文献类型：期刊文献

英文题名：Structure and characteristics of acid and pepsin-solubilized collagens from the skin of cobia (Rachycentron canadum)

作者：Zeng, Shaokui[1,2];Yin, Juanjuan[1,2];Yang, Shuqi[1,2];Zhang, Chaohua[1,2];Yang, Ping[1,2];Wu, Wenlong[1]

机构：[1]Guangdong Ocean Univ, Coll Food Sci & Technol, Zhanjiang 524088, Peoples R China;[2]Guangdong Higher Educ Inst, Key Lab Aquat Prod Adv Proc, Zhanjiang 524088, Peoples R China

年份：2012

卷号：135

期号：3

起止页码：1975

外文期刊名：FOOD CHEMISTRY

收录：SCI-EXPANDED(收录号：WOS:000310396700152)、、EI(收录号：20123715421400)、Scopus(收录号：2-s2.0-84865763437)、WOS

基金：This work was supported by the National Science & Technology Pillar Program (Grant No. 2007BAD29B09) from the Ministry of Science and Technology of China and the Foundation for Agriculture Science and Technology Research Team of Guangdong (Grant No. 2011A020102005). We gratefully acknowledge and are indebted to the anonymous referees for comments and constructive suggestions provided for improving the manuscript.

语种：英文

外文关键词：Rachycentron canadum; Acid-solubilized collagen; Pepsin-solubilized collagen; LC-MS/MS; Fourier transform infrared spectroscopy; Characteristics

外文摘要：Acid-solubilized collagen (ASC) and pepsin-solubilized collagen (PSC) were extracted from the skin of cobia (Rachycentron canadum). The yields of ASC and PSC were 35.5% and 12.3%, respectively. Based on the protein patterns and carboxymethyl-cellulose chromatography, ASC and PSC were composed of alpha 1 alpha 2 alpha 3 heterotrimers and were characterised as type I collagen with no disulfide bond. Their amounts of imino acids were 203 and 191 residues per 1000 residues, respectively. LC-MS/MS analysis demonstrated the high sequences similarities of ASC and PSC. Fourier transform infrared spectroscopy spectra showed that the amide I, II and III peaks of PSC were obtained at a lower wave number compared with ASC. The thermal denaturation temperatures of ASC and PSC, as measured by viscometry, were 34.62 and 33.97 degrees C, respectively. The transition temperatures (T-max) were 38.17 and 36.03 degrees C, respectively, as determined by differential scanning calorimetry (DSC). Both collagens were soluble at acidic pH and below 2% (w/v) NaCl concentration. (C) 2012 Elsevier Ltd. All rights reserved.