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Enzymes in Food Industry: Fermentation Process, Properties, Rational Design and Applications

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

Deadline for manuscript submissions: closed (30 March 2024) | Viewed by 5153

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Special Issue Editors

Prof. Dr. Fufeng Liu

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Guest Editor

College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, China
Interests: enzyme; functional food; rational design; molecular simulation

Dr. Jingming Zhao

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Guest Editor

Manchester Institute of Biotechnology, University of Manchester, Manchester M1 7DN, UK
Interests: metalloenzymes; biocatalysis; protein engineering; enzyme mechanisms

Special Issue Information

Dear Colleagues,

As common bio-macromolecular catalysts, enzymes are widely used in food preparation for improving the taste and texture of food products. More importantly, enzymes perform a crucial role in producing bioactive compounds, important food ingredients and some new nutritional ingredients, which can improve food quality and function. In this Special Issue, we welcome original research or review manuscripts that cover the utility of free enzymes and/or immobilized enzymes as efficient tools that can be applied to various aspects of the food industry. Specifically, novel enzyme mining, the structure–function relationship of enzymes, and the immobilization and modification of enzymes will be a focus. In addition, the development of novel enzymes for creating new food components and rational design of food enzymes are strongly encouraged.

Prof. Dr. Fufeng Liu
Dr. Jingming Zhao
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. 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 engineering
enzyme
food industry
enzyme activity
enzyme immobilization
biocatalysts
enzymatic modification
enzyme design
food ingredients
functional food
bioactive compounds
enzyme stability
molecular simulation
structure–function relationship

Published Papers (6 papers)

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Research

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17 pages, 2840 KiB

Open AccessArticle

Ultrasound-Assisted Multi-Enzyme Extraction for Highly Efficient Extraction of Polysaccharides from Ulva lactuca

by Wenqian Wang, Jinbi Li, Fuping Lu and Fufeng Liu

Foods 2024, 13(6), 891; https://0-doi-org.brum.beds.ac.uk/10.3390/foods13060891 - 15 Mar 2024

Viewed by 781

Abstract

Ulva polysaccharides present several physiological activities including antiviral, antitumor and anti-plasmodial effects. However, current processing usually results in low yields and high prices, thus lacking commercialization potential. The aim of this study was to develop an efficient method for the extraction of Ulva polysaccharides with high biological activity. The effect of cell wall-degrading enzymes including cellulase, hemicellulase, pectinase and protease on Ulva polysaccharide extraction was studied by statistical mixing design. Using the most effective enzyme preparations as the basic components, the optimal proportions of the enzyme mixture were determined as follows: cellulase 35.3%, pectinase 34.5%, alkaline protease 30.2%, which increased the polysaccharide yield from 6.43% in the absence of enzymes to 26.68%. Subsequently, through response surface analysis, the optimal conditions were determined: enzyme concentration of 1.5%, enzymatic time of 1.1 h, ultrasonic time of 90 min and enzymatic temperature of 60 °C. Under the optimal extraction conditions, the extraction yield of Ulva polysaccharides could be increased to 30.14%. Moreover, extracted polysaccharides exhibit strong antioxidant properties in DPPH, ABTS, hydroxyl radical, superoxide radical and H₂O₂-induced cellular damage models. This study laid a solid foundation for the use and development of Ulva polysaccharides. Full article

(This article belongs to the Special Issue Enzymes in Food Industry: Fermentation Process, Properties, Rational Design and Applications)

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17 pages, 4523 KiB

Open AccessArticle

Immobilization of Enological Pectinase on Magnetic Sensitive Polyamide Microparticles for Wine Clarification

by Sandra Cristina Oliveira, Nadya Vasileva Dencheva and Zlatan Zlatev Denchev

Foods 2024, 13(3), 420; https://0-doi-org.brum.beds.ac.uk/10.3390/foods13030420 - 28 Jan 2024

Viewed by 712

Abstract

The use of free pectinases as clarification biocatalysts constitutes a well-established practice in the large-scale production of various types of wines. However, when in the form of free enzymes, the recovery and reusability of pectinases is difficult if not impossible. To address these limitations, the present study focuses on the noncovalent adsorption immobilization of a commercial pectinolytic preparation onto highly porous polyamide 6 (PA6) microparticles, both with and without magnetic properties, prepared via activated anionic polymerization. The two pectinase complexes resulting after immobilization underwent comparative activity and kinetic studies, contrasting them with the free enzyme preparation. In comparison with the free enzyme, the PA6-immobilized pectinase complexes exhibited more than double the specific activity toward the pectin substrate. They displayed a slightly higher affinity to the substrate while acting as faster catalysts that were more resistant to inhibition. Furthermore, the immobilized complexes were applied in the clarification process of industrial rosé must, whereby they demonstrated accelerated performance as compared with the free enzyme. Moreover, the PA6-immobilized pectinase biocatalysts offered the potential for three consecutive cycles of reuse, achieving complete rosé must clarification within relevant timeframes in the range of 3–36 h. All these results suggest the potential industrial application of the pectinases noncovalently immobilized upon PA6 microparticles. Full article

(This article belongs to the Special Issue Enzymes in Food Industry: Fermentation Process, Properties, Rational Design and Applications)

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16 pages, 2237 KiB

Open AccessArticle

Characterization and Molecular Dynamics Simulation of a Lipase Capable of Improving the Functional Characteristics of an Egg-Yolk-Contaminated Liquid Egg White

by Linlin Xu, Fei Pan, Yingnan Li, Huiqian Liu and Chengtao Wang

Foods 2023, 12(22), 4098; https://0-doi-org.brum.beds.ac.uk/10.3390/foods12224098 - 11 Nov 2023

Viewed by 969

Abstract

Lipase has great application potential in hydrolyzing residual yolk lipid in egg white liquid to restore its functional properties. In this study, a lipase gene from Bacillus subtilis was expressed in E. coli BL21 (DE3) and named Lip-IM. Results showed that although Lip-IM has stronger specificity for medium- and short-chain substrates than long-chain substrates (C16, C18), due to its excellent enzyme activity, it also has strong hydrolysis activity for long-chain substrates and maintained over 80% activity at 4–20 °C, but significantly reduced when the temperature exceeds 40 °C. The addition of 0.5% Lip-IM enhanced foaming ability by 26% (from 475 to 501%) and reduced liquid precipitation rate by 9% (from 57 to 48%). Furthermore, molecular dynamics (MD) simulations were run to investigate the conformational stability of Lip-IM at different temperatures. Results showed that Lip-IM maintained a stable conformation within the temperature range of 277–303 K. Fluctuations in the flexible area and backbone movement of proteins were identified as the main reasons for its poor thermal stability. Full article

(This article belongs to the Special Issue Enzymes in Food Industry: Fermentation Process, Properties, Rational Design and Applications)

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15 pages, 3310 KiB

Open AccessArticle

Directed Modification of a GHF11 Thermostable Xylanase AusM for Enhancing Inhibitory Resistance towards SyXIP-I and Application of AusM^PKK in Bread Making

by Dong Zhang, Jing Huang, Youyi Liu, Xingyi Chen, Tiecheng Gao, Ning Li, Weining Huang and Minchen Wu

Foods 2023, 12(19), 3574; https://0-doi-org.brum.beds.ac.uk/10.3390/foods12193574 - 26 Sep 2023

Viewed by 901

Abstract

To reduce the inhibition sensitivity of a thermoresistant xylanase AusM to xylanase inhibitor protein (XIP)-type in wheat flour, the site-directed mutagenesis was conducted based on the computer-aided redesign. First, fourteen single-site variants and one three-amino acid replacement variant in the thumb region of an AusM-encoding gene (AusM) were constructed and expressed in E. coli BL21(DE3), respectively, as predicted theoretically. At a molar ratio of 100:1 between SyXIP-I/xylanase, the majority of mutants were nearly completely inactivated by the inhibitor SyXIP-I, whereas AusM^N127A retained 62.7% of its initial activity and AusM^PKK retained 100% of its initial activity. The optimal temperature of the best mutant AusM^PKK was 60 °C, as opposed to 60–65 °C for AusM, while it exhibited improved thermostability, retaining approximately 60% of its residual activity after heating at 80 °C for 60 min. Furthermore, AusM^PKK at a dosage of 1000 U/kg was more effective than AusM at 4000 U/kg in increasing specific bread loaf volume and reducing hardness during bread production and storage. Directed evolution of AusM significantly reduces inhibition sensitivity, and the mutant enzyme AusM^PKK is conducive to improving bread quality and extending its shelf life. Full article

(This article belongs to the Special Issue Enzymes in Food Industry: Fermentation Process, Properties, Rational Design and Applications)

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14 pages, 2465 KiB

Open AccessArticle

Improving the Thermostability of Serine Protease PB92 from Bacillus alcalophilus via Site-Directed Mutagenesis Based on Semi-Rational Design

by Huabiao Miao, Xia Xiang, Nanyu Han, Qian Wu and Zunxi Huang

Foods 2023, 12(16), 3081; https://0-doi-org.brum.beds.ac.uk/10.3390/foods12163081 - 16 Aug 2023

Viewed by 971

Abstract

Proteases have been widely employed in many industrial processes. In this work, we aimed to improve the thermostability of the serine protease PB92 from Bacillus alcalophilus to meet the high-temperature requirements of biotechnological treatments. Eight mutation sites (N18, S97-S101, E110, and R143) were identified, and 21 mutants were constructed from B-factor comparison and multiple sequence alignment and expressed via Bacillus subtilis. Among them, fifteen mutants exhibited increased half-life (t_1/2) values at 65 °C (1.13–31.61 times greater than that of the wild type). Based on the composite score of enzyme activity and thermostability, six complex mutants were implemented. The t_1/2 values of these six complex mutants were 2.12–10.05 times greater than that of the wild type at 65 °C. In addition, structural analysis revealed that the increased thermal stability of complex mutants may be related to the formation of additional hydrophobic interactions due to increased hydrophobicity and the decreased flexibility of the structure. In brief, the thermal stability of the complex mutants N18L/R143L/S97A, N18L/R143L/S99L, and N18L/R143L/G100A was increased 4-fold, which reveals application potential in industry. Full article

(This article belongs to the Special Issue Enzymes in Food Industry: Fermentation Process, Properties, Rational Design and Applications)

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Review

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19 pages, 3846 KiB

Open AccessReview

A Critical Review on Immobilized Sucrose Isomerase and Cells for Producing Isomaltulose

by Wenjie Jing, Feihong Hou, Xinming Wu, Mingqiang Zheng, Yue Zheng, Fuping Lu and Fufeng Liu

Foods 2024, 13(8), 1228; https://0-doi-org.brum.beds.ac.uk/10.3390/foods13081228 - 17 Apr 2024

Viewed by 340

Abstract

Isomaltulose is a novel sweetener and is considered healthier than the common sugars, such as sucrose or glucose. It has been internationally recognized as a safe food product and holds vast potential in pharmaceutical and food industries. Sucrose isomerase is commonly used to produce isomaltulose from the substrate sucrose in vitro and in vivo. However, free cells/enzymes were often mixed with the product, making recycling difficult and leading to a significant increase in production costs. Immobilized cells/enzymes have the following advantages including easy separation from products, high stability, and reusability, which can significantly reduce production costs. They are more suitable than free ones for industrial production. Recently, immobilized cells/enzymes have been encapsulated using composite materials to enhance their mechanical strength and reusability and reduce leakage. This review summarizes the advancements made in immobilized cells/enzymes for isomaltulose production in terms of refining traditional approaches and innovating in materials and methods. Moreover, innovations in immobilized enzyme methods include cross-linked enzyme aggregates, nanoflowers, inclusion bodies, and directed affinity immobilization. Material innovations involve nanomaterials, graphene oxide, and so on. These innovations circumvent challenges like the utilization of toxic cross-linking agents and enzyme leakage encountered in traditional methods, thus contributing to enhanced enzyme stability. Full article

(This article belongs to the Special Issue Enzymes in Food Industry: Fermentation Process, Properties, Rational Design and Applications)

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