|
KMID : 0903520060490030180
|
|
Journal of the Korean Society of Agricultural Chemistry and Biotechnology
2006 Volume.49 No. 3 p.180 ~ p.185
|
|
|
Purification and Substrate Specificity of Debaryomyces sp. α-Galactosidase by Mannobiose-Sepharose Affinity Column Chromatograpy
|
|
Park Gwi-Gun
|
|
|
Abstract
|
|
|
|
α-Galactosidase was partially purified from the culture filtrate of Debaryomyces sp. by Mannobiose- Sepharose affinity column chromatography. The galactosidase exhibited maximum activity at pH 4.0 and 60oC, and was stable in the pH and temperature ranges of 3 to 4.5 and 30 to 50oC, respectively. The enzyme was inhibited by Hg2+ and Ag2+. The enzyme activity was not affected considerably by treatment with other metal compounds. The enzyme hydrolyzed melibiose to galactose and glucose, raffinose to galactose and sucrose, and Gal3Man3 (63-α-galactosyl-1,4-mannotriose) to galactose and mannotriose. On the contrary, it could not hydrolyze Gal3Man4 (63-α-galactosyl- 1,4-mannotetraose).
|
|
|
KEYWORD
|
|
|
α-galactosidase, Debaryomyces sp., mannobiose-sepharose affinity resin
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
|
|