福州大学学报（自然科学版）2018，Vol.46Issue(1)：136-142,7.DOI:10.7631/issn.1000-2243.16334
海洋来源褐藻胶裂解酶分离纯化及酶学性质研究
Purification and characterization of the alginate lyase isolated from marine
摘要
Abstract
Alginate lyase AlgL was successfully purified from fermented broth of Pseudoalteromonas sp.zb7-4 by DEAE weak anion exchange chromatography and the enzymatic properties of alginate lyase were characterized.The results showed that the purified alginate lyase was a monomer with apparent molecular weight of approximately 32 ku and specific activity of (208.26±5.87)U · mg-1.The optimum pH for enzyme was 7.0,it was stable in the pH range of 6.0 to 10.0,and its relative enzyme activity could still maintain more than 80％ after 1 h' s incubation.The optimum temperature for enzyme was 50 ℃,and its residual enzyme activity was still 80％ after 30 min' s incubation at 40 ℃.Cu2+,Cr3+,Co2+,Ba2+,Sr2+,Hg2+ showed inhibitory effects on the enzyme activity while Hg2+ was the most obvious.The enzyme had a good ability of salt tolerance,and its relative enzyme activity retained more than 66％ after 2 h' s incubation in 3 mol · L-1 NaCl.The values of Km 、Vmax、Kcat,showed that the enzyme was a bifunctional enzyme which prefered sodium polymannuronate (Poly M).关键词
褐藻胶裂解酶/假交替单胞菌/纯化/酶学性质Key words
alginate lyase/Pseudoalteromonas sp./purification/enzymatic property分类
生物科学引用本文复制引用
韩伟,许鑫琦,叶秀云,林娟..海洋来源褐藻胶裂解酶分离纯化及酶学性质研究[J].福州大学学报（自然科学版）,2018,46(1):136-142,7.基金项目
福州市科技计划资助项目(2016-G-42) （2016-G-42）
海洋经济创新发展区域示范项目(2014FJPT02) （2014FJPT02）
福建省企业技术创新资助项目(闽经信投资[2015] 205号) （闽经信投资[2015] 205号）
