Purification and biochemical properties of microbial pectinases—a review

doi:10.1016/S0032-9592(02)00203-0

Process Biochemistry

Volume 38, Issue 7, 28 February 2003, Pages 987-996

https://doi.org/10.1016/S0032-9592(02)00203-0 Get rights and content

Abstract

Pectinases are a complex group of enzymes that degrade various pectic substances present in plant tissues. Pectinases have potential applications in fruit, paper and textile industries. Apart from these industrial applications, these enzymes possess biological importance in protoplast fusion technology and plant pathology. Since applications of pectinases in various fields are widening, it is important to understand the nature and properties of these enzymes for efficient and effective usage. For the past few years, vigorous research has been carried out on isolation and characterization of pectinases. New affinity matrices with improved characteristics and affinity-precipitation techniques have been developed for purification of pectinases. Recently much attention has been focused on chemical modification of pectinases and their catalytic performance by various researchers. These studies are helpful in determining key amino acid residues responsible for substrate binding, catalytic action, and physico-chemical environmental conditions for maximum hydrolysis. This short review highlights progress on purification and understanding the biochemical aspects of microbial pectinases.

Section snippets

Pectic substances and pectinases

Pectic substances and celluloses are the most abundant carbohydrates present in plants. Pectic substances like pectin, protopectin and pectic acids, present in cell wall and middle lamella, contribute firmness and structure to plant tissues. In pectic substances, d-galacturonic acid units are linked together by α-1,4-glycosidic linkages and the carbonyl side groups are 60–90% esterified with methanol. The rhamnose units can be inserted into the main uronide chain and often side chains of

History of pectinase research

The history of pectinases began with an understanding the structure of pectic substances and the mechanism by which pectolytic enzymes degrade pectic substances. Later the microbial production of pectinases became prominent for many decades. Many microorganisms, viz., bacteria, yeast and fungi could produce pectinases. Evidence showed that pectinases are inducible and they can be produced from different carbon sources [15], [16], [17], [18], [19]. In the course of time, numerous reports have

Purification of microbial pectinases

In order to characterize and study the properties of microbial pectinases the enzymes must be purified. Important purification methods for the isolation of different pectinases is briefly summarized in this section. Pectinases from various sources of microorganisms have been purified to homogeneity. An exo-PG has been separated from mycelial extracts of Aspergillus niger by eluting from DEAE cellulose with 0.2 M sodium acetate buffer at pH 4.6. Purification was efficient with 209-fold increase

Biochemical properties of microbial pectinases

An improved knowledge of the properties of microbial pectinases is important in commercialization of industrial production and to apply these enzymes in various potential fields. Hence, many researchers have focused on stability, chemical modification and catalytic performance of pectinases.

Conclusions and perspectives

During the past few decades significant progress has been made in purifying pectinases to homogeneity using different purification methods. The literature shows that extensive research has been focused on PE, PG, PGL and PL; surprisingly PMG and other pectinases have received less attention. Even though new affinity matrices were developed for isolation of pectinase, specific and better purification methods such as immunochemical techniques are needed. Lu and coworkers crystallized endo-PG from

Acknowledgements

We apologize to those whose papers and critical studies were not cited in this article because of space limitation. We are thankful to researchers, colleagues and others who helped directly or indirectly to carry out this work. Gummadi thanks G.R.S., G.S.S., and G.R.L. for stimulation.

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Purification and biochemical properties of microbial pectinases—a review

Abstract

Section snippets

Pectic substances and pectinases

History of pectinase research

Purification of microbial pectinases

Biochemical properties of microbial pectinases

Conclusions and perspectives

Acknowledgements

Adv. Appl. Microbiol.

Enzyme Microbiol. Technol.

Enzyme Microb. Technol.

Enzyme Microbiol. Biotechnol.

Proc. Biochem.

J. Food. Protection

FEMS Microb. Lett.

Enzyme Microbiol. Biotechnol.

J. Biol. Chem.

J. Biol. Chem.

FEBS Lett.

Enzyme Microbiol. Technol.

Bioresour. Technol.

Enzyme Microbiol. Technol.

FEBS Lett.

J. Biol. Chem.

Biochem. Eng. J.

Carbohydr. Res.

J. Mol. Biol.

Clarification of apple juice by fungal PG preparations

Food Technol.

Application of enzymes in fruit juice technology

Bacteria, enzymes and wood permeability

Proc. Biochem.

Advances in food processing using pectic and other enzymes

Chem. Ind.

Ultrafiltration preparation of pectinolytic enzymes from citric acid fermentation broth

Proc. Biochem.

Pectic enzymes

Enzymatic degradation of cell wall and related plant polysaccharides

Crit. Rev. Biotechnol.

Production of pectolytic enzymes: a review

Bioproc. Eng.

Applications of pectinases in the commercial sector: a review

Bioresour. Technol.

Polygalacturonase associated with infection of Valencia orange by Penicillium italicum

Phytopathology

Perspectives in the biological function and the technological application of polygalacturonases

Appl. Microbiol. Biotechnol.

Isolation of tobacco mesophyll cells in intact and active state

Plant Cell. Physiol.

Catabolic repression of synthesis of inducible polygalacturonases and pectinesterase by Aspergillus niger species

Curr. Microbiol.

Effect of carbon sources on the synthesis of pectinase by Aspergilli

Bioproc. Eng.

Statistical optimization of medium components for improved synthesis of pectinase by Aspergillus niger

Bioproc. Eng.

Submerged production of pectolytic enzymes by Aspergillus niger. Effect of different aeration and agitation regimes

Appl. Microbiol. Biotechnol.

Rotating simplex method of optimization of physical parameters for higher production of extracellular pectinases in bioreactor

Bioproc. Eng.

Isolation and characterization of polygalacturonase genes (pecA and pecB) from Aspergillius flavus I

Appl. Environ. Microbiol.

The Erwinina chrysanthemi pecT gene regulates pectinase gene expression

J. Bacteriol.

Cloning, sequence analysis and overexpression of a Saccharomyces cerevisiae endopolygalacturonase-encoding gene (PLG1)

Yeast

Regulation of the expression of endopolygalacturonase gene PGU 1 in Saccharomyces

Yeast

Expression of pectate lyase from Colletotrichum gloesosporioides in C. magna promotes pathogenicity

Mol. Plant Microbe. Interact.

Expression cloning of fungal enzyme genes, a novel approach for efficient isolation enzyme genes of industrial relevance

FEMS Microbiol. Rev.

The pectic, enzymes of Aspergillus niger mercury activated exopolygalacturonase

Biochem. J.

The peptic enzymes of Aspergillus niger: a second exopolygalacturonase

Biochem. J.

Isolation of extracelluar pectolytic enzymes produced by Aspergillus niger

Coolection Chechoslov Commun.

Purification and properties of endopolygalacturonase produced by Rhizopus stolonifer

Biotechnol. Lett.