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Enzymes in Food Bioprocessing—Novel Food Enzymes, Applications, and Related Techniques

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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 (10 November 2023) | Viewed by 11145

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Special Issue Editor

Prof. Dr. Xianghui Qi

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Guest Editor

School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China.
Interests: food enzyme; food bioprocessing; enzymatic catalysis; rational enzyme engineering; directed evolution; enzyme immobilization; enzyme techniques

Special Issue Information

Dear Colleagues,

Enzyme-based food bioprocessing has emerged as an attractive technology that offers an efficient, safe, and eco-friendly alternative to conventional food processing. In fact, enzymatic bioprocessing is widely used to produce or process various foods, such as dairy products, baked goods, beverages and brewing, fats and oils, meats, functional foods, and food additives. A variety of enzymes are used in food bioprocessing, including proteases, amylases, glycoside hydrolases, lipases, transglutaminases, and so on. Interest in using enzymes for food processing has continued to grow as new enzyme-related techniques have emerged to better suit the diverse food processing environments and enable the development of new food products. Furthermore, with advances in the rational, evolutionary and microenvironmental engineering of proteins, there has been a significant improvement in enzyme performance, with their improved stability to temperatures, pH, and organic solvents, and more controlled use in food bioprocessing. To sum up, combined with enzyme engineering, novel food enzymes would play a more efficient role in promoting the development of food processing industries.

We are pleased to announce the launch of a Special Issue of Foods on the theme “Enzymes in Food Bioprocessing—Novel Food Enzymes, Applications, and Related Techniques”, and invite you to contribute.

This Special Issue aims to provide a platform for practitioners and researchers in food bioprocessing to communicate and discuss their experiences and research outcomes in order to advance the application of novel enzymes and related technologies in the food industry. In this Special issue, original research articles and reviews are welcome. Research areas may include (but are not limited to) the following:

Novel food enzymes and their application in food processing.
Advanced tools and technologies in enzymatic food processing.
Enzymatic catalysis and reaction kinetics of food enzymes.
Rational, evolutionary and microenvironment engineering of food enzymes.
Techniques and technologies for food enzyme immobilization.
Innovative strategies for food enzyme reuse and recycling.
Techniques and strategies for new applications of food enzymes.

Prof. Dr. Xianghui Qi
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 enzyme
food bioprocessing
enzymatic catalysis
rational enzyme engineering
directed evolution
enzyme immobilization
enzyme techniques

Published Papers (5 papers)

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Research

13 pages, 2238 KiB

Open AccessArticle

Engineering the Thermostability of the Mono- and Diacylglycerol Lipase SMG1 for the Synthesis of Diacylglycerols

by Lilang Li, Yonghua Wang, Ruiguo Cui, Fanghua Wang and Dongming Lan

Foods 2022, 11(24), 4069; https://doi.org/10.3390/foods11244069 - 16 Dec 2022

Cited by 3 | Viewed by 1560

Abstract

Diacylglycerols (DAGs) display huge application prospectives in food industries. Therefore, new strategies to produce diacylglycerides are needed. Malassezia globose lipase (SMG1) could be used to synthesize DAGs. However, the poor thermostability of SMG1 seriously hampers its application. Herein, a rational design was used to generate a more thermostable SMG1. Compared with the wild type (WT), the M5D mutant (Q34P/A37P/M176V/G177A/M294R/ G28C-P206C), which contains five single-point mutations and one additional disulfide bond, displayed a 14.0 °C increase in the melting temperature (T_m), 5 °C in the optimal temperature, and 1154.3-fold in the half-life (t_1/2) at 55 °C. Meanwhile, the specific activity towards DAGs of the M5D variant was improved by 3.0-fold compared to the WT. Molecular dynamics (MD) simulations revealed that the M5D mutant showed an improved rigid structure. Additionally, the WT and the M5D variants were immobilized and used for the production of DAGs. Compared with the WT, the immobilized M5D-catalyzed esterification showed a 9.1% higher DAG content and a 22.9% increase in residual activity after nine consecutive cycles. This study will pave the way for the industrial application of SMG1. Full article

(This article belongs to the Special Issue Enzymes in Food Bioprocessing—Novel Food Enzymes, Applications, and Related Techniques)

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18 pages, 4575 KiB

Open AccessArticle

The Characterization of a Novel D-allulose 3-Epimerase from Blautia produca and Its Application in D-allulose Production

by Xinrui Tang, Yingfeng An, Muhammad Waheed Iqbal, Hongri Cong, Guoyan Zhang, Yufei Zhang, Yuvaraj Ravikumar, Hossain M. Zabed, Mei Zhao, Haixing Zhou and Xianghui Qi

Foods 2022, 11(20), 3225; https://doi.org/10.3390/foods11203225 - 15 Oct 2022

Cited by 10 | Viewed by 2290

Abstract

D-allulose is a natural rare sugar with important physiological properties that is used in food, health care items, and even the pharmaceutical industry. In the current study, a novel D-allulose 3-epimerase gene (Bp-DAE) from the probiotic strain Blautia produca was discovered for the production and characterization of an enzyme known as Bp-DAE that can epimerize D-fructose into D-allulose. Bp-DAE was strictly dependent on metals (Mn²⁺ and Co²⁺), and the addition of 1 mM of Mn²⁺ could enhance the half-life of Bp-DAE at 55 °C from 60 to 180 min. It exhibited optimal activity in a pH of 8 and 55 °C, and the K_m values of Bp-DAE for the different substrates D-fructose and D-allulose were 235.7 and 150.7 mM, respectively. Bp-DAE was used for the transformation from 500 g/L D-fructose to 150 g/L D-allulose and exhibited a 30% of conversion yield during biotransformation. Furthermore, it was possible to employ the food-grade microbial species Bacillus subtilis for the production of D-allulose using a technique of whole-cell catalysis to circumvent the laborious process of enzyme purification and to obtain a more stable biocatalyst. This method also yields a 30% conversion yield. Full article

(This article belongs to the Special Issue Enzymes in Food Bioprocessing—Novel Food Enzymes, Applications, and Related Techniques)

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20 pages, 3765 KiB

Open AccessArticle

Purification, Characterization, and Immobilization of a Novel Protease-Resistant α-Galactosidase from Oudemansiella radicata and Its Application in Degradation of Raffinose Family Oligosaccharides from Soymilk

by Xueran Geng, Jiayu Lei, Tergun Bau, Dongdong Guo, Mingchang Chang, Cuiping Feng, Lijing Xu, Yanfen Cheng, Ningke Zuo and Junlong Meng

Foods 2022, 11(19), 3091; https://doi.org/10.3390/foods11193091 - 5 Oct 2022

Cited by 3 | Viewed by 1573

Abstract

α-galactosidase (EC 3.2.1.22) are glycosidases that catalyze the hydrolysis of α-1,6-linked D-galactosyl residues of different substrates, which has been widely applied in the food industry. Oudemansiella radicata is a kind of precious edible medicinal mushroom, which is a healthy, green, and safe food-derived enzyme source. In this study, a novel acidic α-galactosidase was purified from the dry fruiting bodies of O. radicata by ion-exchange chromatography and gel filtration, and designated as ORG (O. radicata α-galactosidase). ORG was further immobilized to obtain iORG by the sodium alginate–chitosan co-immobilization method. Then, the characterization of free and immobilized enzymes and their potential application in the removal of the RFOs from soymilk were investigated. The results showed that ORG might be a 74 kDa heterodimer, and it exhibited maximum activity at 50 °C and pH 3.0, whereas iORG showed maximum activity at 50 °C and pH 5.5. In addition, iORG exhibited higher thermal stability, pH stability, storage stability, and a better degradation effect on raffinose family oligosaccharides (RFOs) in soymilk than ORG, and iORG completely hydrolyzed RFOs in soymilk at 50 °C within 3 h. Therefore, iORG might be a promising candidate in the food industry due to its excellent stability, high removal efficiency of RFOs from soymilk, and great reusability. Full article

(This article belongs to the Special Issue Enzymes in Food Bioprocessing—Novel Food Enzymes, Applications, and Related Techniques)

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12 pages, 2541 KiB

Open AccessArticle

Enhanced Extracellular Production and Characterization of Sucrose Isomerase in Bacillus subtilis with Optimized Signal Peptides

by Dan Guo, Mingyu Li, Mengtong Jiang, Guilong Cong, Yuxin Liu, Conggang Wang and Xianzhen Li

Foods 2022, 11(16), 2468; https://doi.org/10.3390/foods11162468 - 16 Aug 2022

Cited by 4 | Viewed by 1878

Abstract

Sucrose isomerase (SIase) catalyzes the hydrolysis and isomerization of sucrose into isomaltulose, which is an important functional sugar widely used in the food industry. However, the lack of safe and efficient expression systems for recombinant SIase has impeded its production and application. In this study, enhanced expression of a SIase from Klebsiella sp. LX3 (referred to as KsLX3-SIase) was achieved in Bacillus subtilis WB800N, by optimizing the signal peptides. First, 13 candidate signal peptides were selected using a semi-rational approach, and their effects on KsLX3-SIase secretion were compared. The signal peptide WapA was most efficient in directing the secretion of KsLX3-SIase into the culture medium, producing a specific activity of 23.0 U/mL, as demonstrated by shake flask culture. Using a fed-batch strategy, the activity of KsLX3-SIase in the culture medium was increased to 125.0 U/mL in a 5-L fermentor. Finally, the expressed KsLX3-SIase was purified and was found to have maximum activity at 45 °C and pH 5.5. Its K_m for sucrose was 267.6 ± 18.6 mmol/L, and its k_cat/K_m was 10.1 ± 0.2 s⁻¹mM⁻¹. These findings demonstrated an efficient expression of SIase in B. subtilis, and this is thought to be the highest level of SIase produced in a food-grade bacteria to date. Full article

(This article belongs to the Special Issue Enzymes in Food Bioprocessing—Novel Food Enzymes, Applications, and Related Techniques)

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12 pages, 1590 KiB

Open AccessArticle

Expression and Biochemical Characterization of a Novel Fucoidanase from Flavobacteriumalgicola with the Principal Product of Fucoidan-Derived Disaccharide

by Yanjun Qiu, Hong Jiang, Yueyang Dong, Yongzhen Wang, Hamed I. Hamouda, Mohamed A. Balah and Xiangzhao Mao

Foods 2022, 11(7), 1025; https://doi.org/10.3390/foods11071025 - 1 Apr 2022

Cited by 8 | Viewed by 2532

Abstract

Fucoidan is one of the main polysaccharides of brown algae and echinoderm, which has nutritional and pharmacological functions. Due to the low molecular weight and exposure of more sulfate groups, oligo-fucoidan or fucoidan oligosaccharides have potential for broader applications. In this research, a novel endo-α-1,4-L-fucoidanase OUC-FaFcn1 which can degrade fucoidan into oligo-fucoidan was discovered from the fucoidan-digesting strain Flavobacterium algicola 12,076. OUC-FaFcn1 belongs to glycoside hydrolases (GH) family 107 and shows highest activity at 40 °C and pH 9.0. It can degrade the α-1,4 glycosidic bond, instead of α-1,3 glycosidic bond, of the fucoidan with a random tangent way to generate the principal product of disaccharide, which accounts for 49.4% of the total products. Therefore, OUC-FaFcn1 is a promising bio-catalyst for the preparation of fucoidan-derived disaccharide. These results further enrich the resource library of fucoidanase and provide the basis for the directional preparation of fucoidan-derived oligosaccharide with specific polymerization. Full article

(This article belongs to the Special Issue Enzymes in Food Bioprocessing—Novel Food Enzymes, Applications, and Related Techniques)

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