Inactivation of α-amylase from Bacillus amyloliquefaciens at low moisture contents

J. Saraiva; S. De Cordt; M. Hendrickx; J. Oliveira; P. Tobback

doi:10.1016/B978-0-444-89372-7.50060-9

Inactivation of _α-amylase from Bacillus amyloliquefaciens at low moisture contents

J. Saraiva
, S. De Cordt
, M. Hendrickx
, J. Oliveira
, P. Tobback

Research output: Chapter in Book/Report/Conference proceedings › Chapter › peer-review

Abstract

The thermal inactivation characteristics of dehydrated α-amylase in solid state at various moisture contents was studied at temperatures between 135 and 150°C. The inactivation kinetics show a first order decay. The enzyme was found to be more thermostable than in aqueous solution. The z-value dependency with moisture content has shown some fluctuactions, having an absolut minimum of 19°C at 23.9% moisture.

Original language	English
Title of host publication	Studies in Organic Chemistry
Pages	459-466
Number of pages	8
Edition	C
DOIs	https://doi.org/10.1016/B978-0-444-89372-7.50060-9
Publication status	Published - 1 Jan 1993
Externally published	Yes

Publication series

Name	Studies in Organic Chemistry
Number	C
Volume	47
ISSN (Print)	0165-3253

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10.1016/B978-0-444-89372-7.50060-9

Cite this

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title = "Inactivation of α-amylase from Bacillus amyloliquefaciens at low moisture contents",

abstract = "The thermal inactivation characteristics of dehydrated α-amylase in solid state at various moisture contents was studied at temperatures between 135 and 150°C. The inactivation kinetics show a first order decay. The enzyme was found to be more thermostable than in aqueous solution. The z-value dependency with moisture content has shown some fluctuactions, having an absolut minimum of 19°C at 23.9\% moisture.",

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AU - Oliveira, J.

AU - Tobback, P.

PY - 1993/1/1

Y1 - 1993/1/1

N2 - The thermal inactivation characteristics of dehydrated α-amylase in solid state at various moisture contents was studied at temperatures between 135 and 150°C. The inactivation kinetics show a first order decay. The enzyme was found to be more thermostable than in aqueous solution. The z-value dependency with moisture content has shown some fluctuactions, having an absolut minimum of 19°C at 23.9% moisture.

AB - The thermal inactivation characteristics of dehydrated α-amylase in solid state at various moisture contents was studied at temperatures between 135 and 150°C. The inactivation kinetics show a first order decay. The enzyme was found to be more thermostable than in aqueous solution. The z-value dependency with moisture content has shown some fluctuactions, having an absolut minimum of 19°C at 23.9% moisture.

UR - https://www.scopus.com/pages/publications/84990455060

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DO - 10.1016/B978-0-444-89372-7.50060-9

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T3 - Studies in Organic Chemistry

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BT - Studies in Organic Chemistry

ER -

Inactivation of _α-amylase from Bacillus amyloliquefaciens at low moisture contents

Abstract

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