食品科学2016，Vol.37Issue(13)：168-172,5.DOI:10.7506/spkx1002-6630-201613030
白姑鱼胰蛋白酶的分离纯化及其性质分析
Purification and Characterization of Trypsin from White Croaker (Argyrosomus argentatus)
摘要
Abstract
An anionic trypsin (named as trypsin A) from the pyloric caeca of white croaker (Argyrosomus argentatus) was purified by ammonium precipitation, DEAE-Sepharose Fast Flow anion exchange chromatography and Sephacryl S-200 gel filtration chromatography. The characteristics of trypsin A were investigated. The results showed that trypsin A migrated as a single protein band with a molecular weight of about 28 kD in SDS-PAGE. Trypsin A exhibited its optimal temperature at 50℃and was stable below 65℃. Trypsin A revealed its optimal pH at 9.5 and was stable in the pH range from 9.5 to 11.0. The purified trypsin A was analyzed by western blotting using anti-common carp trypsin antibody, and the result showed that the active region of the trypsin was highly conservative. Serine proteinase inhibitors were effective against trypsin A.关键词
白姑鱼/胰蛋白酶/分离纯化/酶学性质Key words
white croaker/trypsin/separation and purification/enzymatic characteristics分类
轻工纺织引用本文复制引用
李欢,李婷,詹云超,杜翠红..白姑鱼胰蛋白酶的分离纯化及其性质分析[J].食品科学,2016,37(13):168-172,5.基金项目
厦门市海洋渔业局（南方海洋中心）项目（14CZP03HJ04）；福建省科技厅引导性项目 （）
