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Processes
Special Issues
Advances in Enzyme Biotechnology and Applications in Industry and Environment
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Advances in Enzyme Biotechnology and Applications in Industry and Environment

A special issue of Processes (ISSN 2227-9717). This special issue belongs to the section "Chemical Processes and Systems".

Deadline for manuscript submissions: 20 November 2024 | Viewed by 1980

Special Issue Editors

Prof. Dr. Jianguo Liu

E-Mail Website
Guest Editor
College of Chemistry and Chemical Engineering, China University of Petroleum (East China), Qingdao 266580, China
Interests: enzyme engineering; bioseparation; biocatalysis
Dr. Xingcui Guo

E-Mail Website
Guest Editor
Qingdao Institute of Bioenergy and Biorocess Technology, Chinese Academy of Sciences, Qingdao 266104, China
Interests: bio-based chemicals; green chemistry; biocatalysis

Special Issue Information

Dear Colleagues,

Biotechnology is one of the most promising technologies of our times, and enzyme engineering is an important part of biotechnology. As a biocatalyst, enzymes ave the characteristics of strong specificity, high catalytic efficiency, excellent stereoselectivity, mild reaction conditions, and simple operation. Presently, enzymes are widely used in fields such as food, brewing, textiles, pharmaceuticals, petrochemicals, and the environment. It can improve product quality, reduce labor intensity, save raw materials and energy, protect the environment, and generate huge economic and social benefits. 

This Special Issue on “Advances in Enzyme Biotechnology and Applications in Industry and Environment” seeks high-quality works, focusing on the latest progress and applications of enzyme biotechnology. Topics include, but are not limited to, the following:

  • Expression, purification, and characterization of enzymes;
  • Mutation and immobilization of enzymes;
  • Chemical modification of enzymes;
  • Optimization of enzyme catalysis process;
  • Application of enzymes in industry and the environment. 

Prof. Dr. Jianguo Liu
Dr. Xingcui Guo
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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. Processes is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2400 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • expression
  • purification
  • characterization
  • immobilization
  • mutagenesis
  • enzymic catalysis
  • application

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Further information on MDPI's Special Issue polices can be found here.

Published Papers (2 papers)

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Research

15 pages, 7025 KiB  
Article
Expression, Characterization, and Immobilization of a Novel D-Lactate Dehydrogenase from Salinispirillum sp. LH 10-3-1
by Jianguo Liu, Xuejiao Jiang, Yaru Zheng, Kaixuan Li, Ruixin Zhang, Jingping Xu, Zhe Wang, Yuxuan Zhang, Haoran Yin and Jing Li
Processes 2024, 12(7), 1349; https://doi.org/10.3390/pr12071349 - 28 Jun 2024
Viewed by 487
Abstract
Salinispirillum sp. LH 10-3-1 was newly isolated from the alkali lake water samples collected in Inner Mongolia. In this study, a gene coding for D-lactate dehydrogenase from the strain LH 10-3-1 (SaLDH) was cloned and characterized. The recombinant enzyme was a [...] Read more.
Salinispirillum sp. LH 10-3-1 was newly isolated from the alkali lake water samples collected in Inner Mongolia. In this study, a gene coding for D-lactate dehydrogenase from the strain LH 10-3-1 (SaLDH) was cloned and characterized. The recombinant enzyme was a tetramer with a native molecular mass of 146.2 kDa. The optimal conditions for SaLDH to reduce pyruvate and oxidize D-lactic acid were pH 8.0 and pH 5.0, at 25 °C. Cu2+ and Ca2+ slightly promoted the oxidation and reduction activities of SaLDH, respectively. To improve the stability of SaLDH, the enzyme was immobilized on Cu3(PO4)2-based inorganic hybrid nanoflowers. The results showed that the reduction activity of the hybrid nanoflowers disappeared, and the optimum temperature, specific activity, thermostability, and storage stability of the immobilized SaLDH were significantly improved. In addition, the biotransformation of D-lactic acid to pyruvate catalyzed by SaLDH and the hybrid nanoflowers was investigated. The maximum conversion of D-lactic acid catalyzed by the immobilized SaLDH was 25.7% higher than by free enzymes, and the immobilized SaLDH could maintain 84% of its initial activity after six cycles. Full article
(This article belongs to the Special Issue Advances in Enzyme Biotechnology and Applications in Industry and Environment)
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15 pages, 5800 KiB  
Article
Enhancing Alkaline Protease Stability through Enzyme-Catalyzed Crosslinking and Its Application in Detergents
by Haichuan Yang, Xiankun Ren, Yating Zhao, Tengjiao Xu, Jing Xiao and Hao Chen
Processes 2024, 12(3), 624; https://doi.org/10.3390/pr12030624 - 21 Mar 2024
Viewed by 1173
Abstract
Enzymatic additives, particularly alkaline proteases, play a crucial role in enhancing detergent effectiveness against protein-based stains. Despite advancements in enzyme stabilization techniques, there is a need for innovative strategies to further improve protease stability in laundry detergents. However, research exploring the utilization of [...] Read more.
Enzymatic additives, particularly alkaline proteases, play a crucial role in enhancing detergent effectiveness against protein-based stains. Despite advancements in enzyme stabilization techniques, there is a need for innovative strategies to further improve protease stability in laundry detergents. However, research exploring the utilization of substrate imprinting technology to achieve this objective remains limited. Therefore, this study aims to enhance the stability of alkaline proteases in laundry detergents by employing casein as an imprinting substrate and utilizing transglutaminase-mediated (TGase) crosslinking to modify proteases 102 and 306. The optimal temperature, pH, and thermal stability of the modified alkaline proteases 102 and 306 showed no significant changes. However, these two modified alkaline proteases exhibited varying degrees of improvement in stability among the 14 detergent additives tested. Under 40 °C incubation for 24 h, the relative enzyme activity of modified alkaline protease 102 increased approximately 1.4–15-fold in AEO-9, BS-12, CMI, APG, FMEE, and SOE, while the relative enzyme activity of modified alkaline protease 306 increased approximately 1.2–3.7-fold across different additives (FMEE, AEO-9, BS-12, SOE, FAA, and AEC-9Na). These modified proteases demonstrated improved stability and wider applicability across commercial detergent formulations available. Integrated into standard laundry detergent at a 1:7 ratio before and after modification, they effectively removed protein stains from the cotton fabric after 24 h of 40 °C incubation. These findings provide insights into more effective stain-removal techniques. Full article
(This article belongs to the Special Issue Advances in Enzyme Biotechnology and Applications in Industry and Environment)
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