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Conformational stability of [alpha]-amylase from malted sorghum (Sorghum bicolor): Reversible unfolding by denaturants

Sai Kumar, R. S. and Singh, Sridevi Annapurna and Rao, A. G. Appu (2009) Conformational stability of [alpha]-amylase from malted sorghum (Sorghum bicolor): Reversible unfolding by denaturants. Biochimie, 91 (4). pp. 548-557. ISSN 0300-9084

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Abstract

[alpha]-Amylase from Sorghum bicolor, is reversibly unfolded by chemical denaturants at pH 7.0 in 50

Item Type: Article
Uncontrolled Keywords: Sorghum [alpha]-amylase Conformational stability Cysteine oxidation Protein unfolding Electrostatic interactions
Subjects: 500 Natural Sciences and Mathematics > 07 Life Sciences > 03 Biochemistry & Molecular Biology > 07 Enzyme Biochemistry
600 Technology > 08 Food technology > 21 Cereals > 06 Sorghum
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 14 Dec 2017 04:05
Last Modified: 17 Oct 2018 07:04
URI: http://ir.cftri.com/id/eprint/9068

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