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Enzyme: Mining, Production, Engineering, and Application in Food Industry
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Enzyme: Mining, Production, Engineering, and Application in Food Industry

A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Food Biotechnology".

Deadline for manuscript submissions: closed (20 June 2024) | Viewed by 6942

Special Issue Editor

Dr. Wenjing Cui

E-Mail Website
Guest Editor
School of Biotechnology, Jiangnan University, Wuxi, China
Interests: synthetic biology; protein engineering; bioactive peptides; biosensors

Special Issue Information

Dear Colleagues,

For centuries, enzymes, special products originating from microbes, have played a profound role in food processing, production, and manufacturing owing to the positive impact they have on the high efficiency, specificity, and safety of food production. Recently, "future foods" has emerged as a new focus as people seek healthier foods that are more nutritious, delicious, and sustainable; however, the foods produced along these lines retain problems with texture, nutrition, and flavor. Advances in enzyme technology have enabled the development of new tools and approaches with which to better manipulate food textures and nutritional aspects. Thus, the mining, engineering and heterologous production of food enzymes have hugely expedited both traditional food and future food preparation.

In view of this, the Special Issue is inviting author to submit unpublished original research articles, short communications, and mini-reviews. Submissions should focus on topics, including, but not limited to:

  • Mining the enzymes, especially from microbes, that have been used for or have potential applications in food processing and production.
  • Engineering the enzymes that have been used in traditional food production and future foods, as well as revealing their structure–activity relationship. 
  • Heterologous production of food enzymes in microbial hosts.

Dr. Wenjing Cui
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. Foods is an international peer-reviewed open access semimonthly 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 2900 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

  • food processing
  • food enzymes
  • novel enzyme mining
  • enzyme engineering
  • enzyme application
  • heterologous production of food enzymes
  • proteases
  • carbohydrate degradation-related enzymes
  • food bioactive compound synthesizing-related enzymes
  • structure–activity relationship

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Published Papers (4 papers)

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Research

19 pages, 4799 KiB  
Article
Discovery and Engineering of a Novel Bacterial L-Aspartate α-Decarboxylase for Efficient Bioconversion
by Wenjing Cui, Hao Liu, Yan Ye, Laichuang Han and Zhemin Zhou
Foods 2023, 12(24), 4423; https://doi.org/10.3390/foods12244423 - 10 Dec 2023
Cited by 1 | Viewed by 1271
Abstract
L-aspartate α-decarboxylase (ADC) is a pyruvoyl-dependent decarboxylase that catalyzes the conversion of L-aspartate to β-alanine in the pantothenate pathway. The enzyme has been extensively used in the biosynthesis of β-alanine and D-pantothenic acid. However, the broad application of ADCs is hindered by low [...] Read more.
L-aspartate α-decarboxylase (ADC) is a pyruvoyl-dependent decarboxylase that catalyzes the conversion of L-aspartate to β-alanine in the pantothenate pathway. The enzyme has been extensively used in the biosynthesis of β-alanine and D-pantothenic acid. However, the broad application of ADCs is hindered by low specific activity. To address this issue, we explored 412 sequences and discovered a novel ADC from Corynebacterium jeikeium (CjADC). CjADC exhibited specific activity of 10.7 U/mg and Km of 3.6 mM, which were better than the commonly used ADC from Bacillus subtilis. CjADC was then engineered leveraging structure-guided evolution and generated a mutant, C26V/I88M/Y90F/R3V. The specific activity of the mutant is 28.8 U/mg, which is the highest among the unknown ADCs. Furthermore, the mutant displayed lower Km than the wild-type enzyme. Moreover, we revealed that the introduced mutations increased the structural stability of the mutant by promoting the frequency of hydrogen-bond formation and creating a more hydrophobic region around the active center, thereby facilitating the binding of L-aspartate to the active center and stabilizing the substrate orientation. Finally, the whole-cell bioconversion showed that C26V/I88M/Y90F/R3V completely transformed 1-molar L-aspartate in 12 h and produced 88.6 g/L β-alanine. Our study not only identified a high-performance ADC but also established a research framework for rapidly screening novel enzymes using a protein database. Full article
(This article belongs to the Special Issue Enzyme: Mining, Production, Engineering, and Application in Food Industry)
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13 pages, 3131 KiB  
Article
Enhanced Enzymatic Performance of β-Mannanase Immobilized on Calcium Alginate Beads for the Generation of Mannan Oligosaccharides
by Xinggang Chen, Zhuang Tian, Hongbo Zhou, Guoying Zhou and Haina Cheng
Foods 2023, 12(16), 3089; https://doi.org/10.3390/foods12163089 - 17 Aug 2023
Cited by 2 | Viewed by 1578
Abstract
Mannan oligosaccharides (MOSs) are excellent prebiotics that are usually obtained via the enzymatic hydrolysis of mannan. In order to reduce the cost of preparing MOSs, immobilized enzymes that demonstrate good performance, require simple preparation, and are safe, inexpensive, and reusable must be developed [...] Read more.
Mannan oligosaccharides (MOSs) are excellent prebiotics that are usually obtained via the enzymatic hydrolysis of mannan. In order to reduce the cost of preparing MOSs, immobilized enzymes that demonstrate good performance, require simple preparation, and are safe, inexpensive, and reusable must be developed urgently. In this study, β-mannanase was immobilized on calcium alginate (CaAlg). Under the optimal conditions of 320 U enzyme addition, 1.6% sodium alginate, 2% CaCl2, and 1 h of immobilization time, the immobilization yield reached 68.3%. The optimum temperature and pH for the immobilized β-mannanase (Man-CaAlg) were 75 °C and 6.0, respectively. The Man-CaAlg exhibited better thermal stability, a high degree of pH stability, and less substrate affinity than free β-mannanase. The Man-CaAlg could be reused eight times and retained 70.34% of its activity; additionally, the Man-CaAlg showed 58.17% activity after 30 days of storage. A total of 7.94 mg/mL of MOSs, with 4.94 mg/mL of mannobiose and 3.00 mg/mL of mannotriose, were generated in the oligosaccharide production assay. It is believed that this convenient and safe strategy has great potential in the important field of the use of immobilized β-mannanase for the production of mannan oligosaccharides. Full article
(This article belongs to the Special Issue Enzyme: Mining, Production, Engineering, and Application in Food Industry)
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12 pages, 2795 KiB  
Communication
Highly Efficient Synthesis of Rare Sugars from Glycerol in Endotoxin-Free ClearColi by Fermentation
by Yahui Gao, Zhou Chen, Hideki Nakanishi and Zijie Li
Foods 2023, 12(16), 3078; https://doi.org/10.3390/foods12163078 - 16 Aug 2023
Cited by 1 | Viewed by 1829
Abstract
Rare sugars possess potential applications as low-calorie sweeteners, especially for anti-obesity and anti-diabetes. In this study, a fermentation biosystem based on the “DHAP-dependent aldolases strategy” was established for D-allulose and D-sorbose production from glycerol in endotoxin-free ClearColi BL21 (DE3). Several engineering strategies were [...] Read more.
Rare sugars possess potential applications as low-calorie sweeteners, especially for anti-obesity and anti-diabetes. In this study, a fermentation biosystem based on the “DHAP-dependent aldolases strategy” was established for D-allulose and D-sorbose production from glycerol in endotoxin-free ClearColi BL21 (DE3). Several engineering strategies were adopted to enhance rare sugar production. Firstly, the combination of different plasmids for aldO, rhaD, and yqaB expression was optimized. Then, the artificially constructed ribosomal binding site (RBS) libraries of aldO, rhaD, and yqaB genes were assembled individually and combinatorially. In addition, a peroxidase was overexpressed to eliminate the damage or toxicity from hydrogen peroxide generated by alditol oxidase (AldO). Finally, stepwise improvements in rare sugar synthesis were elevated to 15.01 g/L with a high yield of 0.75 g/g glycerol in a 3 L fermenter. This research enables the effective production of rare sugars from raw glycerol in high yields. Full article
(This article belongs to the Special Issue Enzyme: Mining, Production, Engineering, and Application in Food Industry)
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16 pages, 2668 KiB  
Article
Modification of Ginseng Insoluble Dietary Fiber by Enzymatic Method: Structural, Rheological, Thermal and Functional Properties
by Guihun Jiang, Karna Ramachandraiah, Chaoyi Tan, Nanjie Cai, Kashif Ameer and Xiaoyu Feng
Foods 2023, 12(14), 2809; https://doi.org/10.3390/foods12142809 - 24 Jul 2023
Cited by 8 | Viewed by 1696
Abstract
In this study, the effects of enzymatic modification using cellulase/xylanase on the composition and structural and functional properties of ginseng insoluble dietary fiber (G-IDF) were evaluated. Fourier transform infrared spectroscopy and scanning electron microcopy showed that enzymatic extraction treatment caused obvious structural alterations [...] Read more.
In this study, the effects of enzymatic modification using cellulase/xylanase on the composition and structural and functional properties of ginseng insoluble dietary fiber (G-IDF) were evaluated. Fourier transform infrared spectroscopy and scanning electron microcopy showed that enzymatic extraction treatment caused obvious structural alterations in ginseng-modified (G-MIDF) samples, which exhibited more porous and completely wrinkled surfaces. Comparing the peak morphology of G-MIDF with untreated IDF using X-ray diffractometry, the G-MIDF sample exhibited split peaks at a 2θ angle of 23.71°, along with the emergence of sharp peaks at 28.02°, 31.78°, and 35.07°. Thermo-gravimetric analysis showed that G-MIDF exhibited a specified range of pyrolysis temperature and is suitable for food applications involving processing at temperatures below 300 °C. Overall, it was evident from rheograms that both G-IDF and G-MIDF exhibited a resemblance with respect to viscosity changes as a function of the shear rate. Enzymatic treatment led to significant (p < 0.05) improvement in water holding, oil retention, water swelling, nitrite ion binding, bile acid binding, cholesterol absorption, and glucose absorption capacities. Full article
(This article belongs to the Special Issue Enzyme: Mining, Production, Engineering, and Application in Food Industry)
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