Elsevier

Process Biochemistry

Volume 40, Issue 9, September 2005, Pages 2931-2944
Process Biochemistry

Review
Microbial pectinolytic enzymes: A review

https://doi.org/10.1016/j.procbio.2005.03.026Get rights and content

Abstract

Pectinases or petinolytic enzymes, hydrolyze pectic substances. They have a share of 25% in the global sales of food enzymes. Pectinases are one of the most widely distributed enzymes in bacteria, fungi and plants. Protopectinases, polygalacturonases, lyases and pectin esterases are among the extensively studied pectinolytic enzymes. Protopectinases catalyze the solubilization of protopectin. Polygalacturonases hydrolyze the polygalacturonic acid chain by addition of water and are the most abundant among all the pectinolytic enzymes. Lyases catalyze the trans-eliminative cleavage of the galacturonic acid polymer. Pectinesterases liberate pectins and methanol by de-esterifying the methyl ester linkages of the pectin backbone. Pectinolytic enzymes are of significant importance in the current biotechnological era with their all-embracing applications in fruit juice extraction and its clarification, scouring of cotton, degumming of plant fibers, waste water treatment, vegetable oil extraction, tea and coffee fermentations, bleaching of paper, in poultry feed additives and in the alcoholic beverages and food industries. The present review mainly contemplates on the types and structure of pectic substances, the classification of pectinolytic enzymes, their assay methods, physicochemical and biological properties and a bird's eye view of their industrial applications.

Introduction

In nature, microorganisms have been endowed with vast potentials. They produce an array of enzymes, which have been exploited commercially over the years. Pectinases are of great significance with tremendous potential to offer to industry [1]. They are one of the upcoming enzymes of the commercial sector, especially the juice and food industry [2] and in the paper and pulp industry [3], [4].

Pectinolytic enzymes or pectinases are a heterogeneous group of related enzymes that hydrolyze the pectic substances, present mostly in plants. Pectinolytic enzymes are widely distributed in higher plants and microorganisms [5]. They are of prime importance for plants as they help in cell wall extension [6] and softening of some plant tissues during maturation and storage [7], [8]. They also aid in maintaining ecological balance by causing decomposition and recycling of waste plant materials. Plant pathogenicity and spoilage of fruits and vegetables by rotting are some other major manifestations of pectinolytic enzymes [5], [9], [10], [11], [12], [13], [14].

It has been reported that microbial pectinases account for 25% of the global food enzymes sales. Almost all the commercial preparations of pectinases are produced from fungal sources [14]. Aspergillus niger is the most commonly used fungal species for industrial production of pectinolytic enzymes [15], [16], [17].

This review mainly concentrates on the types of pectinolytic enzymes, their classification, mode of action and the substrates on which they act. It also provides a bird's eye view of the possible applications of these enzymes in industrial sector.

Section snippets

Pectic substances

Pectic substance is the generic name used for the compounds that are acted upon by the pectinolytic enzymes. They are high molecular weight, negatively charged, acidic, complex glycosidic macromolecules (polysaccharides) that are present in the plant kingdom. They are present as the major components of middle lamella between the cells in the form of calcium pectate and magnesium pectate [18]. That the middle lamella is largely composed of pectic substances, has been confirmed by the comparable

The pectinolytic enzymes

The pectinolytic enzymes may be divided in three broader groups as follows [7], [10]:

  • (I)

    Protopectinases: degrade the insoluble protopectin and give rise to highly polymerized soluble pectin.

  • (II)

    Esterases: catalyze the de-esterification of pectin by the removal of methoxy esters.

  • (III)

    Depolymerases: catalyze the hydrolytic cleavage of the α-(1  4)-glycosidic bonds in the d-galacturonic acid moieties of the pectic substances.

Depolymerases act on pectic substances by two different mechanisms, hydrolysis, in

Biotechnological applications of microbial pectinases

Over the years, pectinases have been used in several conventional industrial processes, such as textile, plant fiber processing, tea, coffee, oil extraction, treatment of industrial wastewater, containing pectinacious material, etc. They have also been reported to work on purification of viruses [143] and in making of paper [144], [4]. They are yet to be commercialized.

Conclusion

Most of the studies performed so far have been concentrated with the screening, isolation, production, purification, characterization and applications of pectinolytic enzymes in increasing the fruit juice yield and its clarification. Some reports are available on the applications of pectinases in other industries. Study of the molecular aspects of pectinases and engineering of enzymes that are more robust with respect to their pH and temperature kinetics by the techniques of protein engineering

Acknowledgement

The financial support from the Department of Biotechnology, Ministry of Science and Technology, Government of India to Department of Biotechnology, Himachal Pradesh University, Shimla (India) is thankfully acknowledged.

References (152)

  • L. Marcus et al.

    Purification and characterization of pectolytic enzymes produced by virulent and hypovirulent isolates of Rhizoctonia solani Kuhn

    Physiol Mol Plant Pathol

    (1986)
  • J.V.B. Souza et al.

    Screening of fungal strains for pectinolytic activity: endopolygalacturonase production by Peacilomyces clavisporus 2A.UMIDA.1

    Process Biochem

    (2003)
  • P. Reymond et al.

    Cloning and sequence analysis of a polygalacturonases-encoding gene from the phytopathogenic fungus Sclerotinia sclerotiorum

    Gene

    (1994)
  • S. Centis et al.

    Isolation and sequence analysis of Clpg1, a gene coding for an endopolygalacturonase of the phytopathogenic fungus Colletotrichum lindemuthianum

    Gene

    (1996)
  • W. Guo et al.

    Identification of a novel pelD gene expressed uniquely in plant by Fusarium solani f. sp. pisi (Nectria haematococca, mating type VI) and characterization of its protein as an endo-pectate lyase

    Arch Biochem Biophys

    (1996)
  • A. Gainvors et al.

    Purification and characterization of acidic endo-polygalacturonase encoded by the PGL-1 gene from Saccharomyces cerevisiae

    FEMS-Microbiol Lett

    (2000)
  • R. Pressey et al.

    Two forms of polygalacturonase in tomatoes

    Biochim Biophys Acta

    (1973)
  • R. Pressey et al.

    Modes of action of carrot and peach exo-polygalacturonases

    Phytochemistry

    (1975)
  • N. Pathak et al.

    Multiple forms of polygalacturonase from banana fruits

    Phytochemistry

    (1998)
  • N. Nelson

    A photometric adaptation of the Somogyi method for the determination of glucose

    J Biol Chem

    (1944)
  • Y. Milner et al.

    A copper reagent for the determination of hexuronic acids and certain ketohexoses

    Carbohydrate Res

    (1967)
  • A. Collmer et al.

    Assay methods for pectic enzymes

    Methods Enzymol

    (1988)
  • E. Roboz et al.

    Breakdown of pectic substances by a new enzyme from Neurospora

    J Biol Chem

    (1952)
  • S.A. Singh et al.

    Exo polygalacturonate lyase from a thermophilic Bacillus sp

    Enzyme Microbial Technol

    (1999)
  • A. Dayanand et al.
  • Q.K. Beg et al.

    Bleach-boosting of eucalyptus kraft pulp using combination of xylanase and pectinase from Streptomyces sp. QG-11-3

    Res Bull Panjab University

    (2001)
  • L. Viikari et al.

    Biotechnology in the pulp and paper industry

  • J.R. Whitaker

    Microbial pectinolytic enzymes

  • O.P. Ward et al.

    Enzymatic degradation of cell wall and related plant polysaccharides

    CRC Crit Rev Biotechnol

    (1989)
  • T. Sakai

    Degradation of pectins

  • G. Aguilar et al.

    Constitutive exo-pectinase produced by Aspergillus sp. CH-Y-1043 on different carbohydrate source

    Biotechnol Lett

    (1990)
  • L. Fraissinet-Tachet et al.

    Regulation by galacturonic acid of pectinolytic enzyme production by Sclerotinia sclerotiorum

    Curr Microbiol

    (1996)
  • M.C.M. Pérombelon et al.

    Ecology of soft rot Erwinias

    Annu Rev Phytopathol

    (1980)
  • A.C. Collmer et al.

    The role of pectic enzymes in plant pathogenesis

    Annu Rev Phytopathol

    (1986)
  • C. Lang et al.

    Perspectives in the biological function and the technological application of polygalacturonases

    Appl Microbiol Biotechnol

    (2000)
  • P. Kotzekidov

    Production of polygalacturonases by Byssachlamys fulva

    J Ind Microbiol

    (1991)
  • G.S.N. Naidu et al.

    Production of pectolytic enzymes—a review

    Bioprocess Eng

    (1998)
  • G. Rastogi

    Vishal's objective botany

    (1998)
  • C. Sterling

    Crystal-structure of ruthenium red and stereochemistry of its pectic stain

    Am J Bot

    (1970)
  • M. Gee et al.

    Reaction of hydroxylamine with pectinic acids. Chemical studies and histochemical estimation of the degree of esterification of pectic substances in fruit

    J Agric Food Chem

    (1959)
  • R.M. McCready et al.

    Test for pectin based on reaction of hydroxamic acids with ferric ion

    J Agric Food Chem

    (1955)
  • P. Albersheim et al.

    Histochemical localization at the electron microscope level

    Am J Bot

    (1963)
  • T. Sakai et al.

    Pectin, pectinase and protopectinase: production, properties and applications

    Adv Appl Microbiol

    (1993)
  • R.C. Codner

    Pectinolytic and cellulolytic enzymes in the microbial modification of plant tissues

    J Appl Bacteriol

    (2001)
  • N.G. Sathyanarayana et al.

    Purification and biochemical properties of microbial pectinases—a review

    Process Biochem

    (2003)
  • C.J.B. van der Vlugt-Bergmans et al.

    Endo-xylogalacturonan hydrolase, a novel pectinolytic enzyme

    Appl Environ Microbiol

    (2000)
  • C.S. Brinton et al.

    Definitions written by the committee on nomenclature of pectin of the agriculture-food division

    J Am Chem Soc

    (1927)
  • T. Sakai et al.

    Purification and crystallisation of a protopectin-solubilizing enzyme from Trichosporon penicillatum

    Agric Biol Chem

    (1982)
  • T. Sakai et al.

    Purification and some properties of a protopectin-solubilizing enzyme from Galactomyces reesii strain L

    Agric Biol Chem

    (1984)
  • T. Sakai et al.

    Purification, crystallization and some properties of an endopolygalacturonase from Kluyveromyces fragilis

    Agric Biol Chem

    (1984)
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