Mingtang Tan , Mei Han , Yingyu Zhou , Zhongqin Chen , Wenhong Cao
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引用次数: 0
Abstract
This study aimed to separate and purify antifreeze peptides (AFP) from the autolysate of Litopenaeus vannamei head, and the peptide sequences with antifreeze activity were identified to elucidate the potential antifreeze mechanisms. The initial fractionation of autolysate revealed that the pk1 fraction with less than 3 kDa molecular weight exhibited the highest thermal hysteresis activity (2.28 °C). Notably, the component pk1-A with the strongest antifreeze activity (2.80 °C) was further separated by using a Sephadex G-15 gel filtration column. The results of bioinformatics and computer-assisted techniques indicated that 26 types of peptides from pk1-A were identified as AFP. Among these, KQVHPDTGISSK was selected as a potential Litopenaeus vannamei head antifreeze peptide (LvAFP). The active site (Lys residue) of LvAFP was discovered to strongly interact with water molecules via hydrogen bonding, thereby inhibiting the formation and recrystallization of ice crystals. Therefore, the preparation of LvAFP could improve the high-value utilization of shrimp byproducts.
期刊介绍:
Food Chemistry: X, one of three Open Access companion journals to Food Chemistry, follows the same aims, scope, and peer-review process. It focuses on papers advancing food and biochemistry or analytical methods, prioritizing research novelty. Manuscript evaluation considers novelty, scientific rigor, field advancement, and reader interest. Excluded are studies on food molecular sciences or disease cure/prevention. Topics include food component chemistry, bioactives, processing effects, additives, contaminants, and analytical methods. The journal welcome Analytical Papers addressing food microbiology, sensory aspects, and more, emphasizing new methods with robust validation and applicability to diverse foods or regions.