NDLI: An Irreversible and Kinetically Controlled Process: Thermal Induced Denaturation of L-2-Hydroxyisocaproate Dehydrogenase from Lactobacillus confusus

Content Provider	Springer Nature Link
Author	Bao, Lide Chatterjee, Shivani Lohmer, Sabine Schomburg, Dietmar
Copyright Year	2007
Abstract	The thermal denaturation of Lactobacillus confusus l-2-Hydroxyisocaproate Dehydrogenase (l-HicDH) has been studied by Differential Scanning Calorimetry (DSC). The stability of this enzyme has been investigated at different pH conditions. The results of this study indicate that the thermal denaturation of this enzyme is irreversible and the T $_{ m }$ is dependent on the scan-rate, which suggests that the denaturation process of l-HicDH is kinetically determined. The heat capacity function of l-HicDH shows a single peak with the T $_{ m }$ values between 52.14°C and 55.89°C at pH 7.0 at different scan rates. These results indicate that the whole l-HicDH could unfold as a single cooperative unit, and intersubunit interactions of this homotetrameric enzyme must play a significant role in the stabilization of the whole enzyme. The rate constant of the unfolding is analyzed as a first order kinetic constant with the Arrhenius equation, and the activation energy has been calculated. The variation of the activation energy values obtained with different methods does not support the validity of the one-step irreversible model. The denaturation pathway was described by a three-state model, N → U → F, in which the dissociation of the tetramer takes place as an irreversible step before the irreversible unfolding of the monomers. The calorimetric enthalpy associated with the irreversible dissociation and the calorimetric enthalpy associated with the unfolding of the monomer were obtained from the best fitting procedure. Thermal unfolding of l-HicDH was also studied using Circular Dichroism (CD) spectroscopy. Both methods yielded comparable values.
Starting Page	143
Ending Page	151
Page Count	9
File Format	PDF
ISSN	15723887
Journal	The Protein Journal
Volume Number	26
Issue Number	3
e-ISSN	15734943
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	2007-01-05
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	l-HicDH Differential Scanning Calorimetry (DSC) thermal denaturation transition temperature enthalpy activation energy Animal Anatomy / Morphology / Histology Organic Chemistry Biochemistry Bioorganic Chemistry
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Analytical Chemistry Biochemistry Bioengineering

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