Significant Enhancement of Structural Stability of the Hyperhalophilic ADH from Haloferax volcanii via Entrapment on Metal Organic Framework Support

被引：25
作者：
Carucci, Cristina [1 ]
Bruen, Larah [2 ]
Gascon, Victoria [1 ]
Paradisi, Francesca [2 ,3 ]
Magner, Edmond [1 ]
机构：
[1] Univ Limerick, Bernal Inst, Dept Chem Sci, Limerick V94 T9PX, Ireland
[2] Univ Coll Dublin, Ctr Synth & Chem Biol, Dublin 4, Ireland
[3] Univ Nottingham, Sch Chem, Univ Pk Campus, Nottingham NG7 2RD, England
来源：
LANGMUIR | 2018年 / 34卷 / 28期
基金：
爱尔兰科学基金会;
关键词：
ALCOHOL-DEHYDROGENASE ADH2; ENZYME IMMOBILIZATION; BIOCATALYTIC SYNTHESIS; FACILE SYNTHESIS; IN-SITU; MOF; PROTEINS; STABILIZATION; ENCAPSULATION; MIL-100(FE);
D O I：
10.1021/acs.langmuir.8b01037
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
The use of an in situ immobilization procedure for the immobilization of hyperhalophilic alcohol dehydrogenase in a metal organic framework material is described. The easy and rapid in situ immobilization process enables retention of activity over a broad range of pH and temperature together with a decrease in the halophilicity of the enzyme. The catalytic activity of the immobilized enzyme was studied in nonaqueous solvent mixtures with the highest retention of activity in aqueous solutions of methanol and acetonitrile. The approach demonstrates that this immobilization method can be extended to hyperhalophilic enzymes with enhancements in activity and stability.
引用
收藏
页码：8274 / 8280
页数：7
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