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Rapid kinetic study of Cyclomaltodextrinase from alkalophilic Bacillus sp. I-5 by stopped-flow spectrophotometer
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- Authors
- Advisor
- 박관화
- Issue Date
- 2004
- Publisher
- 서울대학교 대학원
- Keywords
- Cyclomaltodextrinase i-5 (cdase i-5) ; Oligomeric state ; Stopped-flow measurement ; Rapid reaction kinetics
- Description
- Thesis (master`s)--서울대학교 대학원 :농생명공학부,2004.
- Abstract
- The dissociation kinetics of the oligomeric states of Cyclomaltodextrinase I-5 (CDase I-5) and
the quaternary structures of this enzyme have been investigated. CDase exists in oligomer, as an
assembly of six unit of dimer and the equilibrium between the dimer and dodecamer is altered
rapidly in the presence of salt like KCl. Changes in oligomeric state can be monitored by KCl
change in intrinsic fluorescence of tryptophan residues in CDase I-5. The Circular dichroism
demonstrated that this change measurement were distinguished from the denaturation at 1M KCl.
The dissociation of this enzyme was also analysed by analytical ultracentrifugation and gel
permeation chromatography. The rate constant (kd) of dissociation from dodecamer into dimer was
determined at various KCl concentration by stopped-flow spectrophotometer.
The dissociation constants in the presence of at 0.2 M KCl and at 1.0 M KCl were 5.96 s-1 and
7.99 s-1, respectively. The results indicated that the dodecameric CDase dissociated into dimer
more favorably with increasing concentration of salts.
- Language
- English
- URI
- http://dcollection.snu.ac.kr:80/jsp/common/DcLoOrgPer.jsp?sItemId=000000055049
https://hdl.handle.net/10371/67599
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