Suppression of α-Amylase inactivation in the presence of ethanol: Application of a two-step model

Vincent T. Calabrese; Jason W. Minns; Arshad Khan

doi:10.1002/btpr.2308

Suppression of α-Amylase inactivation in the presence of ethanol: Application of a two-step model

Vincent T. Calabrese, Jason W. Minns, Arshad Khan

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Abstract

A number of years ago we reported a two-step inactivation mechanism for α-amylase (enzyme) on the basis of theoretical and experimental studies in aqueous solutions. In the first step the metal (Ca²⁺) ion dissociates reversibly from the enzyme followed by an irreversible thermal inactivation of the apoenzyme. In this study we report inactivation of the enzyme in the presence of ethanol–water solutions. We noticed that as the concentration of ethanol in the aqueous solution is increased, the thermal inactivation of the enzyme is suppressed with almost no inactivation (in 1 h, 30°C) when 50% alcohol is present in the solution. These results are explained by the two-step inactivation model.

Original language	English (US)
Pages (from-to)	1271-1275
Number of pages	5
Journal	Biotechnology progress
Volume	32
Issue number	5
DOIs	https://doi.org/10.1002/btpr.2308
State	Published - Sep 1 2016

All Science Journal Classification (ASJC) codes

Biotechnology

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10.1002/btpr.2308

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title = "Suppression of α-Amylase inactivation in the presence of ethanol: Application of a two-step model",

abstract = "A number of years ago we reported a two-step inactivation mechanism for α-amylase (enzyme) on the basis of theoretical and experimental studies in aqueous solutions. In the first step the metal (Ca2+) ion dissociates reversibly from the enzyme followed by an irreversible thermal inactivation of the apoenzyme. In this study we report inactivation of the enzyme in the presence of ethanol–water solutions. We noticed that as the concentration of ethanol in the aqueous solution is increased, the thermal inactivation of the enzyme is suppressed with almost no inactivation (in 1 h, 30°C) when 50% alcohol is present in the solution. These results are explained by the two-step inactivation model.",

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AU - Khan, Arshad

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AB - A number of years ago we reported a two-step inactivation mechanism for α-amylase (enzyme) on the basis of theoretical and experimental studies in aqueous solutions. In the first step the metal (Ca2+) ion dissociates reversibly from the enzyme followed by an irreversible thermal inactivation of the apoenzyme. In this study we report inactivation of the enzyme in the presence of ethanol–water solutions. We noticed that as the concentration of ethanol in the aqueous solution is increased, the thermal inactivation of the enzyme is suppressed with almost no inactivation (in 1 h, 30°C) when 50% alcohol is present in the solution. These results are explained by the two-step inactivation model.

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Suppression of α-Amylase inactivation in the presence of ethanol: Application of a two-step model

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