J Bacteriol. 1978 March; 133(3): 1073-1077
Alpha-l-arabinofuranosidase from Rhodotorula flava.
E Uesaka,
M Sato,
M Raiju and
A Kaji
ABSTRACT
An alpha-L-arabinofuranosidase (EC 3.2.1.55) from the culture fluid of Rhodotorula flava IFO 0407 grown on beet arabinan as a carbon source has been highly purified. The purified enzyme has a pH optimum of 2.0. The enzyme is unusually acid stable, retaining 82% of its activity after being maintained for 24 h at pH 1.5 and at 30 degrees C. The apparent Km and Vmax values of the enzyme for phenyl alpha-L-arabinofuranoside were determined to be 9.1 mM and 72.5 mumol per min per mg of protein, respectively.
J Bacteriol. 1978 March; 133(3): 1073-1077
This article has been cited by other articles:
-
Kotake, T., Dina, S., Konishi, T., Kaneko, S., Igarashi, K., Samejima, M., Watanabe, Y., Kimura, K., Tsumuraya, Y.
(2005). Molecular Cloning of a {beta}-Galactosidase from Radish That Specifically Hydrolyzes {beta}-(1->3)- and {beta}-(1->6)-Galactosyl Residues of Arabinogalactan Protein. Plant Physiol.
138: 1563-1576
[Abstract]
[Full Text]
-
Saha, B. C., Bothast, R. J.
(1998). Purification and Characterization of a Novel Thermostable alpha -L-Arabinofuranosidase from a Color-Variant Strain of Aureobasidium pullulans. Appl. Environ. Microbiol.
64: 216-220
[Abstract]
[Full Text]
Copyright © 1978 by the American Society for Microbiology. All rights reserved.