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Microbial pectic transeliminases.

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TLDR
The yields of pectic transeliminases are less than other pectinases, and an improved process for the production of these enzymes is necessary.
Abstract
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.

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Citations
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Journal ArticleDOI

Pectin lyase: A review

TL;DR: This review tries to fill the gap by providing all relevant information exclusively for pectin lyase by covering structural aspects, substrate specificity, molecular biology, biotechnological applications and future prospects of pECTin lyases.

Production of Hydrolytic Depolymerising Pectinases

TL;DR: This review is an overview of the microorganisms, substrates, and type of culture used for PGase production and provides a description about the strategies used to enhance the production of PGases.
Journal ArticleDOI

Yeasts: An attractive source of pectinases—From gene expression to potential applications: A review

TL;DR: The classification of pectinases and the methods of detecting pectolytic activity are described, focusing primarily on widely studied yeasts such as Saccharomyces and Kluyveromyces but also touching on yeasts living in extreme environments.
Journal ArticleDOI

Plant cell wall degradation by saprophytic Bacillus subtilis strains: gene clusters responsible for rhamnogalacturonan depolymerization.

TL;DR: The degradation system of rhamnogalacturonan type I (RG-I), a component of pectin from the plant cell wall, is shown in B. subtilis strain 168, the first report on the bacterial system for complete RG-I main chain degradation in plant-pathogenic fungus Aspergillus aculeatus.
Journal ArticleDOI

Purification and characterization of an alkaline pectin lyase from Aspergillus flavus

TL;DR: An alkaline pectin lyase secreted by Aspergillus flavus MTCC 7589 was purified to electrophoretic homogeneity using ammonium sulphate fractionation, anion exchange chromatography on DEAE cellulose and gel filtration chromatography in order to show efficacy in retting of Crotalaria juncea fibers.
References
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Journal ArticleDOI

Applications of pectinases in the commercial sector: a review.

TL;DR: This review discusses various types of pectinases and their applications in the commercial sector.
Journal ArticleDOI

Microbial alkaline pectinases and their industrial applications: a review.

TL;DR: The present review features the potential applications and uses of microbial alkaline pectinases, the nature of pECTin, and the vast range of pectinolytic enzymes that function to mineralize pectic substances present in the environment to explore the potential of these enzymes and to encourage new alkalinepectinase-based industrial technology.
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Industrial applications of pectic enzymes: a review

TL;DR: In this article, a review of the benefits brought to the field by these new technologies and their potential for commercial applications is presented. But it is only recently that technological innovations, such as the use of immobilization supports and continuous-flow systems, have been considered to optimize these fruit processing procedures.
Journal ArticleDOI

Advantages of fungal enzyme production in solid state over liquid fermentation systems

TL;DR: A reaction–diffusion model is presented to try to explain why enzyme production in solid-state fermentation (SSF) is higher than in submerged fermentation (SmF) based on micrographic measurements of mycelial aggregates for each kind of fermentation system.
Journal ArticleDOI

Purification and biochemical properties of microbial pectinases—a review

TL;DR: This short review highlights progress on purification and understanding the biochemical aspects of microbial pectinases.
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