PURIFICATION AND PROPERTIES OF CARNITINE DEHYDROGENASE FROM PSEUDOMONAS SP YS-240

Authors
MORI N MITSUZUMI H KITAMOTO Y
Citation
N. Mori et al., PURIFICATION AND PROPERTIES OF CARNITINE DEHYDROGENASE FROM PSEUDOMONAS SP YS-240, Journal of fermentation and bioengineering, 78(5), 1994, pp. 337-340
Citations number
10
Categorie Soggetti
Food Science & Tenology","Biothechnology & Applied Migrobiology
Journal title
Journal of fermentation and bioengineering → ACNP
ISSN journal
0922338X
Volume
78
Issue
5
Year of publication
1994
Pages
337 - 340
Database
ISI
SICI code
0922-338X(1994)78:5<337:PAPOCD>2.0.ZU;2-Q
Abstract
Carnitine dehydrogenase from Pseudomonas sp. YS-240 was purified to ap parent homogeneity. Purification was achieved by ion-exchange chromato graphy, followed by ammonium sulfate fractionation, hydroxylapatite ch romatography and gel filtration. This enzyme had the molecular weight of 110 kDa and consisted of two identical subunits. The isoelectric po int was found to be 5.5. The optimum pH for enzymatic activity in the oxidation reaction was found to be 9.5. The enzyme was highly specific for L-carnitine and NAD(+). The Michaelis constants for L-carnitine a nd NAD(+) were 1.2 mM and 0.1mM, respectively.