文章摘要
引用本文: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
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
  
DOI:10.7631/issn.1000-2243.16334
中文关键词: 褐藻胶裂解酶  假交替单胞菌  纯化  酶学性质
英文关键词: alginate lyase  Pseudoalteromonas sp.  purification  enzymatic property
基金项目:
作者单位
韩 伟 福州大学生物科学与工程学院福建省海洋酶工程重点实验室福建 福州 350116 
许鑫琦 福州大学生物科学与工程学院福建省海洋酶工程重点实验室福建 福州 350116 
叶秀云 福州大学生物科学与工程学院福建省海洋酶工程重点实验室福建 福州 350116 
林 娟 福州大学生物科学与工程学院福建省海洋酶工程重点实验室福建 福州 350116 
摘要点击次数: 217
全文下载次数: 128
中文摘要:
      以假交替单胞菌(Pseudoalteromonas sp. zb7-4)发酵制备褐藻胶裂解酶粗酶液,采用弱阴离子DEAE交换层析分离褐藻胶裂解酶,分析纯化褐藻胶裂解酶AlgL的酶学特性. 结果表明:AlgL的表观分子质量约为32ku,比活力为(208.26±5.87)U·mg-1;其最适反应pH为7.0,在pH为6.0~10.0范围内稳定性较好,保温1h仍能保持80%以上的相对酶活力;最适反应温度50℃,在40℃保温30min,其残余酶活力高于80%;Cu2+、Cr3+、Co2+、Ba2+、Sr2+、Hg2+对该酶具有不同程度的抑制作用,Hg2+抑制作用最为明显;该酶具有较好的盐耐受性,在3mol·L-1 NaCl反应体系中保温2h,仍残余66%酶活力. 动力学参数KmVmaxKcat测定表明,该酶对聚古罗糖醛酸钠(PG)亲和力较高,为偏好聚甘露糖醛酸钠(PM)裂解作用的双功能酶.
英文摘要:
      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 32ku 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 3mol·L-1 NaCl. The values of KmVmaxKcat showed that the enzyme was a bifunctional enzyme which prefered sodium polymannuronate (Poly M).
查看全文   查看/发表评论  下载PDF阅读器
关闭