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

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

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)1271-1275
Number of pages5
JournalBiotechnology progress
Volume32
Issue number5
DOIs
StatePublished - Sep 1 2016

Fingerprint

Amylases
Ethanol
Enzymes
Hot Temperature
Apoenzymes
Theoretical Models
Metals
Alcohols
Ions

All Science Journal Classification (ASJC) codes

  • Biotechnology

Cite this

@article{15fc4cd9a3d34b6cba6852ea72d1eb24,
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.",
author = "Calabrese, {Vincent T.} and Minns, {Jason W.} and Arshad Khan",
year = "2016",
month = "9",
day = "1",
doi = "10.1002/btpr.2308",
language = "English (US)",
volume = "32",
pages = "1271--1275",
journal = "Biotechnology Progress",
issn = "8756-7938",
publisher = "John Wiley and Sons Ltd",
number = "5",

}

Suppression of α-Amylase inactivation in the presence of ethanol : Application of a two-step model. / Calabrese, Vincent T.; Minns, Jason W.; Khan, Arshad.

In: Biotechnology progress, Vol. 32, No. 5, 01.09.2016, p. 1271-1275.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Suppression of α-Amylase inactivation in the presence of ethanol

T2 - Application of a two-step model

AU - Calabrese, Vincent T.

AU - Minns, Jason W.

AU - Khan, Arshad

PY - 2016/9/1

Y1 - 2016/9/1

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=84978656491&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84978656491&partnerID=8YFLogxK

U2 - 10.1002/btpr.2308

DO - 10.1002/btpr.2308

M3 - Article

C2 - 27253223

AN - SCOPUS:84978656491

VL - 32

SP - 1271

EP - 1275

JO - Biotechnology Progress

JF - Biotechnology Progress

SN - 8756-7938

IS - 5

ER -