Characterization of casein hydrolysates derived from enzymatic hydrolysis
Characterization of casein hydrolysates derived from enzymatic hydrolysis
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酶水解酪蛋白水解产物的表征
DOI：
10.1186/1752-153x-7-62
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发表时间：
2013-04-04
影响因子：
--
通讯作者：
Jin, Huali
中科院分区：
文献类型：
--
作者：
Wang, Jinshui;Su, Yinjie;Jin, Huali
酪蛋白是牛奶中的主要蛋白质成分，因其在食品、医药和化妆品工业中的广泛应用以及作为阐明蛋白质化学基本问题的重要研究材料而引起人们的兴趣。酶解是修饰蛋白质结构以增强蛋白质功能性质的一种重要方法。结果在酶解过程中，酪蛋白水解物的水解度在最初的20分钟内迅速升高，45分钟后达到平台期，然后在接下来的时间里保持相对恒定。随着水解度的增加，相对分子质量大于50kD的多肽的相对百分含量显著降低，而相对分子质量在30~50kD和小于20kD的多肽的相对百分含量显著增加。水解液中α-螺旋和β-TURN的含量较原酪蛋白有所增加。此外，用α-螺旋与β-结构的比值来评价酪蛋白水解物的分子柔韧性也低于酪蛋白原蛋白。结论与对照样品相比，酪蛋白水解物的分子质量分布和结构特征发生了显著变化。这一变化应该是增强功能性质的基础。
BackgroundCasein is the main proteinaceous component of milk and has made us interest due to its wide applications in the food, drug, and cosmetic industries as well as to its importance as an investigation material for elucidating essential questions regarding the protein chemistry. Enzymatic hydrolysis is an important method commonly used in the modification of protein structure in order to enhance the functional properties of proteins. The relationship between enzymatic hydrolysis and structure change of casein need to make more study.ResultsDuring hydrolysis, degree of hydrolysis in the casein hydrolysates increased rapidly in the initial 20 minutes, reached a plateau after 45 minutes, and then kept relative constant for the rest of the hydrolysis. The relative percentage of the released peptides with molecular weight of over 50 kD significantly decreased with hydrolyzation, while those with MW of 30–50 kD and below 20 kD increased significantly. The contents of a-helix and β-turn in the hydrolysates increased compared to the original casein. Moreover, the molecular flexibilities of the casein hydrolysates, estimated by the ratio of α-helix to β-structure, were lower than that of original casein protein.ConclusionsThe significant changes in molecular weight distribution and structure characteristics of casein hydrolysates were found compared to the control sample. This change should be the basis of enhancement of functional properties.