Thermodynamic analysis of Bacillus cereus oligo-1,6-glucosidase and its cumulatively proline-introduced mutant proteins by differential scanning calorimetry

Authors
Watanabe, K Fujita, Y Usami, M Takimoto, A Suzuki, Y
Citation
K. Watanabe et al., Thermodynamic analysis of Bacillus cereus oligo-1,6-glucosidase and its cumulatively proline-introduced mutant proteins by differential scanning calorimetry, J MOL CAT B, 10(1-3), 2000, pp. 257-262
Citations number
22
Categorie Soggetti
Physical Chemistry/Chemical Physics
Journal title
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
ISSN journal
13811177 → ACNP
Volume
10
Issue
1-3
Year of publication
2000
Pages
257 - 262
Database
ISI
SICI code
1381-1177(20000904)10:1-3<257:TAOBCO>2.0.ZU;2-2
Abstract
Differential scanning calorimetry (DSC) was used to characterize thermodyna mically the stability of Bacillus cereus ATCC7064 oligo-1,6-glucosidase (de xtrin 6-alpha-D-glucanohydrolase, EC 3.2.1.10) and its proline-introduced m utants. DSC analysis revealed that the free energy change of unfolding for the mutants cumulatively increased as the number of introduced proline resi dues increased. The resulting increase in the free energy change was ascrib ed to the concomitant decrease in the entropy change of polypeptide backbon e unfolding in the mutants. (C) 2000 Elsevier Science B.V. All rights reser ved.