Information from the abstract
The effects of post-gelation pasteurization (80 °C) and sterilization (121 °C) on microbial transglutaminase (MTG)-crosslinked threadfin bream surimi seafood were evaluated in terms of structure, volatile compounds, and in vitro digestibility. MTG increased gel breaking force and distance while reducing expressible moisture content ( p < 0.05). Pasteurization maintained or slightly improved the textural properties of non-crosslinked gels but weakened MTG-treated gels, indicating greater thermal susceptibility of the crosslinked network. Sterilization caused marked structural deterioration, including β-sheet disruption, weakened hydrophobic interactions, increased disulfide bond formation, and fragmented microstructure. TBARS increased after pasteurization but decreased after sterilization, suggesting further oxidation and malondialdehyde degradation, consistent with increased volatile compounds. Thermal treatment, particularly sterilization, promoted lipid oxidation and Maillard-derived volatiles. MTG initially increased proteolytic susceptibility, whereas thermal processing reduced digestibility because of protein aggregation, oxidative crosslinking, lipid oxidation, and Maillard reactions. Peptidomic analysis showed that MTG increased peptide diversity, whereas thermal processing reduced diversity and shifted peptide profiles toward negatively charged peptides and free amino acids. Overall, sterilization largely offsets the benefits of MTG, while pasteurization led to comparatively less quality deterioration, underscoring the need to optimize thermal processing to balance safety and product quality.
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Related topics: Protein Hydrolysis and Bioactive Peptides · Proteins in Food Systems · Probiotics and Fermented Foods
Thai researcher and institutional participation
Ali Hamzeh · Jirawat Yongsawatdigul · Papungkorn Sangsawad · Pichitpon Luasiri · Sittiruk Roytrakul · Mariena Ketudat-Cairns · Suranaree University of Technology · National Center for Genetic Engineering and Biotechnology
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