摘要
以云南鲷鱼骨为原料,采用低温酸法提取制备鱼骨中的酸溶性胶原蛋白(acid-soluble collagen,ASC),并对ASC的氨基酸组成、亚基组成、红外吸收、紫外吸收、热稳定性、X射线衍射、微观结构、多肽片段以及溶解性进行了全面的分析。氨基酸组成表明ASC主要含甘氨酸、脯氨酸和丙氨酸,而酪氨酸、蛋氨酸和半胱氨酸含量较低;十二烷基硫酸钠-聚丙烯酰胺凝胶电泳结果显示ASC为Ⅰ型胶原蛋白;ASC在230 nm波长处有最大紫外吸收峰;傅里叶变换红外光谱和X射线衍射图谱表明ASC分子排列紧凑,保持了其原有的三螺旋结构;差示扫描量热分析结果显示ASC的变性温度分别为86.5℃和226.2℃,有较好的热稳定性;扫描电子显微镜显示ASC分子分布均匀、表面光滑呈三维立体结构;多肽片段分析结果显示鱼骨胶原的氨基酸构成主要为Gly-X-Y,符合胶原蛋白的一级结构的特点;在p H值小于4的条件下,ASC溶解度较高,当Na Cl质量分数大于4%时,ASC溶解度剧烈下降。
Acid-soluble collagen（ASC） was extracted from the bone of Yunnan bream using cold acetic acid, and its amino acid composition, subunit composition, Fourier transform infrared（FTIR） and UV absorption characteristics, thermal stability and X-ray diffraction（XRD） characteristics, microstructure, peptide fragments and solubility were analyzed. Amino acid analysis showed that ASC mainly consisted of Gly, Pro and Ala, as well as lesser amounts of Tyr, Met, and Cys. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis confirmed ASC to be typical I collagen. The maximum absorption peak of ASC appeared at 230 nm. The FTIR and XRD spectra proved that the helical structure of ASC remained intact. Differential scanning calorimetry showed that ASC had two denaturation temperatures of 86.5 and 226.2 ℃ indicating high thermal stability. Scanning electron microscopy showed that the microstructure of ASC was homogenous with a smooth surface. Peptide analysis showed that amino acid sequence of ASC was Gly-X-Y, which was in agreement with the primary structure characteristics of collagen. The solubility of ASC was relatively high under acidic conditions（p H 〈4）, whereas it dropped sharply when Na Cl concentration was higher than 4%.
作者
姚行行
郭妍
庄永亮
YAO Hanghang;GUO Yan;ZHUANG Yongliang(Yulman Institute of Food Safety,Kunming University of Science and Technology,Kunming 650500,Chin)
出处
《食品科学》
EI
CAS
CSCD
北大核心
2018年第13期35-40,共6页
Food Science
基金
国家自然科学基金地区科学基金项目(31360381)
关键词
鲷鱼骨
胶原蛋白
结构
肽片段
溶解度
bream bone
collagen
structure
peptide fragments
solubility
