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Fermentation
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Enzymes, Biocatalysis and Biosynthesis
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Enzymes, Biocatalysis and Biosynthesis

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

Deadline for manuscript submissions: 12 May 2024 | Viewed by 2111

Special Issue Editor

Dr. Jinyong Yan

E-Mail Website
Guest Editor
Key Laboratory of Molecular Biophysics, The Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Luoyu Road 1037, Wuhan 430074, China
Interests: enzyme; metabolic engineering; synthetic biology; biocatalysis; microbial cell factory

Special Issue Information

Dear Colleagues,

Concerns regarding petroleum depletion and global climate change have driven a switch from the current fossil fuel refinery economy to a sustainable and renewable biorefinery economy. For the sustainable development of a social economy, clean and promising biorefinery and bioeconomy are essential; under this model, renewable resources are used to replace fossil resources, and clean biological processes are used to replace traditional chemical processes.

The use of genetic engineering, metabolic engineering and synthetic biology technologies to engineer enzymes, pathways, microbial chassis and bioprocesses is an important research direction in biomanufacturing. In contrast to chemical conversions, in vitro enzymatic biotransformations and in vivo microbial biosynthesis are characterized by being environmentally friendly and sustainable. However, highly active and stable enzymes, highly efficient pathways and highly robust microbial cell factories are still limited. Engineered enzymes, pathways and microbial cell factories with satisfactory properties are urgently needed to improve biomanufacturing processes.

The goal of this Special Issue is to publish recent innovative research and review papers on enzyme overexpression in microbial systems, biocatalyst preparation and biocatalytic processes, metabolic engineering and synthetic biology approaches for the production of value-added chemicals, and other related topics.

Sincerely,

Dr. Jinyong Yan
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 2600 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

  • enzyme
  • metabolic engineering
  • synthetic biology
  • biotransformation
  • biocatalysis
  • microbial cell factory
  • biocatalyst
  • high-value product

Published Papers (2 papers)

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Research

15 pages, 3585 KiB  
Article
Biochemical Characterization of a Novel Alkaline-Tolerant Xaa-Pro Dipeptidase from Aspergillus phoenicis
by Zixing Dong, Shuangshuang Yang, Kun Zhang, Cunduo Tang, Yunchao Kan and Lunguang Yao
Fermentation 2023, 9(11), 978; https://doi.org/10.3390/fermentation9110978 - 15 Nov 2023
Cited by 1 | Viewed by 922
Abstract
Xaa-Pro dipeptidase (XPD, EC 3.4.13.9; also known as prolidase) catalyzes the hydrolysis of the iminopeptide bond in the trans-Xaa-Pro dipeptides (Xaa represents any amino acid except proline), which makes it find wide applications in food, medical and environmental protection fields. In the present [...] Read more.
Xaa-Pro dipeptidase (XPD, EC 3.4.13.9; also known as prolidase) catalyzes the hydrolysis of the iminopeptide bond in the trans-Xaa-Pro dipeptides (Xaa represents any amino acid except proline), which makes it find wide applications in food, medical and environmental protection fields. In the present study, a novel Xaa-Pro dipeptidase from Aspergillus phoenicis ATCC 14332 (ApXPD) was heterologously expressed and biochemically characterized. Reclassification based on phylogenetic analysis and the version 12.5 MEROPS database showed that this enzyme was the only fungal XPD in the unassigned subfamily that shared the highest sequence identity with Xanthomonas campestris prolidase but not with that from the more related fungal species A. niudulans. As compared with other prolidases, ApXPD also contained a long N-terminal tail (residues 1–63) and an additional region (PAPARLREKL) and used a different arginine residue for dipeptide selectivity. After heterologous expression and partial purification, recombinant ApXPD was highly active and stable over the alkaline range from 8.5 to 10.0, with maximum activity at pH 9.0 and more than 80% activity retained after 1 h incubation at pHs of 8.5–10.0 (55 °C). It also had an apparent optimum temperature of 55 °C and remained stable at 20–30 °C. Moreover, this enzyme was a cobalt-dependent prolidase that only cleaved dipeptides Lys-Pro, Gly-Pro, and Ala-Pro rather than other dipeptides, tripeptides, and tetrapeptides. All these distinct features make A. phoenicis ATCC 14332 XPD unique among currently known prolidases, thus defining a novel Xaa-Pro dipeptidase subfamily. Full article
(This article belongs to the Special Issue Enzymes, Biocatalysis and Biosynthesis)
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17 pages, 1078 KiB  
Article
Optimization of Alkaline Hydrogen Peroxide Pretreatment and Enzymatic Hydrolysis of Wheat Straw for Enhancing Sugar Yields
by Hui Zhang and Junhui Wu
Fermentation 2023, 9(10), 871; https://doi.org/10.3390/fermentation9100871 - 27 Sep 2023
Viewed by 808
Abstract
Optimization of alkaline hydrogen peroxide (AHP) pretreatment and enzymatic hydrolysis of wheat straw (WS) was carried out to enhance fermentable sugar yields with the use of glucose and xylose yields from the pretreated WS as responses. In the first step, variables including temperature, [...] Read more.
Optimization of alkaline hydrogen peroxide (AHP) pretreatment and enzymatic hydrolysis of wheat straw (WS) was carried out to enhance fermentable sugar yields with the use of glucose and xylose yields from the pretreated WS as responses. In the first step, variables including temperature, hydrogen peroxide concentration and time during pretreatment were detected to have significant effects on the sugar yields. The results indicate that maximal sugar yields could be obtained while the WS was pretreated using 71 g/L hydrogen peroxide solution with 200 g/L of solid loading at 50 °C for 7.6 h. The corresponding cellulose recovery, hemicellulose recovery and lignin removal were 97.5%, 84.3% and 75.0%, respectively. In the second step, enzymatic hydrolysis of the pretreated WS was optimized. The results show that the reaction time, enzyme loading and biomass loading during enzymatic hydrolysis also had significant effects on the sugar yields. The final maximum yields of glucose (552.7 mg/gds (mg/g dry substrate)) and xylose (223.6 mg/gds) could be obtained while enzymatic hydrolysis was carried out at 50 °C for 37.0 h using 10.8 FPU/gds (filter paper activity unit per gram dry substrate) of enzyme loading, 88 g/L of biomass loading and 0.3% (w/v) of Tween-80. The corresponding cellulose conversion and hemicellulose conversion were 94.0% and 83.5%, respectively. Full article
(This article belongs to the Special Issue Enzymes, Biocatalysis and Biosynthesis)
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