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 proceeding › Conference contribution › peer-review

3 Citations (Scopus)

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	Stability and stabilization of enzymes
Editors	W. J. J. Van Den Tweel, A. Harder, R. M. Buitelaar
Publisher	Elsevier
Pages	459-466
Number of pages	8
DOIs	https://doi.org/10.1016/B978-0-444-89372-7.50060-9
Publication status	Published - 1 Jan 1993
Event	Proceedings of an International Symposium - Maastricht, Netherlands Duration: 22 Nov 1992 → 25 Nov 1992

Publication series

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

Conference

Conference	Proceedings of an International Symposium
Country/Territory	Netherlands
City	Maastricht
Period	22/11/92 → 25/11/92

Access to Document

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

Cite this

Saraiva, J., Cordt, S. D., Hendrickx, M., Oliveira, J., & Tobback, P. (1993). Inactivation of _α-amylase from Bacillus amyloliquefaciens at low moisture contents. In W. J. J. V. D. Tweel, A. Harder, & R. M. Buitelaar (Eds.), Stability and stabilization of enzymes (pp. 459-466). (Studies in Organic Chemistry; Vol. 47, No. C). Elsevier. https://doi.org/10.1016/B978-0-444-89372-7.50060-9

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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.",

author = "J. Saraiva and Cordt, {S. De} and M. Hendrickx and J. Oliveira and P. Tobback",

year = "1993",

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Saraiva, J, Cordt, SD, Hendrickx, M, Oliveira, J & Tobback, P 1993, Inactivation of _α-amylase from Bacillus amyloliquefaciens at low moisture contents. in WJJVD Tweel, A Harder & RM Buitelaar (eds), Stability and stabilization of enzymes. Studies in Organic Chemistry, no. C, vol. 47, Elsevier, pp. 459-466, Proceedings of an International Symposium, Maastricht, Netherlands, 22/11/92. https://doi.org/10.1016/B978-0-444-89372-7.50060-9

Inactivation of _α-amylase from Bacillus amyloliquefaciens at low moisture contents. / Saraiva, J.; Cordt, S. De; Hendrickx, M. et al.
Stability and stabilization of enzymes. ed. / W. J. J. Van Den Tweel; A. Harder; R. M. Buitelaar. Elsevier, 1993. p. 459-466 (Studies in Organic Chemistry; Vol. 47, No. C).

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

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