...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >Mechanism of solvent induced thermal stabilization of papain
【24h】

Mechanism of solvent induced thermal stabilization of papain

机译：溶剂诱导木瓜蛋白酶热稳定的机理

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

In the present study an attempt is made to elucidate the effects of various cosolvents, such as sorbitol, sucrose, xylose and glycerol, on papain. The stabilizing effects of these cosolvents on the structure and function of papain is determined by the activity measurements, fluorescence spectroscopy and differential scanning calorimetry (DSC). The enzyme activity measurements indicate several fold increase in the thermal stability of the enzyme in all the cosolvents used. The thermal denaturation studies of papain in presence of various concentrations of cosolvents indicated a shift in the apparent thermal denaturation temperature (app T-m) suggesting increased thermal stability of papain in presence of cosolvents. The app T-m shifted from a control value of 83 +/- 1 degrees C to a value of >90 +/- 1 degrees C in presence of 40% sorbitol. The DSC thermogram for native papain can be clearly deconvoluted into two transitions corresponding to left and right domain and in presence of cosolvents both transitions A and B shift to higher temperature. Maximum stabilization was seen in case of 30% sorbitol where the thermal transition temperatures increased compared to control. The results from partial specific volume measurements of papain in presence of cosolvents suggest that the preferential interaction parameter (xi(3)) was negative in all cosolvents and maximum hydration was observed in the case of glycerol where the preferential interaction parameter was 0.165 g/g. These above results suggest that there is a considerable increase in the thermal stability of papain in presence of these cosolvents as a result of preferential hydration. (C) 2007 Elsevier B.V. All rights reserved.
机译：在本研究中，试图阐明各种助溶剂如山梨糖醇，蔗糖，木糖和甘油对木瓜蛋白酶的作用。这些助溶剂对木瓜蛋白酶的结构和功能的稳定作用由活性测量，荧光光谱和差示扫描量热法（DSC）确定。酶活性的测定表明，在所有使用的助溶剂中，酶的热稳定性提高了几倍。在各种浓度的助溶剂存在下木瓜蛋白酶的热变性研究表明，表观热变性温度（app T-m）发生变化，表明在存在助溶剂下木瓜蛋白酶的热稳定性提高。在存在40％山梨糖醇的情况下，应用程序T-m从83 +/- 1摄氏度的控制值转变为> 90 +/- 1摄氏度的值。天然木瓜蛋白酶的DSC热分析图可以清楚地解卷积为对应于左域和右域的两个转变，并且在存在助溶剂的情况下，转变A和B都转移到更高的温度。在30％山梨糖醇的情况下，可以看到最大的稳定性，其中热转变温度比对照高。木瓜蛋白酶在共溶剂存在下的部分比容测量结果表明，在所有共溶剂中，优先相互作用参数（xi（3））均为负，在甘油中，优先相互作用参数为0.165 g / g时观察到最大水化。这些以上结果表明，由于优先水合，在这些助溶剂存在下木瓜蛋白酶的热稳定性有显着提高。 （C）2007 Elsevier B.V.保留所有权利。

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