弹性蛋白肽的制备工艺优化及其理化性质分析  

Optimization of Preparation Process of Elastin Peptides and Analysis of Their Physicochemical Properties

作　　者：李清岚 刘颖 崔春[1] LI Qing-an;LIU Ying;CUI Chun(College of Food Science and Engineering,South China University of Technology,Guangzhou 510640,China)

机构地区：[1]华南理工大学食品科学与工程学院,广州510640

出　　处：《中国调味品》2023年第6期189-194,220,共7页China Condiment

基　　金：国家自然科学基金项目(31201416);国家重点研发计划项目(2016YFD0400803)。

摘　　要：采用牛动脉弹性蛋白为原料,以弹性蛋白酶抑制活性和蛋白回收率为评价指标,研究弹性蛋白肽制备工艺和理化性质。结果表明,胰酶在酶添加量1.0%、pH 11、温度45℃和时间15 h的条件下酶解弹性蛋白,弹性蛋白酶抑制活性(蛋白浓度为10 mg/mL)为35.63%,蛋白回收率可达80.08%;弹性蛋白酶解过程中,部分β-折叠和α-螺旋转化为β-转角,酶解产物小于1000 Da的肽段占45.50%,富含疏水性氨基酸和芳香族氨基酸,具有较强还原力,清除DPPH和ABTS自由基的IC 50值分别为6.90,3.41 mg/mL,且在温度<85℃、pH为中性和碱性的条件下具有良好的稳定性。With bovine arterial elastin as the raw material,elastase inhibitory activity and protein recovery rate as the evaluation indexes,the preparation process and physicochemical properties of elastin peptides are studied.The results show that when elastin is hydrolyzed by pancreatin under the conditions of enzyme addition amount of 1.0%,pH of 11,temperature of 45℃and time of 15 h,the elastase inhibitory activity(protein concentration of 10 mg/mL)is 35.63%and the protein recovery rate is 80.08%.During the enzymolysis of elastin,someβ-folding andα-helix are converted intoβ-turn.In the enzymatic hydrolysate,the peptides less than 1000 Da account for 45.50%,which are rich in hydrophobic amino acids and aromatic amino acids,have strong reducing capacity,and the IC 50 of scavenging DPPH and ABTS radicals is 6.90,3.41 mg/mL respectively,and they have good stability at temperature<85℃,pH neutral and alkaline conditions.

关 键 词：弹性蛋白 胰酶 MMP-12抑制活性 蛋白回收率 理化性质 

分 类 号：TS201.2[轻工技术与工程—食品科学]