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

Cristina Carucci; Larah Bruen; Victoria Gascón; Francesca Paradisi; Edmond Magner

doi:10.1021/acs.langmuir.8b01037

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

Cristina Carucci, Larah Bruen, Victoria Gascón, Francesca Paradisi, Edmond Magner

Department of Chemical Sciences

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Pages (from-to)	8274-8280
Number of pages	7
Journal	Langmuir
Volume	34
Issue number	28
DOIs	https://doi.org/10.1021/acs.langmuir.8b01037
Publication status	Published - 17 Jul 2018

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10.1021/acs.langmuir.8b01037

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abstract = "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.",

author = "Cristina Carucci and Larah Bruen and Victoria Gasc{\'o}n and Francesca Paradisi and Edmond Magner",

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AU - Carucci, Cristina

AU - Bruen, Larah

AU - Gascón, Victoria

AU - Paradisi, Francesca

AU - Magner, Edmond

PY - 2018/7/17

Y1 - 2018/7/17

N2 - 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.

AB - 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.

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U2 - 10.1021/acs.langmuir.8b01037

DO - 10.1021/acs.langmuir.8b01037

M3 - Article

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SN - 0743-7463

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JO - Langmuir

JF - Langmuir

IS - 28

ER -

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

Abstract

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