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Application of Bioenzyme Engineering and Enzyme Catalysis in the Food Industry

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A special issue of Molecules (ISSN 1420-3049).

Deadline for manuscript submissions: 31 October 2026 | Viewed by 2318

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Editors

Dr. Binglin Li

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Guest Editor

College of Food Science and Engineering, Northwest University, Xi’an 710069, China
Interests: food chemistry; bioenzyme engineering; enzyme catalysis; food processing

Prof. Dr. Ivan Kurtovic

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Guest Editor

1. College of Food Science and Technology, Northwest University, Xi’an 710069, China
2. Laboratory of Nutritional and Healthy Food-Individuation Manufacturing Engineering, Xi’an 710069, China
3. Research Center of Food Safety Risk Assessment and Control, Xi’an 710069, China
Interests: biocatalysis; enzyme immobilization; protein (enzyme) purification and characterization; isolation and extraction of natural enzymes; functional bioactive peptides

Prof. Dr. Roberto Fernandez-Lafuente

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Guest Editor

Departamento de Biocatálisis, ICP-CSIC, Campus UAM-CSIC, 28049 Madrid, Spain
Interests: biocatalysis; enzyme immobilization; enzyme stabilization; enzyme chemical modification; bioprocess optimization
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Special Issue Information

Dear Colleagues,

Enzyme engineering and biocatalysis are reshaping food science and manufacturing by enabling precision, efficiency, and sustainability. This Special Issue, “Application of Bioenzyme Engineering and Enzyme Catalysis in the Food Industry,” seeks contributions advancing both fundamental understanding and practical deployment of enzymes across the food value chain—from ingredient biosynthesis and protein modification to gentle processing, flavor development, and waste valorization.

We welcome studies that design, evolve, or repurpose enzymes and biocatalytic systems for food-relevant reactions; implement metabolic engineering to build microbial platforms for producing enzymes and functional molecules; and develop food-grade supports and immobilization strategies that enhance stability, reusability, and continuous processing. Submissions addressing computational protein design, structure–function relationships, process intensification, smart reactors, and scale-up in complex food matrices are especially encouraged.

Contributions may also explore safety and regulatory considerations for food-grade catalysts, life-cycle and techno-economic assessments, integration with green solvents or low-water processes, and the valorization of agri-food by-products within a circular bioeconomy.

We invite original research articles, reviews, communications, and short reports that align with these themes.

Dr. Binglin Li
Prof. Dr. Ivan Kurtovic
Prof. Dr. Roberto Fernandez-Lafuente
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 250 words) can be sent to the Editorial Office for assessment.

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-anonymized peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules 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 2700 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
biotechnology
biocatalysis
metabolic engineering
food-grade supports
protein modification
protein design

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Published Papers (3 papers)

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Research

19 pages, 32881 KB

Open AccessArticle

Comparative Structural Modeling Suggests Distinct Signatures of Conformational Plasticity and Surface Physicochemistry in Phytoene Synthase and Dehydrosqualene Synthase

by Ade Rizqi Ridwan Firdaus, Muhammad Yusuf, Shun Tamaki, Keiichi Mochida and Toto Subroto

Molecules 2026, 31(12), 1995; https://doi.org/10.3390/molecules31121995 - 7 Jun 2026

Viewed by 277

Abstract

Carotenoids are essential metabolites involved in photosynthesis, cellular protection, pigmentation, and antioxidant activities. Phytoene synthase (PSY/CrtB) utilizes C20 substrates in carotenoid biosynthesis, whereas its structural homolog, dehydrosqualene synthase (CrtM), preferentially accepts C15 substrates. Although previous studies have identified CrtM mutations that expand substrate scope, the molecular basis of substrate discrimination in PSY/CrtB remains poorly understood, largely because of the absence of experimentally determined three-dimensional structures. Here, we integrated comparative sequence analysis, homology modeling, and molecular dynamics (MD) simulations to investigate the structural basis of substrate discrimination in PSY/CrtB. Comparative sequence analysis suggested distinct overall conservation landscapes in PSY/CrtB and CrtM, with 20 highly conserved positions shared between them and clustered around the catalytic core. MD simulations suggest that PSY models exhibit minimal differentiation under cross-ligand conditions, consistent with its greater conformational plasticity. Surface property analysis suggested hydrophobic patches and an amphipathic helix (Helix-13) in PSY that were preferentially conserved in PSY homologs relative to CrtM homologs. Taken together, our analyses suggest that greater conformational plasticity may facilitate the accommodation of C20 substrates in PSY and that its conserved hydrophobic surface architecture may shape its surface physicochemistry. These findings suggest that differences in substrate accommodation between PSY/CrtB and CrtM may reflect coordinated variation in conformational dynamics, pocket hydrophobicity, and surface architecture, rather than substantial alterations to the conserved catalytic core. Full article

(This article belongs to the Special Issue Application of Bioenzyme Engineering and Enzyme Catalysis in the Food Industry)

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9 pages, 759 KB

Open AccessArticle

Impact of Pre-Treatment Strategies on Enzymatic Hydrolysis of Alternative Protein Sources: Case Study for Black Soldier Fly Larvae

by Sandra Borges, Tânia C. F. Ribas, André Almeida and Manuela Pintado

Molecules 2026, 31(10), 1770; https://doi.org/10.3390/molecules31101770 - 21 May 2026

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Abstract

The rising global demand for protein-rich food has intensified interest in alternative and sustainable protein sources. Insects, particularly black soldier fly (BSF) larvae, represent promising substrates due to their high nutritional content and potential for valorization into functional ingredients. This study investigated the impact of pre-hydrolysis treatments on the efficiency of enzymatic hydrolysis using alcalase to enhance protein solubilization and bioactive peptide production. Pre-treatments included organic acids (propionic and acetic acid) and a pressure-thermal method. Results indicated that BSF larvae responded differently to the evaluated pre-treatment strategies. Notably, the pressure-thermal treatment combined with enzymatic hydrolysis increased soluble protein content by approximately 30% and antioxidant activity by approximately 20%, suggesting enhanced release of bioactive peptides. Although organic acid treatments increased protein solubility, they did not improve the degree of hydrolysis or antioxidant activity. These findings highlight the potential of pressure-thermal pre-treatment to improve the efficiency of protein extraction from insect biomass and support the integration of such approaches into food bioprocessing strategies aimed at developing novel, high-value protein ingredients. Full article

(This article belongs to the Special Issue Application of Bioenzyme Engineering and Enzyme Catalysis in the Food Industry)

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20 pages, 8469 KB

Open AccessArticle

Enhancing the Catalytic Performance of β-Mannanase via Polyvinyl Alcohol Immobilization and Genipin Modification

by Nazli Ece Varan Faki, Ali Toprak, Guzide Yucebilgic, Dilek Alagöz, Deniz Yildirim and Roberto Fernandez-Lafuente

Molecules 2025, 30(23), 4567; https://doi.org/10.3390/molecules30234567 - 27 Nov 2025

Cited by 1 | Viewed by 1019

Abstract

This study reports the immobilization of β-mannanase from Aspergillus niger—either unmodified or genipin-modified—within polyvinyl alcohol hydrogels (PVA@mannanase and PVA@mannanase-Gen) for the enhanced production of mannooligosaccharides (MOSs). All enzyme preparations showed an optimal pH of 5.0, while immobilization shifted the optimal temperature from 40 °C for the free enzyme to 55 °C for the immobilized forms. Genipin modification notably improved stability, increasing the half-life from 25.3 h (free enzyme) to 429.2 h in PVA@mannanase-Gen, and raised catalytic efficiency by approximately 2.3-fold. Both immobilized preparations retained over 75% of their activity after five reuse cycles at pH 5 and 55 °C. Using PVA@mannanase-Gen under these optimized conditions, MOSs were effectively produced, with mannotetraose as the predominant product. To explore their potential applications, the MOSs generated from locust bean gum were evaluated for effects on MCF-7 and HCT-116 cancer cell lines, resulting in moderate growth inhibition (~24–25% at 0.4 mM after 24 h). Together, these findings demonstrate that the immobilization of the genipin-modified enzyme not only enhances β-mannanase stability and performance but also supports the efficient production of MOSs with promising antitumoral activity. Full article

(This article belongs to the Special Issue Application of Bioenzyme Engineering and Enzyme Catalysis in the Food Industry)

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