摘要
采用Alcalase 2.4 L、Protamex、Papain、PTN6.0 S、Flavorzyme500 MG水解泥鳅蛋白,探讨了各种酶的酶解特性、产物营养组成和清除DPPH.活性的差异。结果表明,PTN6.0 S和Papain酶解产物的蛋白质利用率、肽得率和水解度均较高。各酶解产物的谷氨酸、色氨酸、天冬氨酸的含量都很高;酶解产物中的氨基酸组成较原料泥鳅蛋白更接近FAO/WHO推荐的成人模式。各种酶均能降解泥鳅蛋白中分子量大于3000 Da的片断,产物中以分子量小于500 Da的肽段为主。Alacalase 2.4 L的酶解产物清除DPPH.的能力最强,其次为PTN6.0 S酶解产物、Protamex酶解产物,而Flavorzyme 500 MG酶解产物清除DPPH.的能力最弱。
Loach protein was hydrolyzed by Alcalase 2.4 L, Protamex, Papain, PTN 6.0 S and Flavorzyme 500 MG to study the characteristics of different enzymes, as well as the nutritional compositions and scavenging activity on DPPH · of different protein hydrolysates. Results revealed that the protein utilization, the extraction rate of peptides, and the degree of hydrolysis of PTN 6.0 S and Papain hydrolysates were higher than those of others. All of the hydrolysates were rich in glutamic acid, tryptophan and aspartate. The amino acid compositions of hydrolysates were closer to the reference pattern of amino acids. The fractions with molecular weight more than 3000 Da could be hydrolyzed by all of the enzymes. The fractions with molecular weight less than 500 Da were in the main components. The hydrolysate using Alcalase 2.4 L had the strongest scavenging activity on DPPH · . Inferior to it were the hydrolysates of PTN 6.0 S and Protamex. The hydrolysate using Flavor＇zymeS00 MG had the weakest scavenging activity on DPPH · .
出处
《四川大学学报（工程科学版）》
EI
CAS
CSCD
北大核心
2008年第1期74-80,共7页
Journal of Sichuan University (Engineering Science Edition)
基金
国家十一五科技支撑计划资助项目(2006BAD27B03)
广东省科技计划资助项目(2006A25006001)
关键词
泥鳅蛋白
酶解
氨基酸组成
分子量分布
清除DPPH·活性
loach protein
hydrolysis
amino acid composition
distribution profile of peptide molecular weight
scavenging activity on DPPH ·
