...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>American Journal of Biochemistry >A Novel Thermotolerant β-glucosidase from Aspergillus nidulans has Activity across a Broad pH Profile and a Likely Bacterial Origin
【24h】

A Novel Thermotolerant β-glucosidase from Aspergillus nidulans has Activity across a Broad pH Profile and a Likely Bacterial Origin

机译：构巢曲霉的新型耐热β-葡萄糖苷酶具有广泛的pH分布和可能的细菌来源的活性

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

This study reports the purification and characterization of a recombinant β-glucosidase expressed from an AOX1 promoter in Pichia pastoris carrying an Aspergillus nidulans (A. nidulans) cloned gene. β-glucosidase was optimally active at 50°C and pH 5.5, though it had a broad pH range of pH 3.0 – 10.0 and a broad temperature range of 10 – 80°C. β-glucosidase showed very high affinity to para-Nitrophenyl β-D-glucopyranoside (pNPG). Evidence for a bacterial origin of this gene (AN1804) was provided by the absence of introns, absence of some fungal specific amino acid insertions in its encoded protein sequence, automatic annotation as “periplasmic” and unusual positions in phylogenetic trees showing similarities to bacterial proteins.
机译：这项研究报告了从 AOX1 启动子表达的重组β-葡萄糖苷酶的纯化和表征，所述启动子在携带曲霉菌的毕赤酵母 i> nidulans （ A。 nidulans ）克隆的基因。 β-葡糖苷酶在50°C和pH 5.5时具有最佳活性，尽管它的pH范围在pH 3.0-10.0范围内，温度在10-80°C范围内。 β-葡萄糖苷酶对对硝基苯基β-D-吡喃葡萄糖苷（pNPG）具有很高的亲和力。该基因（AN1804）细菌起源的证据是由于没有内含子，在其编码的蛋白质序列中没有某些真菌特异性氨基酸插入，自动注释为“周质”以及系统树中与细菌蛋白质相似的异常位置。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号