Characterization of Sphingomonas sp. JB13 exo-inulinase: a novel detergent-, salt-, and protease-tolerant exo-inulinase

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• 作者：Junpei Zhou ; Mozhen Peng ; Rui Zhang ; Junjun Li ; Xianghua Tang ; Bo Xu…
• 关键词：Inulinase ; Salt ; Protease ; Detergent ; Sphingomonas
• 刊名：Extremophiles
• 出版年：2015
• 出版时间：March 2015
• 年：2015
• 卷：19
• 期：2
• 页码：383-393
• 全文大小：2,770 KB
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• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Microbiology
  Biotechnology
  Ecology
  
• 出版者：Springer Japan
• ISSN：1433-4909

文摘

A glycoside hydrolase family 32 exo-inulinase gene was cloned from Sphingomonas sp. JB13 and expressed in Escherichia coli BL21 (DE3). The purified recombinant enzyme (rInuAJB13) showed an apparently optimal activity at pH 5.5 and 55?°C and remained activity at 10-0?°C. The addition of most metal ions and chemical reagents showed little or no effect (retaining more than 76.5?% activity) on the enzyme activity, notably the addition of surfactants SDS, CTAB, Tween 80, and Triton X-100. Most local liquid detergents, including Balin, Walch, Ariel, Tide, Tupperware, and Bluemoon, also showed little or no effect (retaining more than 77.8?% activity) on the enzyme activity. rInuAJB13 exhibited 135.3-63.6?% activity at the NaCl concentration of 1.0-.5?M. After incubation with up to 57.0?mg?mL? trypsin and 90.0?mg?mL? proteinase K at 37?°C for 60?min (pH 7.2), rInuAJB13 retained more than 80?% of its initial activity. The enzyme presents a high proportion (28.0?%) of amino acid residues G, A, and V. This paper is the first to report a detergent-, salt-, and protease-tolerant exo-inulinase.