Specific anion effects on enzymatic activity in nonaqueous media

The Journal of Physical Chemistry. B
Dagmar BilanicováMaura Monduzzi

Abstract

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.

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Citations

Jan 19, 2012·Chemical Reviews·Pierandrea Lo Nostro, Barry W Ninham
Aug 10, 2012·Journal of the American Chemical Society·Carlo Augusto BortolottiIsabella Daidone
Jul 5, 2011·The Journal of Physical Chemistry. a·Mario VazdarPavel Jungwirth
Jun 23, 2011·Langmuir : the ACS Journal of Surfaces and Colloids·Mathias BoströmMaura Monduzzi
Aug 13, 2011·Langmuir : the ACS Journal of Surfaces and Colloids·Andrea SalisMaura Monduzzi
Jun 15, 2011·Physical Chemistry Chemical Physics : PCCP·Drew F ParsonsBarry W Ninham
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May 2, 2012·The Journal of Physical Chemistry. B·Diana LousaCláudio M Soares
Dec 24, 2020·The Journal of Physical Chemistry Letters·Denilson Mendes de Oliveira, Dor Ben-Amotz

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