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: closed (10 May 2026) | Viewed by 2255

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
Special Issues, Collections and Topics in MDPI journals

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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. Maolin Tu
Dr. Hongrui Chen
Guest Editors

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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 (3 papers)

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Research

22 pages, 17148 KB  
Article
Impact of Xanthan Gum on the Storage Stability of Pickering Emulsions Stabilized by Myofibrillar Protein Microgel Particles
by Yi Yang, Jingwei Ye, Chenju Zhang, Linjing Gao, Hongbin Lin, Qisheng Zhang, Jiaxin Chen and Rongrong Yu
Foods 2026, 15(8), 1398; https://doi.org/10.3390/foods15081398 - 17 Apr 2026
Cited by 1 | Viewed by 569
Abstract
Myofibrillar protein microgel particles (MMP) are promising Pickering stabilisers due to their structure and delivery potential. However, their fibrous, irregular shape promotes aggregation, limiting practical use. This study investigated the effect of xanthan gum (XG) concentration (0.025–0.4%) on MMP dispersion in water and [...] Read more.
Myofibrillar protein microgel particles (MMP) are promising Pickering stabilisers due to their structure and delivery potential. However, their fibrous, irregular shape promotes aggregation, limiting practical use. This study investigated the effect of xanthan gum (XG) concentration (0.025–0.4%) on MMP dispersion in water and its role in stabilising Pickering emulsions. FTIR and interaction analysis revealed that hydrophobic interactions dominate between XG and MMP, followed by hydrogen bonding and electrostatic forces. At higher XG concentrations (0.2–0.4%), complex particle size decreased from 5.21 μm to 4.49 μm, the contact angle increased from 57.67° to 77.33°, and a uniform dispersed state was achieved. Although increasing XG gradually reduced the emulsifying activity of MMP, it significantly improved the emulsion stability. Microstructure analysis showed that at low XG concentrations, emulsions exhibited phase separation. Rheological measurements indicated that XG-MMP complexes increased continuous-phase viscosity and shear resistance, enhancing macroscopic stability. In summary, at a critical XG concentration of 0.2%, the emulsion undergoes a transition from aggregation-driven instability to network-mediated stabilisation, achieved through the interfacial layer with spatial confinement by a weak aqueous-phase network. This work provides a theoretical foundation and a practical design strategy for fabricating highly stable, tuneable Pickering emulsions based on protein microgel particles. Full article
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14 pages, 3769 KB  
Article
Tilapia Skin-Derived Peptide PFRMY Attenuates Melanogenesis and Tyrosinase Activity via α-MSH/PKA/CREB Signaling Pathways in B16F10 Murine Melanoma Cells
by Yuqiong Song, Chen Lu, Shengjun Chen, Yongqiang Zhao, Hui Huang, Huan Xiang, Xiaoshan Long and Xiao Hu
Foods 2026, 15(8), 1378; https://doi.org/10.3390/foods15081378 - 15 Apr 2026
Viewed by 535
Abstract
The aim of this study was to investigate the anti-melanogenic effects and underlying mechanisms of PFRMY (Pro-Phe-Arg-Met-Tyr), a pentapeptide derived from tilapia skin (Oreochromis niloticus), using B16F10 murine melanoma cells. Treatment with PFRMY (1.0 mg/mL) significantly reduced intracellular melanin content and [...] Read more.
The aim of this study was to investigate the anti-melanogenic effects and underlying mechanisms of PFRMY (Pro-Phe-Arg-Met-Tyr), a pentapeptide derived from tilapia skin (Oreochromis niloticus), using B16F10 murine melanoma cells. Treatment with PFRMY (1.0 mg/mL) significantly reduced intracellular melanin content and tyrosinase (TYR) activity by 39.55 ± 1.51% and 32.46 ± 1.31%, respectively. RT-PCR and Western blotting analyses revealed that PFRMY suppressed melanogenesis through the α-MSH/PKA/CREB signaling pathway. Notably, PFRMY reversed α-MSH-induced upregulation of key downstream factors including PKA, CREB, MITF, and TYR, while showing minimal effects on the protein expression of MC1R or α-MSH. Molecular docking further suggested that PFRMY binds to MC1R with higher affinity than α-MSH, potentially occupying the ligand-binding site and thereby interfering with downstream signaling. Collectively, these findings demonstrate that PFRMY effectively inhibits melanogenesis by competitively antagonizing the α-MSH/MC1R axis, highlighting its potential as a safe and efficacious ingredient for hyperpigmentation treatment and cosmetic applications. Full article
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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
Cited by 1 | Viewed by 713
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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