalanced growth by a large variety of bacte-
368
the most common type of PHA. The ability of lipolytic enzymes
(lipases, carboxylesterases) to perform PHB biodegradation has
been reported. Jaeger et al.168 analyzed the PoE substrate specific-
ities of extracellular lipases purified from B. subtilis, P. aeruginosa,
Pseudomonas alcaligenes, Pseudomonas fluorescens, Pseudomonas
cepacia, extracellular PHA depolymerases produced by Comamonas
sp., Pseudomonas lemoignei, P. fluorescens GK13 and esterase puri-
fied from P. fluorescens GK13. Most of the studied polyesterases
had preferences towards PoEs made of ω-hydroxyalkanoic acids
such as poly(6-hydroxyhexanoate) or poly(4-hydroxybutyrate).168
However, in most cases PHA biodegradation is performed by PHA
depolymerases, which convert the PHA into water-soluble oligo-
mers and monomers.199 Other prominent microorganisms in which
PHB depolymerase has been identified are Rhodospirillum rubrum,
Bacillus megaterium, Acinetobacter beijerinckii and P. lemoignei.200
The purified fungal PHB depolymerases have been summarized
by Kim and Rhee201 and a PHA depolymerase engineering database
has been created.121 The promising results for PHA degradation
demonstrated PHA depolymerase from the Thermobifida
sp. BCC23166202 and Streptomyces roseolus SL3 depolymerase,
which hydrolyzed mcl-PHA and PCL, but not scl-PHA, PES or

ria.168 The poly-3-hydroxybutyrate (P3HB) form of PHB is probably PLA.31 The activity of several commercial lipases203,204 and

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Polyester plastic biodegradation
Figure 1. The main hydrolysis products obtained after polyester hydrolysis by microbial lipolytic enzymes.
Figure 2. The principle of (a) protein engineering and (b) immobilization
to improve the ability of target lipolytic enzymes to degrade polyester
plastics.
B. subtilis DI2 lipase205 on PHA has also been proposed. After DI2
lipase treatment, 21.3% and 28.3% MW decrease and weight loss
of PHA, respectively, have been detected.205 The ability of Geobacil-
lus sp. T1 lipase to degrade amorphous P(3HB) has also been sug-
gested.206 Thus examples presented in this section showed that
the new screening and fundamental research analysis of known
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microbial lipolytic enzymes on PoE decomposition can be an objec-
tive for recent and future studies useful for plastic biodegradation.
Enzymatic degradation of succinate polyesters and their
derivatives
The PBS backbone is flexible and contains readily hydrolysable ester
bonds, which are prone to catalytic degradation by microorganisms
or enzymes. It was observed that P. cepacia lipase can hydrolyze
poly(butylene succinate-co-terephthalate) (PBST).207 Hoshino and
Isono208 tested commercial lipases for their degradation efficiency
of aliphatic PoE films. The authors presented that lipase derived from
Chromobacterium viscosum degraded polybutylene succinate-co-
adipate (PBSA), PCL and PBS; however, lipase F (Rhizopus niveus)
degraded PBSA and PCL in 4–17 days. Another study indicated that
Acidovorax delafieldii strain BS-3 with high lipolytic activity could
break down poly(tetramethylene succinate)-co-(tetramethylene
adipate),209 Rhizomucor miehei lipase catalyzed transformation of
poly(butylene adipate) and PBS into repolymerizable cyclic
oligomers,210 C. antartica lipase (Novozyme 435) towards
poly(butylene succinate-cocyclic carbonate) P(BS-co-CC)s and their
derivative with different carbonate building blocks.211 Next,
R. miehei and P. cepacia lipases were detected to be active against
poly(butylene-co-propylene succinate) copolymers.212 It was found
that cutinase-like enzyme PaCLE1 from Pseudozyma antarctica
JCM10317 can degrade PBSA, PCL and PLA,213 and Cryptococcus
sp.214 and P. aeruginosa lipases215 were able to hydrolyze PBSA. PBS
biodegradation ability was also shown by T. cellulosilytica cutinase20
and recombinant F. solani cutinase.216–218 The most representative
studies from the last decade related to PBS and biodegradation of
its derivatives are summarized in Table 4.
Biodegradation of PLA
PLA, as a biodegradable thermoplastic PoE, is receiving increasing
attention. It was observed that Cryptococcus sp. S-2 lipase exhib-
369
ited homology to enzymes from the cutinase family and
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Table 6. Examples of improvement of PoE-degrading biocatalysts via different protein engineering strategies

Enzyme involved in Protein

polyester engineering Important features determined
Polyester degradation Modification strategy during the study Reference

PET S. viridis AHK190 S226P/R228S Site-directed Substitution of S226P and R228S 36

cutinase Cut190 mutagenesis resulted in achievement of
highest activity and
thermostability. Cut190 (S226P/
R228S) efficiently hydrolyzed
various aliphatic and aliphatic-
co-aromatic PoE films
PET and PBSA Cut190 from S. viridis Q138A/D250C-E296C/Q123H/ Site-directed Replacement of surface Asn and 103
AHK190 (Cut190) N202H; G62A/H129W, G62A/ mutagenesis Gln with Asp, Glu or His
F209S, G62A/F209A, 129 W/ increased Tm. A combined
F209S, H129W/F209A; H129A mutation, Q138A/D250C-
E296C/Q123H/N202H, resulted
in the highest thermostability,
leading to maximum
degradation of PET film
Aliphatic co- aromatic Cutinase type Val, Pro and Lys were introduced Site-directed Est1 (A68V/T253P) degraded 107
PoEs, polyesterases from at A68, T253 and M256, mutagenesis various aliphatic and aliphatic
hydrophilized an T. alba AHK119 respectively co-aromatic PoE and
amorphous PET hydrophilized an amorphous
film PET film
PET Leaf–branch 15 aa residues in the first contact Site-specific Improved enzyme-catalyzed PET 111
compost cutinase shell, of which 11 were defined saturation depolymerization to 90%
(LCC) as targets for mutagenesis mutagenesis conversion in less than 10 h.
Resulting purified TPA
monomers were used to
synthesize PET
PET I. sakaiensis PETase S131A; D177A; H208A; W130A; Site-directed Catalytic aa, substrate binding 114
W130H; M132A; W156A; A180I; mutagenesis channel and aa affecting
Q90A; S185H; S209F; W68L; hydrophobic property of the
Q153L; R94A; N212A enzyme have been identified
PET, polyamides Cutinase from F. Mutations L81A, N84A, L182A, Site-directed L81A and L182A showed an 136
solani pisi V184A and L189A mutagenesis activity increase of 4- and 5-fold
for PET fibers. L182A showed 1-
and 2-fold higher ability to
biodegrade aliphatic polyamide
substrates
PET T. fusca Tfu_0883 I218A, the double mutation Site-directed Both single and double mutants 245
cutinase Q132A/T101A mutagenesis exhibited considerably higher
hydrolysis efficiency on PET
PET Cutinase from F. Cutinase C-terminal fused to Fusion to binding Enzymatic treatment of PET by 246
solani pisi cellulose binding domain N1 domains cutinases during 48 h
from Cellulomonas fimi. decreased the mass of PET
PET Thermomyces Binding of modules from Fusion to binding Fusion enzymes were active both 247
cellullosylitica cellobiohydrolase I from domains on the insoluble PET model
(Thc_Cut1) Hypocrea jecorina (CBM) and substrate bis(benzoyloxyethyl)
cutinase from a PHA depolymerase from terephthalate (3PET) and on PET
A. faecalis (PBM).
PET T. fusca cutinase– Replacing each of W14, W50 and Site-directed W68L and W68Y, among all the 248
CBM fusion W68 with leucine or tyrosine mutagenesis mutants, exhibited significant
protein improvement in binding and
catalytic efficiency (1.4- to
1.5-fold) towards PET fiber
PET Cutinases Thc_Cut1 Double mutant R29N and A30V; Site-directed Exchange of positively charged 249
and Thc_Cut2 triple mutant R19S, R29N, and mutagenesis arginine (R19 and R29) located
from T. A30V; mutants of Thc_Cut2 on the enzyme surface to the
370

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Polyester plastic biodegradation www.soci.org

Table 6. Continued

Enzyme involved in Protein

polyester engineering Important features determined
Polyester degradation Modification strategy during the study Reference

cellulosilytica R19S, R29N, A30V, Q65E, non-charged aa serine and

DSM44535 L183A, R187K asparagine strongly increased
hydrolysis activity for 3PET and
PET
Poly(1,4-butylene T. cellulosilytica Cutinase 1 (Thc_Cut1) was fused Fusion to binding Hydrolysis rates of PBA were 250
adipate) (PBA) cutinase 1 to a polymer binding module domains significantly enhanced when
(Thc_Cut1 (PBM) incubated with the active,
engineered Thc_Cut1_PBM as
compared to the native
Thc_Cut1
PET T. cellulosilytica Fusion to one of three Fusion to binding After enzyme fusion to HFB4 or 251
(Thc_Cut1) Trichoderma hydrophobins, domains HFB7, the hydrolysis of PET was
cutinase HFB4, HFB7 and HFB9b enhanced >16-fold compared
to free enzyme
PBSA A. oryzae cutinase E31S/D142S/D171S Site-directed Positively charged residues (H32, 252
CutL1 mutagenesis K34) of RolA hydrophobins and
negatively charged residues
(E31, D142, D171) of CutL1 are
important for cooperative ion
interaction between RolA and
CutL1
PET T. fusca KW3 and LC- G62A and the double variant Site-directed Enzyme variants with increased 253
cutinase (LCC) G62A/I213S mutagenesis PET hydrolytic activity at 65 °C
were obtained. The single
mutant G62A and double
variant G62A/I213S caused a
weight loss of PET films of more
than 42% after 50 h of
hydrolysis
PBAT C. botulinum esterase D130L, H150F, H156F, and D302L, Site-directed All four variants of the zinc 254
(Cbotu_EstA) F154Y and W274H mutagenesis coordination site (D130L,
H150F, H156F, and D302L)
showed a loss of
thermostability. Variants
carrying mutations of aa in the
zinc-binding domain were able
to release up to 10 times more
soluble products from the
polymeric substrate PBAT
PBAT Esterase from C. Removing 71 residues at the N- Enzyme truncation Increased activity was observed in 255
botulinum terminus resulting in del71Cbotu_EstA variant, which
(Cbotu_EstA) del71Cbotu_EstA variant broke down PET, which was not
hydrolyzed by the wild-type
enzyme Cbotu_EstA
PBSA A. oryzae cutinase D30S, quadruple mutant D30S/ Site-directed D30 is involved in the CutL1–RolA 256
CutL1 E31S/D142S/D171S mutagenesis (cutinase–hydrophobin)
interaction.
PLLA T. cellulosilytica Thc_Cut2_DM (Thc_Cut2_ Site-directed The four enzymes showed 257
Thc_Cut1 and R29N_A30V) and Thc_Cut2_TM mutagenesis different activities towards
Thc_Cut2 (Thc_Cut2_R19S_R29N_A30V). aliphatic PLLA
cutinases
PET Esterase Zinc-binding domain was Site-directed A combination of substitution of 258
(Cbotu_EstA) from subjected to site-directed mutagenesis; residues present in the zinc-
C. botulinum mutagenesis. On the other enzyme binding domain (e.g. S199A)
hand, a specific domain truncation and truncation of 71 aa at the N-
371

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Table 6. Continued

Enzyme involved in Protein

polyester engineering Important features determined
Polyester degradation Modification strategy during the study Reference

consisting of 71 aa at the N- terminus of the enzyme

terminus of the enzyme was synergistically increased the
deleted activity of the enzyme on PET
7-fold
PET Thermobifida fusca G62A/F209A; G62(A89); H129 Site-directed Replacing F209S and F209A 259
(TfCut2) (W159); F209(S238) mutagenesis greatly improved catalytic
activity
PET Polyester hydrolase S171A, D217A, H249A, G254S, Site-directed PE-H (Y250S) variant showed 260
from Pseudomonas S256N, I257S, Y258N, N259Q, mutagenesis improved activity towards PET.
aestusnigri Y250S, Q294A, I219Y
VGXO14T.
PCL Lipase and cutinase Construction of a bifunctional End-to-end fusion Lip-Cut displayed more efficient 261
genes from Lip-Cut enzyme. PCL degradation capability.
Thermomyces Weight loss of PCL film by Lip-
lanuginosus and Cut after 6 h was 13.3, 11.8 and
Thielavia terrestris, 5.7 times higher than that by
respectively Lip, Cut and Lip/Cut mixture,
respectively
PET I. sakaiensis PETase Y87F, T88L, R90S, I208V, I208T, Rational design for IsPETaseS242T and 262
G234N, S238T, S242T, N246D. optimization of IsPETaseN246D possessed
substrate higher enzymatic activity;
binding site; IsPETase S121E/D186H/S242T/
site-directed N246D maintained PET
mutagenesis degradation activity for 20 days,
and unlike wild type lost its
activity within a day
PET I. sakaiensis PETase R280A S121E D186H N233C Site-directed Mutations improved catalytic 263
S282C mutagenesis rates 5- to 7-fold

effectively degraded high-molecular-weight PLA, as well as other
biodegradable plastics, including PBS, PCL and PHB.229 Akutsu-
Shigeno et al.230 cloned poly(DL-lactic acid) depolymerase (PlaA)
from Paenibacillus amylolyticus TB-13, which was defined as lipase.
The ability towards PLA fiber was also demonstrated by lipases from
A. niger231,232 and Candida cylindracea.231 Hydrolytic modification of
the PLLA film using H. insolens cutinase was achieved by Pellis
et al.233 Modification of the polymer resulted in an increase in the
number of hydroxylic and carboxylic groups on the outer surface
of PLLA.233 Kawai234 also suggested that commercially available
lipases can act as PLA depolymerases with preference towards
poly(D-lactic acid). It was concluded that biodegradation of PLA
using microbial enzymes can be challenging for two main reasons:
(i) Tg = 55–62 °C of the polymer; and (ii) mechanical strength of
the polymer, making it less susceptible to biodegradation.235 Never-
theless, it was shown that Est119, a plastic-degrading type of cuti-
nase from T. alba AHK119, possessed a broad substrate specificity
towards PoEs, and could hydrolyze substrates like PLA.87 Some
microbial esterases were also defined as promising biocatalysts for
PLA degradation.70,95,236 Thus lipolytic and lipase-/cutinase-like
enzymes can be a promising solution for biodegradation of PLA.
Other polyesters
Different aliphatic–aromatic copolyesters and ionic phthalic acid-
372
Marten et al.237 demonstrated enzymatic degradation of aliphatic–
aromatic copolyesters containing terephthalate units as aromatic
components using lipase from Pseudomonas sp. The degradation
of polyethylene furanoate (PEF) has also been reported using micro-
bial enzymes.238 PEF made up of 2,5-furandicarboxylic acid (FDCA)
monomers is an emerging bio-based polymer72 and some of the
promising lipolytic biocatalysts which can affect PEF structure were
reported to be H. insolens HiC and Thc_cut1 cutinases.239,240 Haern-
vall et al.29 worked on biodegradation of poly(oxyethylene tere-
phthalate) (PET-PEO) in wastewater treatment plants. The authors
showed that an enzymatic cocktail consisting of an esterase and a
cutinase from Pseudomonas pseudoalcaligenes and a lipase from
Pseudomonas pelagia was effective in the breakdown of PET-
PEO.29 Haernvall et al.32 also investigated hydrolysis of ionic phthalic
acid-based PoEs by wastewater microorganisms and their enzymes.
It was predicted that cutinase PpCutA from P. pseudoalcaligenes and
a putative PpelaLip lipase from P. pelagia could be involved in this
biodegradation process.32 Haernvall et al.241 also reported a new
arylesterase from P. pseudoalcaligenes which can hydrolyze ionic
phthalic PoEs. Aryl esterases belong to the subclass of carboxyl ester
hydrolases that are naturally involved in the hydrolysis of water-
soluble short- to medium-length aromatic esters like lactones (dihy-
drocoumarin (DHC) and acylhomoserine lactones (AHLs).241 There-
fore, although polyesterases are mostly lipolytic and lipase-/

based PoEs can be biodegraded by different polyesterases as well. cutinase-like enzymes, activities towards different PoEs can be

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Polyester plastic biodegradation
found in other carboxyl ester hydrolases as well. More examples of
PoE degradation via lipolytic enzymes hydrolysis are presented in
Table 5.
FROM TODAY'S CHALLENGES TO FUTURE
INNOVATION IN POLYESTER DEGRADATION
PoEs' breakdown processes catalyzed by carboxyl ester hydrolases
can replace harsh chemicals and high-energy processes; however,
knowledge of the diversity of enzymes and microbes acting on
synthetic polymers is still rather limited. The reaction conditions
required for the necessary action of biocatalysts (temperature,
pH, dependence on cofactors, resistance to intermediate reaction
products) also have a great influence on biodegradation. It has
been shown that both PoE itself and carboxylesterase structure
are very important for effective enzymatic PoE hydrolysis.244 The
limitations of native biocatalysts can be overcome by using differ-
ent protein engineering strategies (Fig. 2(a)). Protein engineering
and molecular modeling studies can help in understanding the
behavior of target biocatalysts. Many studies have been per-
formed to improve the effectiveness of different carboxyl ester
hydrolases towards different PoEs (Table 6). It is now generally
accepted that site-directed mutagenesis and design of fused
enzymes are preferable strategies to develop most suitable bioca-
talysts for bioplastics management. One recent study264 presented
a thermophilic whole-cell system for PET degradation using engi-
neered Clostridium thermocellum. The latter bacterium was modi-
fied to secrete LCC. This engineered whole-cell biocatalyst
allowed a simultaneous high-level expression of LCC and degrada-
tion of commercial PET films at 60 °C. After 14 days of incubation
of a batch culture, more than 60% of the initial mass of a PET film
was converted into soluble monomer feedstocks.264 Thus, for gene
and protein engineering progress, the design of new microbial sys-
tems is crucial for efficient PoE biodegradation.
Another strategy to improve PoE plastics management is the
development of biotransformation cascades composed of several
biocatalysts with different substrate preference, or enzyme immo-
bilization (Fig. 2(b)). Gross et al.265 showed that F. solani cutinase
(FsC) is a promising candidate for the enzymatic degradation of
PET, but this enzyme, unfortunately, still suffers from a lack of
activity. The reason for the lack of activity was found to be the
accumulation of cleavage product ethylene glycol (EG) in the
active site of FsC. Accumulated EG reduced the local flexibility of
the target enzyme.265 It was also reported that the PET hydrolysis
product BHET can inhibit PET hydrolysis.72 Addition of a second
enzyme that can hydrolyze products of the first reaction helped
to reduce inhibition of the first enzyme.151,154 The development
of polyesterase-based cocktails should prove to be an attractive
innovation for PoE biodegradation.
Reaction temperature can be considered as one of the most cru-
cial limitations of effective PoE plastic biodegradation. PET and
PUR can be degraded using polyesterase at temperatures up to
70 °C.196,266 Under such temperature conditions amorphous
regions of the PoEs become responsive towards enzymatic degra-
dation.267 Temperature shifts from 40 to 60 °C increase the
amount of PET hydrolysis products tenfold.72 The screening of
thermophilic microorganisms, which produce polyesterases with
a 60–70 °C (and higher) temperature optimum, should be benefi-
cial to improve biodegradation of PoEs. Addition of cofactors to
the reaction medium or immobilization can enhance activity and
thermostability of target biocatalysts as well.36,72,266,268 LCC modi-
fication through glycosylation and expression in Pichia pastoris
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resulted in improved stability of the enzyme and increased the
temperature of thermal-induced aggregation by 10 °C. The latter
resulted in improved catalytic PET hydrolysis.269 The above-
mentioned protein engineering is also one of the most common
choices to increase thermal characteristics of polyesterases.
Another challenge of enzymatic PoEs hydrolysis is the lack of
effective screening methods. PoE-hydrolyzing enzymes are still
screened using substrates intended for detection of esterases
and lipases. Often, polyesterase activities are evaluated based
on clearing zone appearance in agar plates with tributyrin, and
sometimes with more efficient substrates such as polycaprolac-
tone diol or Impranil DLN.129,270 One promising approach was
developed by Zumstein and co-workers.271 The authors sug-
gested incorporating fluorescein dilaurate (FDL), a fluorogenic
ester substrate, into the PoE matrix. Implemented on a microplate
reader platform, the FDL-based approach enabled sensitive and
high-throughput analysis of the enzymatic hydrolysis of eight ali-
phatic PoEs by two fungal esterases (FsC and R. oryzae lipase).271
Such technology can be useful in screening and mechanistic stud-
ies of enzymatic PoE hydrolysis. Danso et al.129 also highlighted
that current cultivation technologies have not yet resulted in the
identification of highly active PoE-degrading enzymes from
global metagenomes and non-cultivated microorganisms. The
further development of smart search algorithms for mining meta-
genome datasets is also certainly a rewarding task.129 There is also
a deficiency of the atomic-level characterization of how common
PoEs are degraded by lipolytic and other related biocatalysts.178
Currently, there is a large, fundamental knowledge gap regarding
bacterial polyesterases, a shortage of information on structure–
function relationships and tertiary structures of the enzymes.
More protein engineering research regarding polyesterases
should be performed to better understand which aa or domains
are responsible for PoE modifications and biodegradation in
selected enzymes.
The ability of lipolytic and lipase-/cutinase-like enzymes to break
down PoEs plastics is now becoming an extensively studied topic
both in research and practical sectors. However, there are several
remaining challenges: (i) isolation of new plastic-decomposing
microorganisms; (ii) development of a screening method enabling
effective identification of polyesterases; (iii) structural and functional
information about these biocatalysts; and (iv) development of
upstream and downstream processing of PoE plastic pollution using
microbial enzymes in real practice. The new fundamental knowl-
edge and innovative technical troubleshooting related to the men-
tioned aspects can be a helpful tool for development of a more
effective eco-friendly approach for plastic-waste management.
CONCLUSIONS
Lipolytic (lipases, esterases, cutinases) and lipase-/cutinase-like
(PETase, PHA depolymerases) enzymes (polyesterases) exhibit
high relevance in polyester waste management. Nevertheless,
effective biodegradation using microbial enzymes encounters
several major limitations such as chemical structure, Tm or Tg of
polyesters. The physicochemical characteristics of polyesterases
(optimal temperature, suitable substrate binding channel, ther-
mostability) additionally seriously influence the success of polyes-
ter waste decomposition. Today a new approach and innovative
solutions are required for both reduction of the production of
non-biodegradable, non-reusable or low-reuse plastics and
improvement of target enzymes or microorganisms as tools for
373
plastic degradation. Protein and metabolic engineering, enzyme
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www.soci.org
design de novo and development of biocatalytic cascade reac-
tions, together with advances in chemical and physical
approaches used in polyester plastic recycling, offer the potential
for a cleaner environment in the future.
CONFLICT OF INTEREST
The authors declare that they have no conflict of interest.
CREDIT AUTHOR STATEMENT
Alisa Gricajeva: conceptualization, visualization, writing and origi-
nal draft preparation, reviewing and editing; Ashok Kumar Nadda:
conceptualization, writing and original draft preparation, review-
ing and editing; Renata Gudiukaite: conceptualization, visualiza-
tion, writing and original draft preparation, reviewing and
editing, supervision.
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