Pectolytic enzymes play an important role in food processing industries and alcoholic beverage industries. These enzymes degrade pectin and reduce the viscosity of the solution so that it can be handled easily. These enzymes are mainly synthesized by plants and microorganisms. Aspergillus niger is used for industrial production of pectolytic enzymes. This fungus produces polygalacturonase, polymethylgalacturonase and pectinlyase. This review mainly concerns with the production of pectolytic enzymes using different carbon sources. It also deals with the effect of operating parameters such as temperature, aeration rate, agitation and type of fermentation on the production of these enzymes.

T Panda

Department Of Chemical Engineering

G. Sathya Narayana Naidu

Pectin

Aspergillus niger

BEVERAGE

enzyme activity

enzyme synthesis

Fermentation

Food processing

nonhuman

priority journal

review

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IIT Madras

Production of pectolytic enzymes – a review

Bioprocess Engineering

The present study is focused on the utilization of fruit and agro-industrial wastes for the production of yeast pectinases using response surface optimization techniques. Orange peel (OP), groundnut oil cake (GC), MnSO4 and incubation period (IP) were found as significant parameters for pectinase production. The central composite design of media optimization indicated that OP (5), GC (4), MnSO4 (0.08%, w/v) and IP (48 h) increased the pectinase production by 9-fold. Crude pectinase promoted the enzymatic peeling of oranges and processing of raw banana fibers. Topographical changes of enzyme treated orange and mango peels were studied using AFM which provides a new tool to unravel the role of pectin aggregation in the dissolution of middle lamella during enzymatic hydrolysis. Changes in the fingerprint regions of enzyme treated fruit substrates were observed along with the disappearance of the impurities such as waxes and pectin using FTIR spectral analysis. © 2016 Elsevier Ltd.

Biocatalysis and Agricultural Biotechnology

Enhanced production of pectinase by Saccharomyces cerevisiae isolate using fruit and agro-industrial wastes: Its application in fruit and fiber processing

The effect of various parameters such as pH, agitation and aeration was studied for maximum production of pectin lyase (PL) and pectate lyase (PGL) by a novel yeast strain Debaryomyces nepalensis in bioreactor. The optimal levels of pH, aeration and agitation rate was found to be 7.0, 300 rpm and 1 vvm, respectively. Under these conditions, D. nepalensis produced 14,200 U/L of PL and 12,000 U/L of PGL corresponding to a productivity of 600 U/L h and 500 U/L h of PL and PGL, respectively. Fed-batch production was studied by feeding inducer (lemon peel), carbon source (galactose) individually and in combination at 12 h of growth for enhanced production of PL and PGL. Combined feeding of inducer and carbon source at 12 h was found to be the best strategy for enhanced production of PL and PGL. Under these conditions, production of PL and PGL increased to 23,300 U/L and 22,400 U/L, respectively which corresponded to a productivity of 728 U/L h of PL and 700 U/L h of PGL, respectively. The production was increased by 1.6- and 1.8-fold and productivity by 1.2- and 1.4-fold for PL and PGL, respectively when compared to batch culture. © 2007 Elsevier Ltd. All rights reserved.

Bioresource Technology

Batch and fed batch production of pectin lyase and pectate lyase by novel strain Debaryomyces nepalensis in bioreactor

Pectin and other pectic substances are complex polysaccharides, which contribute firmness and structure to plant tissues as a part of the middle lamella. The basic unit in pectic substances is galacturonan (α-D-galacturonic acid). Pectic substances are classified into two types; homogalacturonan and heterogalacturonan (rhamnogalacturonan). In homogalacturonan, the main polymer chain consists of α-D-galacturonate units linked by (1 → 4) glycosidic bonds, whereas in rhamnogalacturonan, the primary chain consist of (1→4) linked α-D-glacturonates and with about 24% L-rhamnose units that are β(1→2) and β(1→4) linked to D-galacturonate units (Whitaker, 1991). The side chains of rhamnogalacturonans usually consist of L-arabinose or D-galacturonic acid units. In plant tissues, about 6070% of the galacturonate units are esterified with methanol and occasionally with ethanol. Based on the degree of esterification, pectic substances are classified into protopectin, pectinic acid, pectin and polygalacturonic acid (Table 1). Molecular size, degree of esterification and weight distribution of polygalacturonic acid residues are important factors that contribute to heterogeneity in pectic substances. Relative molecular masses of pectic substances isolated from various sources such as citrus fruits, apple and plums, range from 25 to 350 kDa. Pectinases are a complex and diverse group of enzymes involved in the degradation of pectic substances. The diversity of forms of pectic substances in plant cells probably accounts for the existence of various forms of these enzymes. Pectinases are classified depending on their substrate and mode of enzymatic reaction (Fig. 1). Pectinases act as carbon recycling agents in nature by degrading pectic substances to saturated and unsaturated galacturonans, which are further catabolized (Table represented) to 5-keto-4-deoxy-uronate and finally to pyruvate and 3-phosphoglyceraldehyde (Vincent-Sealy et al., 1999). Pectinases from phytopathogenic fungi such as Aspergillus flavus, Fusarium oxysporum and Botrytis cinerea are also known to play a vital role in plant pathogenicity or virulence by degrading pectic compounds present in cell wall (Lang and Drenberg, 2000; DiPietro and Roncero, 1996; Ten Have et al., 1998). Pectinases, especially polygalacturonase, is known to play a major role in pectin breakdown during the final stages of fruit ripening (Sozzi- Quiroga and Fraschina, 1997; Chin et al., 1999). Polymethylgalacturonase (PMG), polygalacturonase (PG), pectin lyase (PL), polygalacturonate lyase (PGL) and pectinesterase (PME) are industrially important pectinases discussed in this chapter. © 2007 Springer.

Industrial Enzymes: Structure, Function and Applications

Structural and biochemical properties of pectinases

Debaryomyces nepalensis was previously isolated, which is capable of producing pectin lyase and pectate lyase using pectin as sole source of carbon. The parameters affecting the activity of these enzymes are categorized into two, viz., chemical (amount of substrate and enzyme) and physical (pH of reaction mixture and temperature of incubation). The effect of these parameters on pectin lyase and pectate lyase was studied using central composite design. The optimal conditions of amount of substrate and enzyme (culture broth) were found to be 545 μl (∼1 g/l pectin) and 123 μl for pectin lyase and 707 μl (∼1.1 g/l polygalacturonic acid) and 96 μl for pectate lyase. The optimum pH and temperature for reaction was found to be 6.4 and 35 °C for pectin lyase and 7.5 and 32 °C for pectate lyase. After optimization, the activity of pectin lyase and pectate lyase was increased by 1.3- and 1.4-fold, respectively. © 2006 Elsevier B.V. All rights reserved.

Biochemical Engineering Journal

Optimization of chemical and physical parameters affecting the activity of pectin lyase and pectate lyase from Debaryomyces nepalensis: A statistical approach

Pectic transeliminases, also known as pectic lyases or pectinases, are involved in the degradation of pectic substances. They have a wide range of applications in food and textile processing. Although Aspergillus and Penicillium spp. produce pectin lyases, bacteria are the major producers of polygalacturonate lyase. The yields of pectic transeliminases are less than other pectinases. Since new applications for pectic transeliminases are emerging, an improved process for the production of these enzymes is necessary. © Springer 2005.

Biotechnology Letters

Microbial pectic transeliminases

The synthesis of pectinase is investigated using six species of Aspergillus, with five media differing either in their carbon sources or level of carbon source(s). Five of the six species used, synthesized appreciable amounts of pectinase in the media containing sugars. Pectinase synthesis was highest for A. niger, NCIM 548, with all the sugar containing media. A. foetidus, NCIM 510, was the only one among the organisms studied, that responded well to the medium containing pectin in the absence of additional sugars supplied in the medium. © 1995 Springer-Verlag.

Effect of carbon sources on the synthesis of pectinase by Aspergilli

Brazilian Journal of Food Technology

Errata

World Journal of Microbiology & Biotechnology

Production of pectinases by Aspergillus niger in solid state fermentation at high initial glucose concentrations

Pectinase production profile of Aspergillus foetidus in solid state cultures at different acidities

Applied Microbiology and Biotechnology

Experimental and theoretical investigations of submerged fermentation and synthesis of pectinolytic enzymes by Aspergillus niger

Production of pectolytic enzymes - A review

Journal	Data powered by TypesetBioprocess Engineering
Publisher	Data powered by TypesetSpringer Verlag
ISSN	0178515X
Open Access	No