PURIFICATION AND CHARACTERIZATION OF AN ENDO-1,4-BETA-D-GALACTANASE FROM ASPERGILLUS-SOJAE

Citation
I. Kimura et al., PURIFICATION AND CHARACTERIZATION OF AN ENDO-1,4-BETA-D-GALACTANASE FROM ASPERGILLUS-SOJAE, Journal of fermentation and bioengineering, 85(1), 1998, pp. 48-52
Citations number
33
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Food Science & Tenology","Biothechnology & Applied Migrobiology
ISSN journal
0922-338X
Volume
85
Issue
1
Year of publication
1998
Pages
48 - 52
Database
ISI
SICI code
0922-338X(1998)85:1<48:PACOAE>2.0.ZU;2-D
Abstract
An endo-1,4-beta-D-galactanase (EC 3.2.1.89) was purified to homogenei ty from a solid-state culture of Aspergillus sojae. The molecular weig ht of the galactanase was estimated to be 39,700 by sodium dodecyl sul fate-polyaclylamide gel electrophoresis (SDS-PAGE). Gel filtration chr omatography indicated the native enzyme to be a monomer. The isoelectr ic point of the galactanase was 3.60. The optimum pH and temperature o f the enzyme activity were 4.5 and 50 degrees C, respectively. The gal actanase was stable from pH 6.0 to 10.0, and up to 35 degrees C. The K -m value for arabinogalactan from soybean was 0.82 mg/ml. The activity of the enzyme was significantly inhibited by Mn2+, Hg2+, Ag+, and Fe3 +, and no stimulation by metal ions was apparent. After the hydrolysis of arabinogalactan from soybean, the major products were galactobiose and galactose, and no liberation of arabinose was observed in the rea ction mixture.