...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Applied Microbiology >Increased Crystalline Cellulose Activity via Combinations of Amino Acid Changes in the Family 9 Catalytic Domain and Family 3c Cellulose Binding Module of Thermobifida fusca Cel9A
【24h】

Increased Crystalline Cellulose Activity via Combinations of Amino Acid Changes in the Family 9 Catalytic Domain and Family 3c Cellulose Binding Module of Thermobifida fusca Cel9A

机译：通过在Thermobifida fusca Cel9A的9族催化域和3c家族纤维素结合模块中氨基酸变化的组合，提高结晶纤维素活性

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

摘要

Amino acid modifications of the Thermobifida fusca Cel9A-68 catalytic domain or carbohydrate binding module 3c (CBM3c) were combined to create enzymes with changed amino acids in both domains. Bacterial crystalline cellulose (BC) and swollen cellulose (SWC) assays of the expressed and purified enzymes showed that three combinations resulted in 150% and 200% increased activity, respectively, and also increased synergistic activity with other cellulases. Several other combinations resulted in drastically lowered activity, giving insight into the need for a balance between the binding in the catalytic cleft on either side of the cleavage site, as well as coordination between binding affinity for the catalytic domain and CBM3c. The same combinations of amino acid variants in the whole enzyme, Cel9A-90, did not increase BC or SWC activity but did have higher filter paper (FP) activity at 12% digestion.
机译：结合了Thermoififida fusca Cel9A-68催化结构域或碳水化合物结合模块3c（CBM3c）的氨基酸修饰，以创建两个结构域中氨基酸均发生变化的酶。表达和纯化的酶的细菌结晶纤维素（BC）和溶胀纤维素（SWC）分析表明，三种组合分别导致活性增加150％和200％，并且与其他纤维素酶的协同活性也增加。几种其他组合导致活性大大降低，从而深入了解了在裂解位点两侧的催化裂隙中的结合之间的平衡以及对催化域与CBM3c的结合亲和力之间的协调关系的需求。整个酶Cel9A-90中氨基酸变体的相同组合不会增加BC或SWC活性，但在12％的消化率下确实具有更高的滤纸（FP）活性。

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