登录    注册    忘记密码    使用帮助

详细信息

南美白对虾虾头内源酸性蛋白酶的分离纯化及其酶学特性研究     被引量:10

Purification and characteristics of endogenous acid protease from shrimp head of Litopenaeus vannamei

文献类型:期刊文献

中文题名:南美白对虾虾头内源酸性蛋白酶的分离纯化及其酶学特性研究

英文题名:Purification and characteristics of endogenous acid protease from shrimp head of Litopenaeus vannamei

作者:庄志凯[1,2];杜嵇华[1];吉宏武[2];连文伟[1]

机构:[1]中国热带农业科学院农业机械研究所,广东湛江524091;[2]广东海洋大学食品科技学院,广东湛江524088

年份:2012

卷号:33

期号:18

起止页码:116

中文期刊名:食品工业科技

外文期刊名:Science and Technology of Food Industry

收录:CSTPCD、、北大核心2011、CSCD2011_2012、北大核心、CSCD

基金:国家科技支撑计划项目(2007BAD29B09);国家科技支撑计划和政策引导项目(2008BAD94B08);广东省科技计划项目(2008A020100002)

语种:中文

中文关键词:南美白对虾虾头;内源酸性蛋白酶;分离纯化;酶学性质

外文关键词:Litopenaeus vannamei shrimp head; endogenous acid protease; purification; enzymatic characteristics

中文摘要:通过10%~50%的硫酸铵盐析和两次柱层析,从南美白对虾虾头的匀浆液中分离纯化出一种内源酸性蛋白酶,经电泳分析测得其分子量为27.45ku,该酶的Km值、Vmax值、最适pH和最适反应温度分别为2.01g/L、26.39μg/min、3.0和30℃。内源酸性蛋白酶的热稳定性较差,Pepstatin A和EDTA对该蛋白酶表现出强烈的抑制作用,Hg+能完全抑制该蛋白酶,但Ca2+却能激活该蛋白酶。据此推断该蛋白酶是一种金属蛋白酶,该酶活性中心含有一些金属离子,其性质类似于胃蛋白酶类。

外文摘要:Endogenous acid protease was purified from a shrimp head homogenate of Litopenaeus vannamei by 10%~50% of ammonium sulfate fractions and twice chromatography.Its molecular weight was estimated to be 27.45ku by SDS-PAGE electrophoresis and its apparent Km,Vmax,optimal pH and optimal temperature for casein were 2.01g/L,26.39μg/min,3.0 and 30℃,respectively.The endogenous acid protease had weak thermostability and could be significantly inhibited by Pepstatin A,EDTA and Hg+,but activated by Ca2+.It's inferred the protease from Litopenaeus vannamei shrimp head was a kind of Metalloproteases and that activity centers might also contain small amounts of metalions,the property of the enzyme was similar to the pepsin.

参考文献:

正在载入数据...

版权所有©广东海洋大学 重庆维普资讯有限公司 渝B2-20050021-8 
渝公网安备 50019002500408号 违法和不良信息举报中心