Origins and features of pectate lyases and their applications in industry.

Calcium ion Optimal pH Optimal temperature Pectate lyase Protein structure Textile industry

Journal

Applied microbiology and biotechnology
ISSN: 1432-0614
Titre abrégé: Appl Microbiol Biotechnol
Pays: Germany
ID NLM: 8406612

Informations de publication

Date de publication:
Sep 2020
Historique:
received: 12 05 2020
accepted: 02 07 2020
revised: 12 05 2020
pubmed: 16 7 2020
medline: 15 5 2021
entrez: 16 7 2020
Statut: ppublish

Résumé

Pectate lyase treatment can be an alternative strategy of the chemical processing, which causes severe environmental pollution, and has been broadly studied and applied for diverse industrial applications including textile industry, beverage industry, pulp processing, pectic wastewater pretreatment, and oil extraction. This review gave a brief description of the origins, enzymatic characterizations, structure, and applications of pectate lyases (Pels). Most of the reported pectate lyases are originated from microorganisms with a small number of them from plants and animals. Due to the diverse environments that these microorganisms exist, Pels present diversified features, especially for the range of optimal pH and temperature. The diversified biochemical properties of Pels define their applications in different industries, and the applications of alkaline Pels on cotton bioscouring and ramie degumming in textile industry were focused in this review. This review also discussed the perspectives of the development and applications of Pels. KEY POINTS: • The first review on pectate lyase focusing on biotechnological applications. • Origins, features, structures, applications of pectate lyases reviewed. • Applications of alkaline Pels in textile industry demonstrated. • Perspectives on future development and applications of Pels discussed.

Identifiants

pubmed: 32666183
doi: 10.1007/s00253-020-10769-8
pii: 10.1007/s00253-020-10769-8
doi:

Substances chimiques

Pectins 89NA02M4RX
Polysaccharide-Lyases EC 4.2.2.-
pectate lyase EC 4.2.2.2
polygalacturonic acid VV3XD4CL04

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

7247-7260

Subventions

Organisme : Natural Science Foundation of Hubei Province
ID : 2018CFB319
Organisme : Hubei Technological Innovation Special Fund
ID : 2017ACA171

Auteurs

Pan Wu (P)

State Key Laboratory of Biocatalysis and Enzyme Engineering, Hubei Collaborative Innovation Center for Green Transformation of Bio-Resources, School of Life Sciences, Hubei University, Wuhan, 430062, China.
Wuhan Sunhy Biology Co., Ltd., Wuhan, 430206, China.

Shihui Yang (S)

State Key Laboratory of Biocatalysis and Enzyme Engineering, Hubei Collaborative Innovation Center for Green Transformation of Bio-Resources, School of Life Sciences, Hubei University, Wuhan, 430062, China.

Zhichun Zhan (Z)

Wuhan Sunhy Biology Co., Ltd., Wuhan, 430206, China.

Guimin Zhang (G)

State Key Laboratory of Biocatalysis and Enzyme Engineering, Hubei Collaborative Innovation Center for Green Transformation of Bio-Resources, School of Life Sciences, Hubei University, Wuhan, 430062, China. zhangguimin@hubu.edu.cn.

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