Structural and Biochemical Properties of Pectinases
01 Jan 2007-pp 99-115
TL;DR: Pectin and other pectic substances are complex polysaccharides, which contribute firmness and structure to plant tissues as a part of the middle lamella as mentioned in this paper.
Abstract: 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 ( -D-galacturonic acid). Pectic substances are classified into two types; homogalacturonan and heterogalacturonan (rhamnogalacturonan). In homogalacturonan, the main polymer chain consists of -D-galacturonate units linked by 1 → 4 glycosidic bonds, whereas in rhamnogalacturonan, the primary chain consist of 1→ 4 linked -D-glacturonates and with about 2–4% L-rhamnose units that are 1→ 2 and 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 60–70% 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
Citations
More filters
TL;DR: A comprehensive review of various aspects on processing, preservation and value addition to the cashew apple is presented in this article, where a wide variety of methods ranging from chemical preservatives to high pressure processing have been evaluated for the improvement of shelf life.
64 citations
TL;DR: The role of different hydrolytic enzymes is important to the biobased refinery as mentioned in this paper, and the application of the advanced biotechnological approach can help in the development of a consolidated bioprocessing approach.
59 citations
TL;DR: Cold active pectinases derived from cold-adapted microorganisms, are known to function at low to freezing temperatures and may be an alternative to address the problem of low-temperature processing.
Abstract: Pectinase has been an integral part of commercial food processing, where it is used for degradation of pectin and facilitates different processing steps such as liquefaction, clarification and juice extraction. The industry currently uses pectinases from mesophilic or thermophilic microorganisms which are well established, but recently, there has been is a new trend in the food industry to adopt low-temperature processing. This trend is due to the potential economic and environmental advantages which the industry envisages. In order to achieve this change, an alternative for the existing pectinases, which are mostly mesophilic and temperature-dependent, must be identified, which can function efficiently at low temperatures. Psychrophilic pectinases derived from cold-adapted microorganisms, are known to function at low to freezing temperatures and may be an alternative to address the problem. Psychrophilic pectinases can be obtained from the vast microflora inhabiting various cold regions on earth such as oceans, Polar Regions, snow-covered mountains, and glaciers. This article is intended to study the advantages of cold active pectinases, its sources, and the current state of the research.
58 citations
Cites background from "Structural and Biochemical Properti..."
...Pectatelyase has a mass of ~30–40 kDa and has a parallel β-helix domain that is formed by parallel strands which fold into a large right-handed helix and a major loop region [38, 39]....
[...]
TL;DR: In this paper, a review of the recent advancements in the field of pectinases is presented, focusing on the use of natural as well as recombinant microbial sources, metagenomic approaches, metabolic engineering, site directed mutagenesis and media engineering techniques.
Abstract: The wide utility and catalytic efficiency of microbial pectinase in various industries has greatly increased its global demand. Among the natural sources of pectinases, microbial pectinases are used frequently for its ease of production and unique physicochemical properties. Yet similar to other industrial enzymes, pectinases also face the constraint of thermo-tolerance and low yield in its economised production. The current review addresses the various strategies adopted to meet the high yield and thermo-tolerance of pectinases as well as the various attempts made in the field of pectinases to its improved production and better catalytic efficiency. The utilisation of natural as well as recombinant microbial sources, metagenomic approaches, metabolic engineering, site directed mutagenesis and media engineering techniques adopted in the field of pectinases have been discussed. The significance of pectinases in various industries is depicted by enlisting its applications. To the best our knowledge the current review is unique being the first attempt to compile the recent advancements in the field of pectinases.
52 citations
Cites background from "Structural and Biochemical Properti..."
...A critical study on the various reviews on pectinases indicate different aspects of this group of enzymes such as its structural–functional characteristics (Gummadi et al. 2007), purification (Gummadi and Panda 2003), applications (Khan et al. 2013; Pedrolli et al. 2009; Sharma et al. 2013) etc....
[...]
TL;DR: Various production methods related to the optimization of the product and its significant contribution to the pharmaceutical industry (either pectinase or derived pectic substances) are described in this article.
Abstract: Both pectin and pectinase are vitally imperative biomolecules in the biotechnological sector. These molecules are a feasible non-toxic contrivance of nature with extensive applicative perception. Understanding pectic substances and their structure, unique depolymerization, and biochemical properties such as a catalytic mechanism and the strong interrelationship among these molecules could immensely enhance their applicability in industries. For instance, gaining knowledge with respect to the versatile molecular heterogeneity of the compounds could be considered as the center of concern to resolve the industrial issues from multiple aspects. In the present review, an effort has been made to orchestrate the fundamental information related to structure, depolymerization characteristics, and classification of pectin as well as the types and biochemical properties of pectinase. Furthermore, various production methods related to the optimization of the product and its significant contribution to the pharmaceutical industry (either pectinase or derived pectic substances) are described in this article.
43 citations
References
More filters
TL;DR: This review discusses various types of pectinases and their applications in the commercial sector.
1,001 citations
"Structural and Biochemical Properti..." refers background in this paper
...Industrial applications of pectinases have been reviewed by different authors ( Kashyap et al., 2001; Hoondal et al., 2002; Naidu and Panda, 1998a; Gummadi and Panda, 2003; Gummadi and Kumar, 2005)....
[...]
Book•
01 Jun 1985
TL;DR: This book discussesFermented Protein Foods in the Orient: Shoyu and Miso in Japan, and potential Infective and Toxic Microbiological Hazards Associated with the Consumption of Fermented Foods.
Abstract: Vinegar. The Microbiology of Vegetable Fermentations. The Silage Fermentation. Fermentative Upgrading of Wastes for Animal Feeding. Cocoa, Coffee and Tea. Thickeners of Microbial Origin. Bread and Baker's Yeast . Sourdough Breads and Related Products. The Microbiology of Alcoholic Beverages. Cheeses. Fermented Milks. Fermented Protein Foods in the Orient: Shoyu and Miso in Japan. Fermented Fish and Fish Products. Fermented Sausages. Protein-rich Foods Based on Fermented Vegetables. Food Flavour from Yeast. Biology and Technology of Mushroom Culture. Algae as Food . Bio-Enrichment of Fermented Foods: Production of Vitamins in Fermented Foods. Production of Industrial Enzymes and Some Applications in Fermented Foods . Koji. Food Fermentation in the Tropics. African Fermented Foods. Fermented Foods of the Indian Sub-Continent. Fermented Weaning Foods. Potential Infective and Toxic Microbiological Hazards Associated with the Consumption of Fermented Foods. The Impact of Genetic Engineering on Food and Beverage Fermentations. Index
792 citations
01 Jan 1999
790 citations
"Structural and Biochemical Properti..." refers background in this paper
...Both belong to different families of polysaccharide lyases in the carbohydrate-active enzymes (CAZY) classification ( Coutinho and Henrissat, 1999, http://afmb.cnrs-mrs.fr/CAZY/)....
[...]
Book•
17 Dec 1999
TL;DR: Structure and Synthesis of Carbohydrates and Carbohydrate Analogues Post-transitional Glycosylation of Proteins Biochemistry of Carbohydrate Modifying Enzymes Structure and Function of Non-Catalytic Modules Industrial Exploitation of Carb carbohydrate Modifying enzymes Engineering Carbohydrate modifying EnZymes Subject Index.
Abstract: Structure and Synthesis of Carbohydrates and Carbohydrate Analogues Post-transitional Glycosylation of Proteins Biochemistry of Carbohydrate Modifying Enzymes Structure of the Catalytic Domains of Carbohydrate Modifying Enzymes Structure and Function of Non-Catalytic Modules Industrial Exploitation of Carbohydrate Modifying Enzymes Engineering Carbohydrate Modifying Enzymes Subject Index.
580 citations
TL;DR: Results indicate that the Bcpg1 gene, encoding endopolygalacturonase, is required for full virulence in B. cinerea.
Abstract: Botrytis cinerea, a fungus that causes diseases in over 200 plant species, secretes a number of endopolygalacturonases that have been suggested to be involved in pathogenesis. However, so far the corresponding genes have not been isolated from this fungus. We cloned Bcpg1, encoding endopolygalacturonase, with the pgaII gene from Aspergillus niger as a heterologous probe. The Bcpg1gene is expressed to similar levels in liquid cultures of B. cinerea containing either 1% polygalacturonic acid or 1% sucrose, and is expressed during infection of tomato leaves. The Bcpg1 gene was eliminated by partial gene replacement, and the resulting mutants were tested for virulence on tomato leaves and fruits, as well as on apple fruits. Although the mutants were still pathogenic and displayed similar primary infections when compared with control strains, a significant decrease in secondary infection, i.e., growth of the lesion beyond the inoculation spot, was observed on all three host tissues. These results indicate that...
520 citations