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Innovative Food Proteins and Polyphenols: Mechanisms, Functional Properties, and Sustainable...
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Innovative Food Proteins and Polyphenols: Mechanisms, Functional Properties, and Sustainable Processing

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

Deadline for manuscript submissions: 5 December 2025 | Viewed by 2735

Special Issue Editors

Dr. Yuemei Zhang

E-Mail Website
Guest Editor
Department of Food Science and Technology, School of Food and Health, Beijing Technology and Business University, Beijing 100048, China
Interests: meat products; frozen meat; thawed drip; myofibrillar proteins; protein denaturation; protein oxidation; gelation; cryoprotection; meat microbiology; freshness; shelf-life
Special Issues, Collections and Topics in MDPI journals
Dr. Ying Wang

E-Mail Website
Guest Editor
School of Food and Health, Beijing Technology and Business University, Beijing, China
Interests: meat; meat processing; flavor; livestock by-product
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This issue focuses on the emerging role of proteins and polyphenols in enhancing food systems. Proteins contribute to food texture, nutrition, and stability, while polyphenols offer antioxidant, antimicrobial, and health-promoting properties. The interactions between these components significantly impact functionality, influencing bioavailability, microbial resistance, and overall food quality. This issue delves into the underlying mechanisms of these interactions and their implications for processing properties such as texture, stability, and preservation.

Highlighted topics include machine learning (ML) and artificial intelligence (AI) applications in food processing, novel packaging technologies, and smart materials that monitor protein-polyphenol interactions, providing cutting-edge tools for optimizing food quality and stability. A dedicated section addresses sustainable, eco-friendly processing, featuring green extraction methods for proteins and polyphenols, energy reduction in processing, and by-product waste valorization, which are essential steps toward a more sustainable food industry. This issue also emphasizes the value of cross-disciplinary collaborations in nanotechnology, bioengineering, and functional foods. Innovative delivery systems, such as nanoencapsulation for bioactive polyphenols and proteins, offer ways to enhance both nutritional impact and shelf life. By integrating insights from molecular, biochemical, and technological perspectives, this issue aims to deepen our understanding of the roles of proteins and polyphenols, driving the development of healthier, more functional, and sustainable food products.

Dr. Yuemei Zhang
Dr. Ying Wang
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

  • food protein
  • food polyphenols
  • ood functionality
  • food processing properties
  • fermentation
  • antioxidant activity
  • food preservation

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Published Papers (2 papers)

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Research

23 pages, 3420 KiB  
Article
Optimising Enzymatic Cross-Linking: Impact on Physicochemical and Functional Properties of Lupin Flour and Soy Protein Isolate
by Teguh Santoso, Yusur Al-Shaikhli, Thao M. Ho, Mishenki Rajapakse and Thao T. Le
Foods 2025, 14(11), 1976; https://doi.org/10.3390/foods14111976 - 3 Jun 2025
Viewed by 326
Abstract
The growing demand for plant-based protein alternatives has driven interest in protein modifications to enhance their functional properties in food applications. Enzymatic cross-linking using laccases derived from Rhus vernicifera (LR) and transglutaminase (TG) offers a promising strategy to enhance protein solubility, emulsifying properties, [...] Read more.
The growing demand for plant-based protein alternatives has driven interest in protein modifications to enhance their functional properties in food applications. Enzymatic cross-linking using laccases derived from Rhus vernicifera (LR) and transglutaminase (TG) offers a promising strategy to enhance protein solubility, emulsifying properties, and foaming properties of food proteins. This study varied the enzymatic reaction conditions, including enzyme concentration, pH, temperature, incubation time, and ferulic acid addition, for the most effective cross-linking between proteins in lupin flour (LF) and soy protein isolate (SPI), resulting in changes in physicochemical and functional properties of the cross-linked proteins. LR-induced cross-linking in lupin and soy proteins was most favourable at 142.5 U/100 mg protein, pH 6, and 20 °C, where ferulic acid enhanced cross-linking efficiency with prolonged incubation (20 h). TG-induced cross-linking in lupin and soy proteins was most favourable at 1.25 U/100 mg protein, pH 6 and 30 °C, where high-molecular-weight aggregates were observed. Cross-linking modified protein surface characteristics, increasing ζ-potential and particle size due to protein aggregation, while ferulic acid further enhanced polymerisation. Morphological analysis revealed a porous powder structure across all samples with increased porosity in cross-linked samples as evidenced by the predominance of small fragments within the particles. Prolonged incubation led to partial disaggregation in LR-treated samples unless they were stabilised by ferulic acid. Under mild conditions (1 h, pH 6, 20 °C), LR and ferulic acid-added samples showed minor and significant improvements in protein solubility and foaming stability, respectively. Additionally, a significant increase in foaming ability was observed in ferulic acid-added LR samples after prolonged incubation (20 h), compared to the corresponding control. In contrast, prolonged incubation (20 h) or TG treatment had a lower foaming stability compared to the mild LR treatment. Emulsifying ability and emulsion stability showed limited variation across treatments. These findings suggest that cross-linking conditions influence specific functional properties, highlighting the need for further optimisation to achieve desired protein functionality in food applications. Full article
(This article belongs to the Special Issue Innovative Food Proteins and Polyphenols: Mechanisms, Functional Properties, and Sustainable Processing)
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17 pages, 3264 KiB  
Article
Differential Enzymatic Hydrolysis: A Study on Its Impact on Soy Protein Structure, Function, and Soy Milk Powder Properties
by Qian Li, Baoyue Chang, Guo Huang, Di Wang, Yue Gao, Zhijun Fan, Hongbo Sun and Xiaonan Sui
Foods 2025, 14(5), 906; https://doi.org/10.3390/foods14050906 - 6 Mar 2025
Cited by 1 | Viewed by 2102
Abstract
Protein constitutes the primary nutrient in soy, and its modifications are intricately linked to the properties of the soy milk powder. This study employed six main commercial enzymes (bromelain, neutrase, papain, trypsin, flavourzyme, and alcalase) to investigate the impact of enzymatic hydrolysis on [...] Read more.
Protein constitutes the primary nutrient in soy, and its modifications are intricately linked to the properties of the soy milk powder. This study employed six main commercial enzymes (bromelain, neutrase, papain, trypsin, flavourzyme, and alcalase) to investigate the impact of enzymatic hydrolysis on the structural and functional properties of soy protein isolate (SPI), as well as its influence on the physicochemical properties of soy milk powder. The findings indicated that each of enzymes exhibits distinct specificity, with the degree of hydrolysis following the order: alcalase > flavourzyme > papain > bromelain > neutrase > trypsin. Enzymatic hydrolysis facilitates the unfolding of SPI, leading to the exposure of chromogenic fluorophores and hydrophobic amino acid residues, which in turn promotes an increase in free sulfhydryl content. Concurrently, this process induces the transformation of α-helix and β-sheet into β-turn and random coil. The enzyme modification enhances the solubility, emulsification, and foaming activities of SPI and significantly augment its antioxidant properties (p < 0.05). However, this enzymatic treatment adversely affects the stability of its emulsification and foaming properties. Subsequent to enzymatic hydrolysis, soy milk powder demonstrated a reduction in particle size and an improvement in solubility, which significantly enhanced its flavor profile. In summary, alcalase offers substantial advantages in augmenting the functional properties of SPI and increasing the solubility of soy milk powder. However, this process adversely affects the flavor profile of soy milk powder, a consequence attributed to the broad hydrolysis specificity of alcalase. Full article
(This article belongs to the Special Issue Innovative Food Proteins and Polyphenols: Mechanisms, Functional Properties, and Sustainable Processing)
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