自溶(生物学)
胰蛋白酶
纤维
蛋白多糖
化学
生物化学
丝氨酸
胶原酶
羟脯氨酸
蛋白质水解
生物物理学
酶
生物
细胞外基质
作者
Zi-qiang Liu,Feng-yan Tuo,Lina Song,Yuxin Liu,Xiuping Dong,Dongmei Li,Dayong Zhou,Fereidoon Shahidi
标识
DOI:10.1016/j.foodchem.2018.02.117
摘要
Trypsin, a representative serine proteinase, was used to hydrolyse the collagen fibres from sea cucumber (Stichopus japonicus) to highlight the role of serine proteinase in the autolysis of sea cucumber. Partial disaggregation of collagen fibres into collagen fibrils upon trypsin treatment occurred. The trypsin treatment also caused a time-dependent release of water-soluble glycosaminoglycans and proteins. Therefore, the degradation of the proteoglycan bridges between collagen fibrils might account for the disaggregation of collagen fibrils. For trypsin-treated collagen fibres (72 h), the collagen fibrils still kept their structural integrity and showed characteristic D-banding pattern, and the dissolution rate of hydroxyproline was just 0.21%. Meanwhile, Fourier transform infrared analysis showed the collagen within trypsin-treated collagen fibres (72 h) still retaining their triple-helical conformation. These results suggested that serine proteinase participated in the autolysis of S. japonicus body wall by damaging the proteoglycan bridges between collagen fibrils and disintegrating the latter.
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