PECTIN

Pectin is a complex heteropolysaccharide composed of linear chains of α-D-galacturonic acid or other

similar sugar derivatives, commonly found in plant cell walls as cementing material.
Pectin often remains associated with other cell wall polysaccharides like cellulose, hemicellulose and
lignin.
Pectin is responsible for providing firmness and structure to the cell wall and also helps in intercellular
adhesion and mechanical resistance of the cell.

STRUCTURE
Pectins are a family of covalently associated galacturonic acid-rich plant cell wall polysaccharides.
About 70% of all pectin contains galacturonic acid and all pectin polysaccharides contain galacturonic
acid linked at the O-1 and O-4 positions of the polymer.

The structural elements of pectin are classified

into two families:
1. Galacturonans
2. Rhamnogalacturonans

Figure 1: Structure of Pectin

Galactorunans consist of a backbone of α-
(1,4)-linked D-galacturonic acid residues. It can either be branched or unbranched.
The backbone in rhamnogalacturonans, however, contains diglycosyl repeating units of α-L-
rhamnose-(1,4)-α-D-galacturonic acid.

ENZYMES INVOLVED IN BIODEGRADATION OF PECTIN

Pectinases is a group of enzymes (at least seven different enzymes) involved in the breakdown of
pectin obtained from various sources.

Due to the diverse group of pectin that is found in different living organisms, pectinases are diverse.
Most common and industrially important pectinases are divided into different groups on the basis of
the differences in their substrate, structure, and reaction mechanism.
Some of the common pectinolytic enzymes are:
i. Pectinesterases
ii. Polygalacturonases
iii. Pectin Lyases
iv. Pectin Depolymerases

MICROORGANISMS INVOLVED IN BIODEGRADATION OF PECTIN

Different groups of microorganisms are known to produce multiple sets of pectinolytic enzymes that
aid either in the absorption of nutrients or help in the pathogenesis of microbial diseases.

1. Pectinolytic bacteria
Bacteria produce different sets of pectinolytic enzymes that help in the overall degradation of
pectin substrates. Some of the common pectinolytic bacteria include Bacillus, Pseudomonas, and
Staphylococcus.
Some bacteria like Bacillus badius, Bacillus asahin, Bacillus psychrosaccharolyticus, and
Pseudomonas aeruginosa even utilize the pectinolytic activity in their pathogenesis of different
diseases.

2. Pectinolytic fungi
Phanerochaete chrsosporium is one of the most studied basidiomycetes (white rot) fungi that
degrade most of the complex polysaccharides like cellulose, pectin, and chitin.
Other fungal species Magnaporthe oryzae, Giberella zeae, Botrytis fuckeliana, Sclerotinia
sclerotiorum, Aspergillus nidulans, Trichoderma virens, Podospora anserine, Rhizopus oryzae,
and Aspergillus clavatus.

MECHANISM OF MICROBIAL DEGRADATION PECTIN

Mechanism of de-esterification by Pectin esterases and Pectin methyl esterases
Pectin esterases act on the pectin substrates by one of the three mechanisms:

1. The single-chain mechanism where the enzyme acts on all substrate side on the polymeric chain.
2. The multiple-chain mechanism involving the catalysis of just one reaction which then dissociates
the substrate.
3. A multiple-attack mechanism where the enzyme catalyzes multiple reactions before the enzyme-
substrate complex dissociates.
Mechanism of Hydrolytic cleavage in Polygalacturonases and Pectin lyases
 The process of hydrolytic cleavage of α-1,4-glycosidic bonds in pectin begins with the
positioning of the active site amino acids on the susceptible glycosidic bonds.
 The motifs on the active sites interact with the substrate on either side of the designated bond
through multiple hydrogen bonds.
 The hydrogen bonds create sufficient strain and distortion on the susceptible glycosidic bond.
 The distortion is followed by proton transfer between the amino acids of the active site and the
glycosidic bond.
 This causes the cleavage of glycosidic bonds with the release of the first end product with
subsequent formation of a covalent bond between the substrate and the catalytic site nucleophile