摘要
The sensory characteristics of chicken skin chewy and soft are a crucial demand of consumers for hedonism of Chinese style soft-boiled chicken(Bai Qie Ji).In this investigation,the surface hydrophobicity of chicken skin protein was found to be the highest at 60 min.The exposure of hydrophobic groups led to the formation of protein cross-linking aggregates.The main force of maintaining protein was disulfide bond and hydrophobic interaction after stewing.A total of 536 metabolites with significant differences(P<0.05)were identified,among which amino acids,peptides and analogues,glycerophosphocholines,fatty acids and conjugates accounted for the majority.The t-g-t,β-sheet andβ-turn,N-acyl amino acid and 5’-umami nucleotide was significantly positively correlated with stewing time.In summary,the chicken skin collagen structure was conferred by augmented disulfide bonds,and N-acyl amino acids were pivotal metabolites,which offering novel insights into the processing mechanism of collagenous foodstuffs.
基金
supported by China Agriculture Research System of MOF and MARA(CARS-41)
National Natural Science Foundation of China(No.32472259).
