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] College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, China; [2] Key Laboratory of Aquatic Product Advanced Processing, Guangdong Higher Education Institutes, Zhanjiang 524088, China

年份：2012

卷号：135

期号：3

起止页码：1975

外文期刊名：Food Chemistry

收录：EI(收录号：20123715421400)

语种：英文

外文关键词：Fourier transform infrared spectroscopy - Amino acids - Sulfur compounds - Sodium chloride - Covalent bonds - Differential scanning calorimetry

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 α1α2α3 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 °C, respectively. The transition temperatures (Tmax) were 38.17 and 36.03 °C, respectively, as determined by differential scanning calorimetry (DSC). Both collagens were soluble at acidic pH and below 2% (w/v) NaCl concentration. ? 2012 Elsevier Ltd. All rights reserved.