Specific anion effects on enzymatic activity in nonaqueous media

Dagmar Bilaničová; Andrea Salis; Barry W. Ninham; Maura Monduzzi

doi:10.1021/jp805451w

Specific anion effects on enzymatic activity in nonaqueous media

Dagmar Bilaničová, Andrea Salis^*, Barry W. Ninham, Maura Monduzzi

^*Corresponding author for this work

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

63 Citations (Scopus)

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-β-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 (Na ₂SO₄, NaH₂PO₄/ Na ₂HPO₄, NaCl, NaBr, Nal, 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.

Original language	English
Pages (from-to)	12066-12072
Number of pages	7
Journal	Journal of Physical Chemistry B
Volume	112
Issue number	38
DOIs	https://doi.org/10.1021/jp805451w
Publication status	Published - 25 Sept 2008

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title = "Specific anion effects on enzymatic activity in nonaqueous media",

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-β-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 (Na 2SO4, NaH2PO4/ Na 2HPO4, NaCl, NaBr, Nal, 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.",

author = "Dagmar Bilani{\v c}ov{\'a} and Andrea Salis and Ninham, {Barry W.} and Maura Monduzzi",

year = "2008",

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doi = "10.1021/jp805451w",

language = "English",

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T1 - Specific anion effects on enzymatic activity in nonaqueous media

AU - Bilaničová, Dagmar

AU - Salis, Andrea

AU - Ninham, Barry W.

AU - Monduzzi, Maura

PY - 2008/9/25

Y1 - 2008/9/25

N2 - 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-β-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 (Na 2SO4, NaH2PO4/ Na 2HPO4, NaCl, NaBr, Nal, 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.

AB - 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-β-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 (Na 2SO4, NaH2PO4/ Na 2HPO4, NaCl, NaBr, Nal, 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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U2 - 10.1021/jp805451w

DO - 10.1021/jp805451w

M3 - Article

SN - 1520-6106

VL - 112

SP - 12066

EP - 12072

JO - Journal of Physical Chemistry B

JF - Journal of Physical Chemistry B

IS - 38

ER -

Specific anion effects on enzymatic activity in nonaqueous media

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