Animal-Derived Food Resources: Advancing Innovations and Functional Applications

A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Nutraceuticals, Functional Foods, and Novel Foods".

Deadline for manuscript submissions: 10 May 2026 | Viewed by 377

Special Issue Editors


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Guest Editor
College of Food Science and Engineering, Ningbo University, Ningbo, China
Interests: protein; non-thermal processing; structure–function relationships; peptide; probiotics; sensory science
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Guest Editor
School of Food and Bioengineering, Xihua University, Chengdu, China
Interests: animal by-product valorization; alternative proteins; aquatic products; hydrogel; polysaccharides

Special Issue Information

Dear Colleagues,

Animal-derived foods represent a vital component of the global diet, providing high-quality proteins, essential nutrients, and bioactive compounds. In response to increasing demand for sustainable, nutritious, and functional food systems, there is growing interest in both traditional and underutilized animal resources, as well as novel ingredients integrated into animal-based products. This Special Issue of Foods aims to highlight cutting-edge research on the development, characterization, and application of animal-derived food resources, including, but not limited to, meat, dairy, eggs, aquatic products, and emerging alternatives.

We invite researchers to submit original research articles, reviews covering the following topics:

  • Valorization of Animal By-Products: High-value conversion of processing side-streams (e.g., blood, bones, offal, shells) into edible ingredients, functional additives, or bioactive compounds such as proteins, peptides, collagen, and enzymes.
  • Next-Generation Processing Technologies: Application of non-thermal methods (e.g., high-pressure processing, cold plasma, pulsed electric fields), enzymatic engineering, and digital monitoring tools to enhance the safety, quality, shelf life, and native functionality of animal-derived foods.
  • Cellular Agriculture and Novel Ingredients: Research on cultivated (cell-based) meat, poultry, seafood, and dairy, along with fermentation-derived proteins, insect biomass, and marine polysaccharides as innovative inputs in animal food systems.
  • Structure–Function and Matrix Design: Studies on the behavior of proteins, peptides, and other components in complex food matrices (e.g., meat emulsions, dairy gels) for tailored texture, stability, and bioactivity.
  • Species Diversification and Underutilized Resources: Nutritional, sensory, and safety assessments of non-conventional animal sources and traditional regional foods.
  • Sensory Science and Consumer Acceptance: Palatability, acceptability, and optimization strategies for novel animal-based products, including those with alternative or upcycled ingredients.
  • Traceability, Authenticity, and Nutritional Profiling: Advanced analytical approaches (e.g., spectroscopy, omics) for ensuring origin, preventing fraud, and evaluating nutritional quality.

We welcome high-quality contributions that will support a more sustainable, efficient, and innovative future for animal-derived food production and consumption.

Dr. Maoling Tu
Dr. Hongrui Chen
Guest Editors

Manuscript Submission Information

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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.

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Keywords

  • animal by-product valorization
  • non-thermal processing
  • cellular agriculture
  • structure-function relationships
  • alternative proteins
  • species diversification
  • sensory science
  • food traceability
  • precision fermentation

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Published Papers (1 paper)

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Research

18 pages, 3767 KB  
Article
Effect of Boiling on Meretrix lyrata Protein Structure Variation and Its Mechanism Based on Data-Independent Acquisition (DIA) Quantitative Proteomics
by Wen-Hui Shang, Zhi-Chao Chang, Yi-Wen Wang, Quzhen Luosang, Yu-Yu Hang, Zhi-Sheng Pei and Xuan-Ri Shen
Foods 2025, 14(24), 4278; https://doi.org/10.3390/foods14244278 - 12 Dec 2025
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Abstract
This study employed a multi-technique approach to investigate the structural and conformational changes in proteins in Meretrix lyrata (M. lyrata) adductor, foot, and siphon tissues during boiling. Data-independent acquisition (DIA) quantitative proteomics was utilized to identify differentially expressed proteins (DEPs) in [...] Read more.
This study employed a multi-technique approach to investigate the structural and conformational changes in proteins in Meretrix lyrata (M. lyrata) adductor, foot, and siphon tissues during boiling. Data-independent acquisition (DIA) quantitative proteomics was utilized to identify differentially expressed proteins (DEPs) in six temporal comparison groups (20–0 s, 40–20 s, 60–40 s, 80–60 s, 100–80 s, and 120–100 s). The results showed that key myofibrillar proteins, including myosin heavy chain, paramyosin, and actin, exhibited tissue-specific expression patterns, while low-molecular-weight degradation fragments (<17 kDa) appeared with prolonged heating. Turbidity measurements peaked in adductor and siphon tissues at 60 s and in foot tissue at 80 s. Heating resulted in a narrowed particle size distribution (100–1000 nm), and a decreased zeta potential, indicating a reduction in protein surface charge. Fourier transform infrared spectroscopy revealed hydrogen bond disruption and secondary structure transitions, marked by a reduction in α-helix content with a corresponding increase in β-sheet and random coil structures. In total, 6527 proteins were identified, and Gene Ontology (GO) enrichment analysis highlighted the DEPs’ involvement in biological regulation and metabolic processes. Collectively, these results provide comprehensive characterization of protein denaturation, degradation, and structural reorganization in M. lyrata tissues during the boiling process. Full article
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