Extraction and characterization of acid- and pepsin-soluble collagens from the scales, skins and swim-bladders of grass carp (Ctenopharyngodon idella)

被引：66
|
作者：
Liu, Dasong [1 ,2 ]
Zhang, Xuan [1 ]
Li, Tiancheng [1 ]
Yang, Hongxu [1 ]
Zhang, Hongchao [1 ]
Regenstein, Joe M. [3 ]
Zhou, Peng [1 ,2 ]
机构：
[1] Jiangnan Univ, State Key Lab Food Sci & Technol, Sch Food Sci & Technol, Wuxi 214122, Jiangsu, Peoples R China
[2] Synerget Innovat Ctr Food Safety & Nutr, Wuxi 214122, Jiangsu, Peoples R China
[3] Cornell Univ, Dept Food Sci, Ithaca, NY 14853 USA
来源：
FOOD BIOSCIENCE | 2015年 / 9卷
基金：
中国国家自然科学基金;
关键词：
Acid-soluble collagen; Pepsin-soluble collagen; Crass carp; Scale; Skin; Swim-bladder; HYPOPHTHALMICHTHYS-MOLITRIX; BONE; NILOTICUS; GELATIN;
D O I：
10.1016/j.fbio.2014.12.004
中图分类号：
TS2 [食品工业];
学科分类号：
0832 ;
摘要：
The objective of this study was to characterize and compare the acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from the scales, skins and swim-bladders of grass carp. Both ASC and PSC from the three tissues were mainly characterized as type I collagen, with similar electrophoretic patterns and amino acid profiles. PSG from the three tissues was more susceptible to hydrolysis by V8 protease than ASC. Both ASC and PSG from the three tissues showed similar peptide hydrolysis patterns. The maximum transition temperatures of both ASC and PSC from the internal tissue (swim-bladders) were only slightly higher than those of ASC and PSC from the external tissues (scales and skins). These results suggest that collagens from the three tissues of grass carp had almost similar biochemical properties, and could be used as potential substitutes for mammalian collagens due to their comparatively high thermostability. (C) 2014 Elsevier Ltd. All rights reserved.
引用
收藏
页码：68 / 74
页数：7
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