Proteins and Peptides in Food: From Preparation to Properties and Applications

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

Deadline for manuscript submissions: 15 April 2026 | Viewed by 575

Special Issue Editors


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Guest Editor
School of Food Science and Technology, Jiangnan University, Lihu Road 1800, Wuxi 214122, China
Interests: food protein; peptides; functional foods; healthier rice products; in vitro digestion

E-Mail Website
Guest Editor
School of Food Science and Technology, Jiangnan University, Lihu Road 1800, Wuxi 214122, China
Interests: nutritional composition; food protein modification; functional regulation mechanisms in rice; development of new functional food products; rice product innovation
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Special Issue Information

Dear Colleagues,

Proteins and peptides have attracted significant interest as natural and functional ingredients in the food industry, driven by the growing demand for health-promoting and clean-label products. Synthetic additives and processed ingredients often face scepticism due to concerns over safety, allergies, and long-term health impacts. As a result, there has been a shift toward utilizing proteins and peptides, derived from various sources, for their nutritional and functional benefits. These biomolecules represent rich sources of essential amino acids and exhibit a range of bioactive properties, including antioxidant, antimicrobial, antihypertensive, and immunomodulatory activity, making them highly valuable in enhancing food quality and functionality. Although proteins and peptides show great potential as multifunctional food ingredients, their application is accompanied by challenges that need to be addressed to maximize their efficacy. Issues such as low bioavailability, instability during processing, potential allergenicity, and a bitter taste can limit their use in food systems. Recent technological advances have focused on developing novel delivery systems and modification methods to overcome these obstacles. Applications such as encapsulation, enzymatic hydrolysis, functional conjugates, and incorporation into edible films and nano-emulsions represent some of the innovative approaches currently being explored to improve the stability, sensory attributes, and bioactivity of protein- and peptide-enriched foods.

Dr. Xinxia Zhang
Prof. Dr. Li Wang
Guest Editors

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Keywords

  • protein
  • peptide
  • modification
  • application
  • healthier rice products
  • nutritional composition

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Published Papers (1 paper)

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Research

13 pages, 2176 KB  
Article
Formation and Characterization of Bifunctional Nanoparticles Fabricated from Insoluble Rice Peptide Aggregate: Effect of Enzymes
by Xinxia Zhang, Shengze Ma, Ting Li and Li Wang
Foods 2025, 14(22), 3974; https://doi.org/10.3390/foods14223974 - 20 Nov 2025
Viewed by 425
Abstract
This study systematically investigates the effects of enzyme type (Alcalase, Trypsin, Protamex) on the properties of rice peptide nanoparticles (RPNs) and their efficacy in stabilizing high internal phase emulsions (HIPEs). RPNs prepared with Alcalase (RPNs-alc) exhibited the smallest particle size (≈379.6 nm), a [...] Read more.
This study systematically investigates the effects of enzyme type (Alcalase, Trypsin, Protamex) on the properties of rice peptide nanoparticles (RPNs) and their efficacy in stabilizing high internal phase emulsions (HIPEs). RPNs prepared with Alcalase (RPNs-alc) exhibited the smallest particle size (≈379.6 nm), a uniform unimodal distribution, the highest content of hydrophobic amino acid, and the strongest DPPH (2,2-Diphenyl-1-picrylhydrazyl) radical scavenging activity (57.32%). In contrast, RPNs from Protamex (RPNs-pro) showed larger, heterogeneous particles with a bimodal distribution and lower antioxidant capacity. Interfacial characterization revealed that RPNs-alc had a superior three-phase contact angle, indicating enhanced interfacial activity. Structural stability analysis confirmed that hydrophobic interactions and hydrogen bonds are the primary forces maintaining all RPNs. Consequently, HIPEs stabilized by RPNs-alc and RPNs-typ displayed solid-like behavior and a regular network microstructure, leading to exceptional physical stability. Conversely, RPNs-pro led to unstable HIPEs with non-uniform droplets and interfacial aggregation, promoting droplet flocculation. These findings demonstrate that enzyme selection critically determines the functional properties of RPNs, with Alcalase-derived RPNs being the most effective bifunctional particles, offering a viable pathway for valorizing proteolytic by-products in fabricating stable, antioxidant-rich Pickering emulsions. Full article
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