FACULTY SCIENCE AND TECHNOLOGY

SBT4033
ENZYME TECHNOLOGY AND FERMENTATION

INDIVIDUAL ASSIGNMENT:

CURRENT ISSUES CONCERNING ENZYME TECHNOLOGY

NAME : AMIR ZULKHAIRI BIN ZURAIMI

MATRIC NUMBER : 1130751

GROUP : KSA

LECTURERS NAME : DR NAZMI ABDUL MANAP

 Enzymes are found in all part of cells. There are six classes of
enzyme reaction which are oxidoreductase, transferase, hydrolase, lyase,
isomerase and ligase. This classes of enzymes have a different reaction
where oxidoreductase involve in oxidation and reduction reactions,
transferases to transfer functional group, hydrolase for hydrolysis
reaction, lyase function in breaking the C-C, C-O, and C-N bonds,
isomerise to isomerisation reaction and lastly ligase involve in the
formation of bonds. After synthesis within a cell, enzymes can function
independently of the cell provided certain conditions are maintained. Enzyme
technology involves the production, isolation and purification of enzymes.
Commercial enzymes are obtained generally from plants, animals and
microbes

Nowadays, there are like 4000 enzymes are known, and out of this,
approximately 200 microbial original types are being used commercially.
However, only about 20 enzymes are produced on a truly industrial scale.
The world enzyme demand is satisfied by about 12 major producers and
400 minor suppliers. Nearly 75% of the total enzymes are produced by
three top enzyme companies, i.e. Denmark-based Novozymes, US-based
DuPont (through the May 2011 acquisition of Denmark-based Danisco)
and Switzerland-based Roche. About 158 enzymes were used in food
industry, 64 enzymes in technical application and 57 enzymes in
feedstuff, of which 24 enzymes are used in three industrial sectors. Almost
75% of all industrial enzymes are hydrolytic enzymes.

In the twenty-first century, chemical and associated industries quest

a transition prototype from traditional chemical-based concepts to a
greener, sustainable and environmentally-friendlier catalytic alternative,
both at the laboratory and industrial scale. In this context, bio-based
catalysis offers numerous benefits along with potential biotechnological
and environmental applications. The bio-based catalytic processes are
energy efficient than conventional methodologies under moderate
processing, generating no and negligible secondary waste pollution.
Thanks to key scientific advances, now, solid-phase biocatalysts can be
economically tailored on a large scale. Nevertheless, it is mandatory to
recover and reprocess the enzyme for their commercial feasibility, and
immobilization engineering can efficiently accomplish this challenge.

The first part of the present review work briefly outlines the
immobilization of lignin-modifying enzymes (LMEs) including lignin
peroxidase (LiP), manganese peroxidase (MnP) and laccase of white-rot
fungi (WRF). Whereas, in the second part, a particular emphasis has been
given on the recent achievements of carrier-immobilized LMEs for the
degradation, decolorization, or detoxification of industrial dyes and dye-
based industrial wastewater effluents.

Research on lignin-degrading enzymes has greatly intensified in

recent years because of their potential applications in a variety of
biotechnological applications. These applications include
biotransformation of lignocellulosic biomass to feeds, fuels, and
chemicals; biopulping; biobleaching of paper pulps; decolorizing and
detoxifying kraft bleach plant effluents; and degradation of highly toxic
environmental chemicals such as dioxins, polychlorinated biphenyls,
various dye pollutants, and polyaromatic hydrocarbons Basidiomycetous
fungi involved in white rot decay of wood are known to play a major role in
the mineralization of the lignin polymer to carbon dioxide and water in the
terrestrial environment, while bacteria are believed to be relatively
unimportant in this process. Three major classes of extracellular enzymes
designated manganese-dependent peroxidases (MNPs), lignin peroxidases
(LIPs), and laccases are believed to be important in the fungal degradation
of lignin. LIPs and MNPs are heme proteins, while laccases are copper-
containing proteins. Some wood-degrading fungi contain all three classes
of lignin-modifying enzymes (LMEs), while the others contain only one or
two of these enzymes.

The sea grasses and mangrove plants are the major contributors of
lignocellulose in the highly productive coastal marine environments.
Microbial degradation of the lignin component is the rate-limiting step
affecting the availability of lignocellulose-derived dissolved organic carbon
in the food chain. Fungi associated with decaying sea grass and mangrove
plants contribute about 3% of the biomass per g (dry weight) of detritus
and contribute nearly 75 to 100% of nitrogen in decaying salt marsh grass
ecosystems. The association and importance of terrestrial species of fungi
with plant detritus in the coastal marine environment have also been
documented. However, there is little published information on the lignin-
degrading ability of obligate or facultative marine fungi. Only a few
isolated reports indicate low-level degradation of [14C] lignin-labeled
lignocellulose by marine fungi. Moreover, the presence of MNPs, LIPs, and
laccases in these fungi has not been investigated except for two recent
surveys. In this study, we describe the production and characteristics of
LMEs, mineralization of synthetic, side chain-labeled [ 14C] lignin, and
degradation of various heterocyclic and azo dyes by a marine isolate
of Flavodon flavus isolated from decaying sea grass leaves in a tropical
coral lagoon.

Reference:
1) Bilal, M., Asgher, M., Parra-Saldivar, R., Hu, H., Wang, W., Zhang, X., & Iqbal, H. M. (2017).
Immobilized ligninolytic enzymes: An innovative and environmental responsive technology
to tackle dye-based industrial pollutantsA review. Science of The Total Environment, 576,
pp. 646-659.
2) Raghukumar, C., Dsouza, T. M., Thorn, R. G., & Reddy, C. A. (1999). Lignin-modifying
enzymes of Flavodon flavus, a basidiomycete isolated from a coastal marine
environment. Applied and Environmental Microbiology, 65(5), pp. 2103-2111.