Advances in Enzyme Engineering, Biocatalysis and Biosynthesis, 2nd Edition

A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Biocatalysis".

Deadline for manuscript submissions: closed (31 August 2024) | Viewed by 1030

Special Issue Editor


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Guest Editor
The Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, China
Interests: protein engineering; enzyme engineering; multienzyme cascade reaction; synthesis of food and pharmaceutical by biocatalysis
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Special Issue Information

Dear Colleagues,

This Special Issue is a continuation of a previous successful Special Issue, “Advances in Enzyme Engineering, Biocatalysis and Biosynthesis”.

Enzyme engineering is a vital, modern biotechnology with which to fine tune enzymes. As a new advanced technology, it greatly promotes the development of life and industry. Enzyme engineering strategies not only include natural enzyme mining, heterologous expression, directed evolution, gene shuffling or family shuffling, enzyme immobilization, and synzymes, but also rational design based on structure–function insights, computational methods, and machine learning, as well as novel scaffolding and compartmentalization techniques to improve the performance of multienzyme systems. Efficient enzyme engineering strategies improve enzymatic properties, such as activity, specificity, stability, and stereoselectivity, as well as balancing sequential reactions and route intermediates by co-localizing multiple enzymes. This will facilitate the application of biocatalysis and biosynthesis in the food, pharmaceutical, and chemical fields, as well as accelerate the development of a green biological manufacturing industry.

Therefore, for this Special Issue, we are interested in presenting the most recent progress in advances in enzyme engineering, biocatalysis, and biosynthesis. Fundamental studies with which to establish innovative and efficient enzyme engineering strategies, as well as studies related to the development of biocatalysis and biosynthesis processes applied to industries, are welcome.

It is with great pleasure and honor that we invite you to submit a review article or original research paper for possible publication in this Special Issue.

Prof. Dr. Ruizhi Han
Guest Editor

Manuscript Submission Information

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Catalysts is an international peer-reviewed open access monthly journal published by MDPI.

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Keywords

  • enzyme engineering
  • protein engineering
  • biocatalysis
  • biosynthesis

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Published Papers (1 paper)

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Research

12 pages, 5537 KiB  
Article
Engineering of Cyclodextrin Glucosyltransferase from Paenibacillus macerans for Improved Regioselectivity and Product Specificity Toward Hydroxyflavone Glycosylation
by Jin Wang, Binhao Wang, Jieyu Zhou, Jinjun Dong, Ye Ni and Ruizhi Han
Catalysts 2025, 15(2), 120; https://doi.org/10.3390/catal15020120 - 26 Jan 2025
Viewed by 649
Abstract
The regioselective glycosylation and product specificity of hydroxyflavonoid compounds profoundly influences their biological activity and stability, offering significant therapeutic potential. However, most cyclodextrin glucosyltransferases (CGTases) inherently lack regioselectivity and product specificity for flavone glycosylation. Herein, a CGTase from Paenibacillus macerans was engineered for [...] Read more.
The regioselective glycosylation and product specificity of hydroxyflavonoid compounds profoundly influences their biological activity and stability, offering significant therapeutic potential. However, most cyclodextrin glucosyltransferases (CGTases) inherently lack regioselectivity and product specificity for flavone glycosylation. Herein, a CGTase from Paenibacillus macerans was engineered for enhanced glycosylation regioselectivity and product specificity by combining molecular docking analysis and saturation mutagenesis strategies. K232L (favoring 4′-and 6-hydroxyflavones) and K232V (favoring 7-hydroxyflavone) were identified with distinct preferences. In addition, H233Y (preferring for 4′-hydroxyflavones), H233T (preferring for 6′-hydroxyflavones), and H233K (preferring for 7′-hydroxyflavones) also demonstrated distinct regioselectivity. These variants further exhibited enhanced hydrolytic activity, enabling the efficient production of short sugar-chain glycosides. Molecular dynamics (MDs) simulations revealed that the variants adopted optimized catalytic conformations with increased loop region flexibility near the binding pocket, enhancing substrate accessibility. These findings underscore the pivotal roles of K232 and H233 in broadening the substrate scope of CGTase and offer valuable guidance for enzyme engineering targeting regioselective glycosylation. Full article
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