Specific anion effects on enzymatic activity in nonaqueous media

被引：60

作者：

Bilanicova, Dagmar ^{[1
,3
]}

Salis, Andrea ^{[1
]}

Ninham, Barry W. ^{[2
]}

Monduzzi, Maura ^{[1
]}

机构：

[1] Univ Cagliari CSGI Cittadella Monserrato, Dept Chem Sci, I-09042 Monserrato, Italy

[2] Australian Natl Univ, Dept Appl Math, Canberra, ACT, Australia

[3] Slovak Tech Univ, Dept Food Technol & Biotechnol, Bratislava, Slovakia

来源：

JOURNAL OF PHYSICAL CHEMISTRY B | 2008年 / 112卷 / 38期

关键词：

D O I：

10.1021/jp805451w

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The present work shows that salt anions affect the activity of Pseudomonas cepacia lipase both in aqueous and in nonaqueous media (NAM) according to a Hofmeister series. The biocatalytic assay in water was the hydrolysis of p-nitrophenyl acetate, whereas the esterification between 1-hexyl-beta-D-galactopyranoside and palmitic acid was followed in an organic solvent. The solid lipase preparations to be used in NAM were obtained through lyophilization in the presence of concentrated solutions of Hofmeister salts (Na2SO4, NaH2PO4/Na2HPO4, NaCl, NaBr, NaI, NaSCN). Salts affect enzyme activity in organic media through two mechanisms: (1) enzyme protection during lyophilization; (2) enzyme activation during the reaction. At least in our case, the latter seems to be more important than the former. The decrease of the activation energy caused by the stabilization of the transition state due to "kosmotropic" anions might be the driving force of enzyme activation. According to the most recent findings, dispersion forces may be responsible of specific anion enzyme activation/deactivation in NAM.

引用

页码：12066 / 12072

页数：7

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