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Fermentation
Special Issues
Microbial Production of Industrial Enzymes
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Microbial Production of Industrial Enzymes

A special issue of Fermentation (ISSN 2311-5637). This special issue belongs to the section "Industrial Fermentation".

Deadline for manuscript submissions: 31 May 2025 | Viewed by 1769

Special Issue Editor

Prof. Dr. Yihan Liu

E-Mail Website
Guest Editor
College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, China
Interests: biocatalysis; enzyme engineering; fermentation engineering; industrial microbiology
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Enzymes are highly efficient biocatalysts extensively researched for industrial-scale catalysis due to several distinct advantages, including their ability to operate under milder reaction conditions, their exceptional product selectivity, and their lower environmental and physiological toxicities. Today, microbial enzymes are widely used across various industries, including food, pharmaceuticals, feed, detergents, textiles, paper, and leather; however, not all industrial enzymes meet the critical requirements for industrial applications, partly due to their low activity, insufficient stability, and limited yield, which restrict their use in various industries. In recent decades, numerous strategies have been employed to overcome the challenges posed by the limitations of enzymes in the various industry.

The aim of this Special Issue is to publish both innovative research findings and review articles on the microbial production of industrial enzymes. Contributions focusing on the development of novel enzymes are also welcome.

Prof. Dr. Yihan Liu
Guest Editor

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. Fermentation 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 2100 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

  • mining and evolution of enzymes
  • high-level expression of industrial enzymes
  • fermentation process control of enzymes
  • production of industrial enzymes
  • modification of host strains

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

Published Papers (2 papers)

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Research

14 pages, 1558 KiB  
Article
Biocatalytic Potential of a Raoultella terrigena-Derived Lipolytic Enzyme for High-Performance Detergents
by Mfezeko Noxhaka, Nonso E. Nnolim, Lindelwa Mpaka and Uchechukwu U. Nwodo
Fermentation 2025, 11(4), 225; https://doi.org/10.3390/fermentation11040225 - 17 Apr 2025
Viewed by 247
Abstract
Dump sites harbour microorganisms with potential for environmentally friendly industrial applications. This study assessed the lipolytic activity of municipal dumpsite-associated bacteria and evaluated the stability of the most potent isolate’s lipolytic enzyme against laundry detergents. It also examined the crude lipase’s ability to [...] Read more.
Dump sites harbour microorganisms with potential for environmentally friendly industrial applications. This study assessed the lipolytic activity of municipal dumpsite-associated bacteria and evaluated the stability of the most potent isolate’s lipolytic enzyme against laundry detergents. It also examined the crude lipase’s ability to remove stains from cotton fabric. Among twelve bacteria isolated, five demonstrated notable halo zones on tributyrin agar plates. The diameters (mm) were MN38 (11 ± 1.4), MN1310 (8.5 ± 0.7), MN28 (6.5 ± 0.71), MN18 (7.0 ± 1.4), and MN310 (8.15 ± 0.21). Quantitative analysis revealed that MN38 exhibited the highest lipase activity (14.76 ± 0.27 U/mL), while MN1310 showed the lowest (6.40 ± 0.85 U/mL). Nucleotide sequence analysis identified the isolates as Raoultella terrigena veli18 (MN38), Stenotrophomonas maltophilia veli96 (MN1310), Viridibacillus sp. veli10 (MN28), Stenotrophomonas sp. veli19 (MN18), and Klebsiella sp. veli70 (MN310). The crude lipase from R. terrigena veli18 maintained 73.33%, 52.67%, 55.0%, and 54.0% of its original activity after 60 min of exposure to Sunlight, Surf, Maq, and Omo, respectively. Adding crude lipase to enzyme-free laundry detergents significantly enhanced their cleaning efficacy, completely removing oil stains from cotton fabric. This performance of R. terrigena veli18 crude lipase highlights its potential as an effective detergent bio-additive. Full article
(This article belongs to the Special Issue Microbial Production of Industrial Enzymes)
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16 pages, 16734 KiB  
Article
Engineering a Protease K for Efficient Degradation of Wool Scale Layer Using a Substrate Pocket Modification
by Lei Zhao, Xiangyang Ma, Yunan Ding, Kaixin Zheng, Kefen Wang, Fuping Lu and Yihan Liu
Fermentation 2025, 11(2), 51; https://doi.org/10.3390/fermentation11020051 - 22 Jan 2025
Cited by 1 | Viewed by 961
Abstract
The outermost surface of wool is covered by a scale layer, posing challenges to some steps of fabric processing. This layer, primarily composed of keratin, resists degradation by conventional proteases due to its high disulfide bond content. Protease K, an extracellular serine endo-proteinase [...] Read more.
The outermost surface of wool is covered by a scale layer, posing challenges to some steps of fabric processing. This layer, primarily composed of keratin, resists degradation by conventional proteases due to its high disulfide bond content. Protease K, an extracellular serine endo-proteinase derived from Tritirachium album Limber (tPRK), is known for its ability to digest native keratin. However, its limited activity against keratin has restricted its application in wool scale layer treatment. In this study, the substrate-binding pocket of tPRK was engineered, yielding the mutant N162A, which demonstrated an 84% increase in catalytic activity toward keratin. Additionally, the catalytic efficiency (kcat/Km) of N162A on keratin improved by 44.52%. Structural analysis indicated that modifications in the substrate-binding pocket reduced steric hindrance during substrate entry while enhancing substrate binding. Additionally, 3.3 mg/mL of amino acids were released within 6 h, which were catalyzed by N162A, with a 61% increase compared to the native tPRK. Moreover, the N162A variant effectively reduced the scale layer thickness without compromising the tensile strength of the wool, maintaining its mechanical properties. The findings provide a sustainable strategy for the wool industry while broadening the scope of biotechnological applications in the textile sector. Full article
(This article belongs to the Special Issue Microbial Production of Industrial Enzymes)
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