Microbial Enzymes: Production, Modification and Functions

A special issue of Microorganisms (ISSN 2076-2607). This special issue belongs to the section "Microbial Biotechnology".

Deadline for manuscript submissions: closed (31 May 2023) | Viewed by 2797

Special Issue Editor


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Guest Editor
Institute of Bast Fiber Crops, Chinese Academy of Agricultural Sciences, Changsha 410205, China
Interests: enzymes; cloning; probiotics; biocontrol bacterium; functional proteome; food biotechnology; efficient fermentation
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Special Issue Information

Dear Colleagues,

Microbial enzymes that are mostly derived from different environmental microorganisms have considerable economic potential for applications in agriculture; food, beverages and feed; detergent; textiles; leather; pulp and paper; and pharmaceutical and biomining industries because of their unique properties and adaptation to different environments. The biocatalytic uses for microbial enzymes have grown immensely in recent years since they are ecologically correct, have a high specificity and selectivity, and have a wide diversity of reactions. Moreover, the conditions to obtain and optimize the production of enzymes in terms of nutrients, pH, temperature and aeration are easily controlled in bioreactors. The discovery of novel microbial enzymes, enzyme modification through directed evolution or rational engineering, and the development of economical bioprocesses will accelerate and be possible on an increasingly large scale. Immobilization processes allow for the reuse of these enzymes and increase stability. This Special Issue aims to present recent research advances in microbial enzymes, and the main emphasis is given, but not limited, to new enzyme discovery, catalytic and adaptation mechanisms, and structural analysis. Manuscripts of original research, communications and reviews are all welcome.

Dr. Pengjun Shi
Guest Editor

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Keywords

  • microbial enzyme discovery
  • enzyme characterization and function
  • enzyme production and purification
  • enzymes highly expressed
  • enzyme modification and engineering
  • stability and adaptation mechanism
  • molecular evolution
  • fermentation
  • structure and function
  • bioinformatics
  • biotechnological and industrial application

Published Papers (1 paper)

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Research

15 pages, 4543 KiB  
Article
Enhancing the Catalytic Activity of Glycolate Oxidase from Chlamydomonas reinhardtii through Semi-Rational Design
by Yingting Feng, Shuai Shao, Xueting Zhou, Wan Wei, Xun Liu, Yi Tang, Yuhao Hua, Jianyong Zheng, Yinjun Zhang and Xiangxian Ying
Microorganisms 2023, 11(7), 1689; https://0-doi-org.brum.beds.ac.uk/10.3390/microorganisms11071689 - 28 Jun 2023
Viewed by 1228
Abstract
Glycolate oxidase is a peroxisomal flavoprotein catalyzing the oxidation of glycolate to glyoxylate and plays crucial metabolic roles in green algae, plants, and animals. It could serve as a biocatalyst for enzymatic production of glyoxylate, a fine chemical with a wide variety of [...] Read more.
Glycolate oxidase is a peroxisomal flavoprotein catalyzing the oxidation of glycolate to glyoxylate and plays crucial metabolic roles in green algae, plants, and animals. It could serve as a biocatalyst for enzymatic production of glyoxylate, a fine chemical with a wide variety of applications in perfumery, flavor, and the pharmaceutical and agrochemical industries. However, the low catalytic activity of native glycolate oxidase and low levels of active enzyme in heterologous expression limit its practical use in industrial biocatalysis. Herein, the glycolate oxidase from Chlamydomonas reinhardtii (CreGO) was selected through phylogenetic tree analysis, and its low level of soluble expression in E. coli BL21(DE3) was improved through the use of the glutathione thioltransferase (GST), the choice of the vector pET22b and the optimization of induction conditions. The semi-rational design of the fusion enzyme GST-Gly-Ser-Gly-CreGO led to the superior variant GST-Gly-Ser-Gly-CreGO-Y27S/V111G/V212R with the kcat/Km value of 29.2 s−1·mM−1, which was six times higher than that of the wild type. In contrast to GST-Gly-Ser-Gly-CreGO, 5 mg/mL of crude enzyme GST-Gly-Ser-Gly-CreGO-Y27S/V111G/V212R together with 25 μg/mL of catalase catalyzed the oxidation of 300 mM of methyl glycolate for 8 h, increasing the yield from 50.4 to 93.5%. Full article
(This article belongs to the Special Issue Microbial Enzymes: Production, Modification and Functions)
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