胃蛋白酶
化学
消化(炼金术)
Ⅰ型胶原
体外
生物化学
结缔组织
食品科学
热稳定性
酶
色谱法
内分泌学
生物
遗传学
作者
Miao Zhang,Di Zhao,Shuran Zhu,Yingqun Nian,Xinglian Xu,Xinglian Xu,Chunbao Li
标识
DOI:10.1016/j.foodres.2020.109225
摘要
Collagen, especially type I collagen, a major component for connective tissue in meat, determines the background tenderness and affects digestibility of meat. Heating may induce great changes in protein structure and its pepsin-treated digestion. The objective of this study was to investigate how heating affected type I collagen structure and in vitro pepsin-treated digestion. Type I collagen was heated at 60 °C, 70 °C, 80 °C for 0.5 to 2.5 h, and the spectrometric measurements and in vitro pepsin digestion were performed. Increased heating temperature caused the exposure of aromatic residues and an elevation of intensity of synchronous fluorescence spectra, but a reduction in the conformational stability of type I collagen (P < 0.05). Under the in vitro pepsin digestion, the Km value of enzymatic reaction increased as heating temperature rose, but overheating attenuated the affinity of type I collagen to pepsin. Heating at 70 °C for 0.5 h is good for type I collagen to get higher digestion.
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