Purification and characterization of L-2,3-butanediol dehydrogenase of Brevibacterium saccharolyticum C-1012 expressed in Escherichia coli

Authors
Takusagawa, Y Otagiri, M Ui, S Ohtsuki, T Mimura, A Ohkuma, M Kudo, T
Citation
Y. Takusagawa et al., Purification and characterization of L-2,3-butanediol dehydrogenase of Brevibacterium saccharolyticum C-1012 expressed in Escherichia coli, BIOS BIOT B, 65(8), 2001, pp. 1876-1878
Citations number
9
Categorie Soggetti
Agricultural Chemistry","Biochemistry & Biophysics
Journal title
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
ISSN journal
09168451 → ACNP
Volume
65
Issue
8
Year of publication
2001
Pages
1876 - 1878
Database
ISI
SICI code
0916-8451(200108)65:8<1876:PACOLD>2.0.ZU;2-G
Abstract
The L-2,3-butanediol dehydrogenase produced in E coti JM109/pLBD2-CTC was p urified by 5 steps. The molecular mass of this enzyme was estimated at 110 kDa and the subunit was measured to be 30 kDa. The L-BDH had some differenc es from the BDHs from other sources in substrate specificity, pI value, pH stability, effects of divalent cations, and organic acids.