Characterization of an arylsulfatase from a mutant library of Pseudoalteromonas carrageenovora arylsulfatase

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• 作者：Yanbing Zhu^a ; ^b ; ^c ; ^d ; Han Liu^a ; Chaochao Qiao^a ; Lijun Li^a ; ^b ; ^c ; ^d ; Zedong Jiang^a ; ^b ; ^c ; ^d ; Anfeng Xiao^a ; ^b ; ^c ; ^d ; Hui Ni^a ; ^b ; ^c ; ^d ; ^{nihui@jmu.edu.cn} ; ^{nihui1973@yahoo.com.cn}
• 关键词：H260L ; mutant arylsulfatase H260L ; WT ; wild-type arylsulfatase ; pNPS ; p-nitrophenyl sulfate ; IPTG ; isopropyl-β-d-thiogalactopyranoside ; SDS-PAGE ; sodium dodecyl sulfate-polyacrylamide gel electrophoresis ; EDTA ; ethylenediaminetetraacetic acid ; β-ME ; β-mercaptoethanol ; DTT ; dithiothreitol ; SD ; standard deviation
• 刊名：International Journal of Biological Macromolecules
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：96
• 期：Complete
• 页码：370-376
• 全文大小：1231 K
• 卷排序：96

文摘

A library of Pseudoalteromonas carrageenovora arylsulfatase mutants was constructed based on error-prone PCR method. We obtained a mutant arylsulfatase H260L with improved thermal stability. This mutant arylsulfatase exhibited stability across a pH range of 6.0–9.0. It had a relatively good resistance against some detected detergents. We identified the desulfation activity of H260L for the sulfate groups in Gracilaria lemaneiformis agar.