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Advances in Food Enzymology: Development and Application of Enzyme Preparations
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Advances in Food Enzymology: Development and Application of Enzyme Preparations

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

Deadline for manuscript submissions: 31 January 2025 | Viewed by 5802

Special Issue Editor

Dr. Ke Xiong

E-Mail Website
Guest Editor
Beijing Engineering and Technology Research Center of Food Additives, Beijing Technology & Business University (BTBU), No. 33 Fucheng Road, Haidian, Beijing 100048, China
Interests: basic application research of food enzyme preparations; high-throughput screening of enzyme resources; molecular structure and function research of protein peptidases; food safety and nutrition research of grains and oils

Special Issue Information

Dear Colleagues,

The study of food enzymology is one of the principal frontiers of the field of biotechnology in the 21st century. With the ongoing and continued discovery of new enzyme sources and advances in enzyme molecular modification technology, the range of applications for enzyme preparations has further expanded, promising extensive prospects and development potential. Enzyme preparations have become increasingly important in enhancing the texture of food, improving its flavor, and boosting its nutritional value. Additionally, enzyme preparations have significant applications in food analysis and testing, serving as essential tools used to ensure food quality and safety.

This Special Issue invites papers in the following areas:

  • Enzyme engineering technology;
  • Enzyme design and development;
  • Exploring new enzyme sources;
  • New compound enzyme preparation;
  • Specialized enzyme preparation;
  • Enzyme preparation for food processing;
  • Enzyme preparation for food testing.

Dr. Ke Xiong
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

  • enzyme preparations
  • enzyme resources
  • enzyme engineering
  • enzyme molecular design
  • food testing
  • compound enzyme
  • food processing

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

Published Papers (4 papers)

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Research

14 pages, 4414 KiB  
Article
Identification of a Novel Chitinase from Bacillus paralicheniformis: Gene Mining, Sequence Analysis, and Enzymatic Characterization
by Xianwen Ma, Dian Zou, Anying Ji, Cong Jiang, Ziyue Zhao, Xiaoqi Ding, Zongchen Han, Pengfei Bao, Kang Chen, Aimin Ma and Xuetuan Wei
Foods 2024, 13(11), 1777; https://doi.org/10.3390/foods13111777 - 5 Jun 2024
Viewed by 1020
Abstract
In this study, a novel strain for degrading chitin was identified as Bacillus paralicheniformis HL37, and the key chitinase CH1 was firstly mined through recombinant expression in Bacillus amyloliquefaciens HZ12. Subsequently, the sequence composition and catalytic mechanism of CH1 protein were analyzed. The [...] Read more.
In this study, a novel strain for degrading chitin was identified as Bacillus paralicheniformis HL37, and the key chitinase CH1 was firstly mined through recombinant expression in Bacillus amyloliquefaciens HZ12. Subsequently, the sequence composition and catalytic mechanism of CH1 protein were analyzed. The molecular docking indicated that the triplet of Asp526, Asp528, and Glu530 was a catalytic active center. The enzymatic properties analysis revealed that the optimal reaction temperature and pH was 65 °C and 6.0, respectively. Especially, the chitinase activity showed no significant change below 55 °C and it could maintain over 60% activity after exposure to 85 °C for 30 min. Moreover, the optimal host strain and signal peptide were obtained to enhance the expression of chitinase CH1 significantly. As far as we know, it was the first time finding the highly efficient chitin-degrading enzymes in B. paralicheniformis, and detailed explanations were provided on the catalytic mechanism and enzymatic properties on CH1. Full article
(This article belongs to the Special Issue Advances in Food Enzymology: Development and Application of Enzyme Preparations)
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18 pages, 3760 KiB  
Article
Co-Immobilization of Alcalase/Dispase for Production of Selenium-Enriched Peptide from Cardamine violifolia
by Shiyu Zhu, Yuheng Li, Xu Chen, Zhenzhou Zhu, Shuyi Li, Jingxin Song, Zhiqiang Zheng, Xin Cong and Shuiyuan Cheng
Foods 2024, 13(11), 1753; https://doi.org/10.3390/foods13111753 - 3 Jun 2024
Cited by 1 | Viewed by 749
Abstract
Enzymatically derived selenium-enriched peptides from Cardamine violifolia (CV) can serve as valuable selenium supplements. However, the industrial application of free enzyme is impeded by its limited stability and reusability. Herein, this study explores the application of co-immobilized enzymes (Alcalase and Dispase) on amino [...] Read more.
Enzymatically derived selenium-enriched peptides from Cardamine violifolia (CV) can serve as valuable selenium supplements. However, the industrial application of free enzyme is impeded by its limited stability and reusability. Herein, this study explores the application of co-immobilized enzymes (Alcalase and Dispase) on amino resin for hydrolyzing CV proteins to produce selenium-enriched peptides. The successful enzyme immobilization was confirmed through scanning electron microscopy (SEM), energy dispersive X-ray (EDX), and Fourier-transform infrared spectroscopy (FTIR). Co-immobilized enzyme at a mass ratio of 5:1 (Alcalase/Dispase) exhibited the smallest pore size (7.065 nm) and highest activity (41 U/mg), resulting in a high degree of hydrolysis of CV protein (27.2%), which was obviously higher than the case of using free enzymes (20.7%) or immobilized Alcalase (25.8%). In addition, after a month of storage, the co-immobilized enzyme still retained a viability level of 41.93%, showing fairly good stability. Encouragingly, the selenium-enriched peptides from co-immobilized enzyme hydrolysis exhibited uniform distribution of selenium forms, complete amino acid fractions and homogeneous distribution of molecular weight, confirming the practicality of using co-immobilized enzymes for CV protein hydrolysis. Full article
(This article belongs to the Special Issue Advances in Food Enzymology: Development and Application of Enzyme Preparations)
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14 pages, 4501 KiB  
Article
Effective Degradation of Free Gossypol in Defatted Cottonseed Meal by Bacterial Laccases: Performance and Toxicity Analysis
by Liangyu Zhang, Hao Zheng, Xingke Zhang, Xiaoxue Chen, Yanrong Liu, Yu Tang, Wei Zhang, Zhixiang Wang, Lihong Zhao and Yongpeng Guo
Foods 2024, 13(4), 566; https://doi.org/10.3390/foods13040566 - 13 Feb 2024
Cited by 3 | Viewed by 1592
Abstract
Cottonseed meal (CSM) is the major by-product of the cottonseed oil extraction process with high protein content. However, the presence of free gossypol (FG) in CSM severely restricts its utilization in the food and animal feed industries. The development of a biological strategy [...] Read more.
Cottonseed meal (CSM) is the major by-product of the cottonseed oil extraction process with high protein content. However, the presence of free gossypol (FG) in CSM severely restricts its utilization in the food and animal feed industries. The development of a biological strategy for the effective removal of FG in CSM has become an urgent need. In this study, three bacterial laccases including CotA from Bacillus licheniformis, CueO from Escherichia coli, and LcLac from Loigolactobacillus coryniformis were heterologously expressed and investigated for their FG degradation ability. The results showed that CotA laccase displayed the highest FG-degrading capacity among the three laccases, achieving 100% FG degradation at 37 °C and pH 7.0 in 1 h without the addition of a redox mediator. Moreover, in vitro and in vivo studies confirmed that the hepatotoxicity of FG was effectively eliminated after oxidative degradation by CotA laccase. Furthermore, the addition of CotA laccase could achieve 87% to 98% FG degradation in defatted CSM within 2 h. In conclusion, CotA laccase can be developed as an effective biocatalyst for the detoxification of FG in CSM. Full article
(This article belongs to the Special Issue Advances in Food Enzymology: Development and Application of Enzyme Preparations)
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20 pages, 11920 KiB  
Article
Optimization of 4,6-α and 4,3-α-Glucanotransferase Production in Lactococcus lactis and Determination of Their Effects on Some Quality Characteristics of Bakery Products
by Ramazan Tolga Niçin, Duygu Zehir-Şentürk, Busenur Özkan, Yekta Göksungur and Ömer Şimşek
Foods 2024, 13(3), 432; https://doi.org/10.3390/foods13030432 - 29 Jan 2024
Viewed by 1625
Abstract
In this study, the production of 4,6-α (4,6-α-GTase) and 4,3-α-glucanotransferase (4,3-α-GTase), expressed previously in Lactococcus lactis, was optimized and these enzymes were used to investigate glycemic index reduction and staling delay in bakery products. HP–SEC analysis showed that the relevant enzymes were [...] Read more.
In this study, the production of 4,6-α (4,6-α-GTase) and 4,3-α-glucanotransferase (4,3-α-GTase), expressed previously in Lactococcus lactis, was optimized and these enzymes were used to investigate glycemic index reduction and staling delay in bakery products. HP–SEC analysis showed that the relevant enzymes were able to produce oligosaccharides from potato starch or malto-oligosaccharides. Response Surface Methodology (RSM) was used to optimize enzyme synthesis and the highest enzyme activities of 15.63 ± 1.65 and 19.01 ± 1.75 U/mL were obtained at 1% glucose, pH 6, and 30 °C for 4,6-α-GTase and 4,3-α-GTase enzymes, respectively. SEM analysis showed that both enzymes reduced the size of the starch granules. These enzymes were purified by ultrafiltration and used to produce bread and bun at an enzyme activity of 4 U/g, resulting in a decrease in the specific volume of the bread. It was found that the estimated glycemic index (eGI) of bread formulated with 4,6-α-GTase decreased by 18.01%, and the eGI of bread prepared with 4,3-α-GTase decreased by 13.61%, indicating a potential delay in staling. No significant differences were observed in the sensory properties of the bakery products. This is the first study showing that 4,6-α-GTase and 4,3-α-GTase enzymes have potential in increasing health benefits and improving technological aspects regarding bakery products. Full article
(This article belongs to the Special Issue Advances in Food Enzymology: Development and Application of Enzyme Preparations)
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