期刊
FOOD CHEMISTRY
卷 256, 期 -, 页码 113-118出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2018.02.117
关键词
Sea cucumber (Stichopus japonicus); Autolysis; Collagen fibres; Collagen fibrils; Trypsin
资金
- National Natural Science Foundation of China [30901124, 31401562, 31401520, 31401519]
- Project of Distinguished Professor of Liaoning Province [2015-153]
- Cultivation Plan for Youth Agricultural Science and Technology Innovative Talents of Liaoning Province [2015002]
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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