This study investigates the ultrasound-assisted enzymatic extraction of collagen hydrolysates (CH) from chicken skin, heads, and feet, aiming to generate bioactive peptides with potent antioxidant activity. Process optimization involved acetic acid pre-treatment, ultrasonication (39 kHz), and enzymatic hydrolysis using collagenase, followed by ultrafiltration (10 kDa). The optimized treatment (T2) yielded hydrolysates with a high degree of hydrolysis (85.31%) and protein content (11.73 g/dL). SDS-PAGE revealed predominantly low-molecular-weight peptides, indicative of effective collagen breakdown. Antioxidant capacity, measured via DPPH and ABTS+ assays, was significantly elevated in T2 (76.38% and 91.41%, respectively). Peptidomic profiling was conducted using LC-ESI-MS/MS on a QTOF mass spectrometer, enabling the identification of numerous peptide sequences. In-silico bioactivity prediction using the BIOPEP database and Peptide Ranker algorithm revealed multiple sequences with high antioxidant potential, particularly short-chain peptides rich in hydrophobic and aromatic residues. The integration of advanced proteomic tools and bioinformatic analyses confirmed the efficacy of ultrasound-assisted enzymatic hydrolysis in producingfunctionally relevant peptides. These findings support the valorization of poultry by-products as a sustainable source ofantioxidative peptides for potential applications in food and health sectors.
Sucheta Roy, Rituparna Banerjee, N. B. Maheswarappa et al.· Journal of Meat Science· 0 citations
The global protein transition is accelerating the development of alternative protein foods, mainly derived from plants, insects, algae, fungi, and cellular agriculture. Ensuring the authenticity, safety, and nutritional adequacy of these emerging protein matrices requires molecular-level characterization beyond traditional compositional analyses. Proteomics and peptidomics have emerged as transformative analytical platforms capable of decoding the molecular signatures that define protein origin, structural integrity, digestibility, functionality, and health potential. The review comprehensively examines the application of proteomics, and peptidomics for profiling alternative protein foods. Further, the source authentication strategies based on species-specific protein and peptide biomarkers, detection of adulteration in complex matrices, and allergenicity assessment is discussed. Special attention is also given to nutritional proteomics with protein digestibility, gastrointestinal peptide release, and identification of bioactive sequences. SIGNIFICANCE: The importance of this review is that proteomics and peptidomics are becoming central in the management of the fast-growing environment of alternative protein foods, such as plant-based, insect, algal, fungal, and cultured meat products. It provides an explanation of the application of mass spectrometry-based processes to decode molecular signatures defining the origin of proteins, their structural integrity, digestibility, allergenicity, and bioactive properties, and thus directly contribute to safety, nutritional analysis, and authenticity of the product. Presentation of the article includes the integration of the knowledge of traditional muscle foods with alternative systems of proteins, where validated protein and peptide biomarkers are used in authentication, fraud detection, and allergy risk assessment in a wide variety of matrices. It also indicates the role of nutritional proteomics and peptidomics in informing the formulation strategy to promote digestibility and release of health-promoting peptides. In general, this review will guide scientists, the food industry, and regulations to use modern proteomic technologies in quality assurance, regulation decision-making, and the development of sustainable protein foods.
Rituparna Banerjee, P. K. Nanda, Laura Alessandroni et al.· Journal of Proteomics· 0 citations
