吉林大学学报（理学版）Issue(5)：1054-1059,6.DOI:10.13413/j.cnki.jdxblxb.2015.05.43
玉米半胱氨酸蛋白酶的原核表达及酶学性质表征
Prokaryotic Expression and Characterization of Cysteine Protease from Zea mays
摘要
Abstract
Cysteine protease from Zea mays (zmCP1)was cloned by PCR with corn genome DNA as template,and ligated to pET28a(+),expressed in E .coli BL21(DE3).The recombinant enzyme was identified by SDS-PAGE and Western blotting, finally purified through Ni-chelating affinity chromatography.The purity can reach 95%.The properties characterization of zmCP1 showed that the optimal temperature was 55 ℃,and the optimal pH was 6.0,the half-time was 39.82 min at 90 ℃.The enzyme kinetics researches with R-AMC and LAFR-AMC as substrate show that zmCP1 has better affinity and catalytic activity to small substrate.关键词
玉米/半胱氨酸蛋白酶/原核表达/酶学性质Key words
Zea mays/cysteine protease/prokaryotic expression/enzyme properties分类
生物科学引用本文复制引用
刘回民,陈方奇,郑明珠,程国栋,詹冬玲,刘景圣..玉米半胱氨酸蛋白酶的原核表达及酶学性质表征[J].吉林大学学报（理学版）,2015,(5):1054-1059,6.基金项目
国家自然科学基金(批准号:31171760)、公益性行业(粮食)科技专项基金(批准号:201313011-3)和吉林农业大学科研启动基金 （批准号:31171760）
