摘要
为了制备山羊乳酪蛋白活性肽,选用中性蛋白酶、胰蛋白酶、木瓜蛋白酶和碱性蛋白酶,采用对比和正交试验方法,研究山羊乳酪蛋白单酶和复合酶的酶解工艺,测定山羊乳酪蛋白的总肽键物质的量,优选出山羊乳酪蛋白的酶解工艺参数,初步研究羊乳酪蛋白酶解液的抗氧化活性。结果表明:山羊乳酪蛋白的总肽键物质的量为8.5379mmol/g。单酶中胰蛋白酶和中性蛋白酶对山羊乳酪蛋白的水解度较大,碱性蛋白酶较小。胰蛋白酶对山羊乳酪蛋白适宜的酶解工艺条件为加酶量2500U/g、pH7.5、50℃条件下酶解2h。中性蛋白酶和胰蛋白酶复合,胰蛋白酶和碱性蛋白酶复合的水解度较大,其水解度、平均肽链长度和平均相对分子量分别为17.34%、16.40%,5.77、6.10和692、732。中性蛋白酶单酶,胰蛋白酶和碱性蛋白酶复合的羊乳酪蛋白酶解液的抗氧化活性较强。
In order to prepare highly active peptides derived from goa t s milk casein （GMC）, the enzymolysis technology for GMC with neutral protease, trypsin, papain or alkaline protease was optimized using orthogonal array design. Based on this, these enzymes were combined pairwise for achieving a maximum amino nitrogen content in GMC hydrolyaste. Meanwhile, the antioxidant activity of GMC hydrolyastes prepared via single enzyme or double enzyme hydrolysis was also evaluated by DPPH radical scavenging assay. Results showed that a content of total peptide substances of 8.5379 mmol/g was exhibited in GMC. For single enzyme hydrolysis, neutral protease and trypsin could hydrolyze GMC with higher degree of hydrolysis when compared to alkaline protease; for double enzyme hydrolysis, the combination of trypsin with neutral protease or alkaline protease exhibited higher degree of hydrolysis than other combinations, and the corresponding values of degree of hydrolysis, average peptide chain length and average relative molecular weights were 17.34%, 5.77 and 692 for neutral protease ＋ trypsin and 16.40%, 6.10 and 732 for trypsin ＋ alkaline protease, respectively. Additionally, neutral protease and trypsin ＋ alkaline protease hydrolysates of GMC displayed stronger DPPH radical scavenging activity than other hydrolysates.
出处
《食品科学》
EI
CAS
CSCD
北大核心
2009年第21期252-257,共6页
Food Science
基金
"十一五"国家科技支撑计划项目(2006BAD04A11)
西北农林科技大学科研专项项目(07ZR005)
关键词
山羊乳酪蛋白
酶解工艺
蛋白酶
氨基态氮含量
抗氧化
goat s milk casein（GMC）
enzymolysis technology
protease
amino nitrogen content
antioxidant
