Action of trypsin on structural changes of collagen fibres from sea cucumber (Stichopus japonicus). (1st August 2018)

• Record Type: Journal Article
• Authors: Liu, Zi-qiang; Tuo, Feng-yan; Song, Liang; Liu, Yu-xin; Dong, Xiu-ping; Li, Dong-mei; Zhou, Da-yong; Shahidi, Fereidoon
• Is Part Of: Food chemistry. Volume 256(2018)
• Page Start: 113
• Page End: 118
• Publication Date: 2018-08-01
• Subjects: Sea cucumber (Stichopus japonicus) -- Autolysis -- Collagen fibres -- Collagen fibrils -- Trypsin; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2018.02.117
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Collagen fibres were partially degraded into collagen fibrils by trypsin. Trypsin treatment freed glycosaminoglycan and hydroxyproline from collagen fibres. The damage to collagen by trypsin was very slight. Serine proteinase participated in the autolysis of sea cucumber. Abstract: 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.