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Purification, properties and mass spectrometry analysis of two novel thermotolerant endoglucanases from Bacillus akihai I -2

机译:来自Bacillus akihai I -2的两种新型热能内荧光酶的纯化,性质和质谱分析

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The alkaliphilic bacterium strain I -2, which was isolated from soda lakes, was identified as Bacillus akibai by 16S rRNA sequence analysis and suggested to be a new subspecies of genus Bacillus. Two novel thermotolerant alkaline endoglucanases I -2-A and I -2-B were produced by this alkaliphilic strain. The purified I -2-A and I -2-B had molecular mass of approximately 60 and 90 kDa, respectively. The optimum pH of I -2-A was about 9.0, while that of I -2-B was about 8.0. Both enzymes exhibited maximum activity at around 50 °C and were stable up to 50 °C .The two enzymes were resistant to most metal ions and reagents examined. Mass spectrometry analysis indicated that I -2-A was probably different from the endoglucanases reported. I -2-B showed homology with those of family A5 endoglucanases but low similarity was found in C-terminal amino acid sequence.
机译:从苏打湖中分离的碱性细菌菌株I -2被鉴定为Bacillus akibai,通过16S rRNA序列分析,并表明是芽孢杆菌属的新亚种。通过该碱性菌株生产两种新型热辐射性碱性内切糖酶I-2 -A和I -2-B.纯化的I-2 -A和I-2 -B分别具有约60和90kDa的分子量。 I-2-A的最佳pH约为9.0,而I -2-B的最佳pH约为8.0。这两种酶在约50℃的最大活性上表现出最大的活性,并且稳定至50℃。两种酶对大多数金属离子和检测的试剂抗性。质谱分析表明I -2-A可能与报告的内切葡聚糖酶不同。 I -2-B显示与家庭A5内切葡聚糖酶的同源性,但在C末端氨基酸序列中发现了低相似性。

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