Affiliation:
1. Shenzhen Institute of Guangdong Ocean University Shenzhen 518120 China
2. College of Food Science and Technology Guangdong Ocean University Zhanjiang 524088 China
3. Guangdong Provincial Key Laboratory of Aquatic Products Processing and Safety Guangdong Provincial Engineering Technology Research Centre of Seafood Zhanjiang 524088 China
4. Guangdong Province Engineering Laboratory for Marine Biological Products Key Laboratory of Advanced Processing of Aquatic Product of Guangdong Higher Education Institution Zhanjiang 524088 China
Abstract
SummaryEnzymatic supramolecular assembly was applied to increase the thermal hysteresis activity (THA) of tilapia skin collagen peptides and their applicability as cryoprotectants. The THA value of the glutamine‐assembled product increased by 61.5% and its ice crystal content dropped by 33.93% compared to the collagen peptides. Following initial separation and purification, the THA of Gln‐AFPs was further elevated by 28.6%. After five freeze–thaw cycles, tilapia surimi treated with 8% Gln‐AFPs had high levels of salt‐soluble protein, total sulfhydryl content, Ca2+‐ATPase activity, and water‐holding capacity. Additionally, the cryoprotective effect of Gln‐AFPs on the surimi was found to be superior to that of commercial antifreeze. The majority of the Gln‐AFPs turns folded, according to FTIR analysis, and ‐helices were produced. After supramolecular assembly, the Gln‐AFPs structure also smoothed out. As a result, the enzymatic supramolecular assembly drastically increased the antifreeze activity of the tilapia skin‐collagen peptides, which could eventually be developed into a novel antifreeze additive in the food industry.
Funder
Natural Science Foundation of Shenzhen Municipality