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KMID : 1234420110390030245
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Korean Journal of Microbiololgy and Biotechnology
2011 Volume.39 No. 3 p.245 ~ p.251
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Substrate Specificities of α-Galactosidase from Mortierella sp
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Park Gwi-Gun
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Abstract
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α-Galactosidase was purified from a culture filtrate of Mortierella sp. by CM-sephadex C-50, and subsequent Sephadex G-100 column chromatography. The final preparation thus obtained showed a single band on SDS-polyacrylamide gel electrophoresis. The molecular weight was determined to be 56 kDa. Gal3Man4 (63-mono-O-α-D-galactopyranosyl-4-O-β-Dmannotetraose), Gal2,3Man5 (62,3-di-O-α-D-galactopyranosyl-4-O-β-D-mannopentaose), Gal2Man3 (62-mono- O-α-D-galactopyranosyl-4-O-β-D-mannotriose), Gal2Man6 (62-mono-O-α-D-galactopyranosyl-4-O-β-D-mannohexaose) and Gal2Man5 (62-mono-O-α-D-galactopyranosyl-4-O-β-D-mannopentaose), prepared from 3 types of microbial β-mannnanase, were used as substrates. Gal3Man4 and Gal2Man3 had a stubbed α-galactosyl residue on the 2nd and 3rd mannose from the reducing end of mannotetraose and mannotriose, thus α-galactosidase showed a preference for stubbed α-galactosyl residue. α-Galactosidase hydrolyzed Gal3Man4 more rapidly than Gal2Man3. However, α-galactosidase hardly acted on Gal2,3Man5, Gal2Man6 or Gal2Man5. The enzyme hydrolyzed melibiose to galactose and glucose, raffinose to galactose and sucrose, and also stachyose to galactose and raffinose.
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KEYWORD
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α-galactosidase, galactosyl manno-oligomer, Mortierella sp., substrate specificity
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