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KMID : 0545120040140040863
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Journal of Microbiology and Biotechnology
2004 Volume.14 No. 4 p.863 ~ p.867
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Purification and Characterization of Guar Galactomannan Degrading α-Galactosidase from Aspergillus oryzae DR-5
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Ramalingam G
Mulimani VH
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Abstract
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α-Galactosidase from A. oryzae DR-5 was induced in the presence of melibiose raffinose galactose and locust bean galactomannan. The enzyme was purified to homogeneity by precipitation with acetone followed by ion-exchange chromatography using DEAE-Sephacel. The purified enzyme showed a single band in both nondenaturing- PAGE and SDS-PAGE. The enzyme was a glycoprotein in nature by activity staining. The molecular weight of the purified enzyme was 93- 95 kDa by SDS-PAGE. The enzyme exhibited the optimum pH and temperature at 4.7 and 60oC respectively. α-Galactosidase activity was strongly inhibited by Ag2+ Hg2+ Cu2+ and galactose. EDTA 110- phenanthraline and PMSF did not inhibit the enzyme activity whereas N-bromosuccinimide completely inhibited enzyme activity. Investigation by TLC showed complete hydrolysis of stachyose and raffinose in soymilk in 3 h at pH 5.0 and 50oC.
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