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Glycobiology Advance Access originally published online on May 5, 2004
Glycobiology 2004 14(7):593-598; doi:10.1093/glycob/cwh091
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Glycobiology vol. 14 no. 7 © Oxford University Press 2004; all rights reserved.

Hydrolysis of Man9GlcNAc2 and Man8GlcNAc2 oligosaccharides by a purified {alpha}-mannosidase from Candida albicans

Héctor M. Mora-Montes2, Everardo López-Romero2, Samuel Zinker3, Patricia Ponce-Noyola2 and Arturo Flores-Carreón1,2

2 Instituto de Investigación en Biología Experimental, Facultad de Química, Universidad de Guanajuato, Guanajuato, Guanajuato 36000, Mexico, and the 3 Departamento de Genética y Biología Molecular, CINVESTAV del IPN, Apartado Postal 14-740, México, D.F. 07000, Mexico

Received on October 14, 2003; revised on January 8, 2004; accepted on January 9, 2004

A soluble {alpha}-mannosidase from Candida albicans was purified to homogeneity by sequential size exclusion, ion exchange, and affinity chromatographies in columns of Sepharose CL6B, DEAE Bio-Gel A, and Concanavalin A Sepharose 4B, respectively. Analytical electrophoresis of the purified preparation in 10% SDS–polyacrylamide gels stained with Coomassie blue revealed a single polypeptide of 43 kDa that was responsible for enzyme activity. The purified enzyme primarily trimmed Man9GlcNAc2 to produce Man8GlcNAc2 isomer B and mannose as a function of time of incubation up to 12 h at 37°C. Prolonged incubation with the enzyme resulted in the accumulation after 24 h of other oligosaccharides corresponding to Man7GlcNAc2 and probably Man6GlcNAc2. These two products were also observed when Man8GlcNAc2 isomer B instead of Man9GlcNAc2 was used as substrate. Other oligosaccharides, such as Man6GlcNAc2-Asn, Man5GlcNAc2-Asn, and the {alpha}1,3- and {alpha}1,6-linked mannobiosides, were not hydrolyzed at all. These properties are consistent with an {alpha}1,2-mannosidase that may represent a new member of the glycosylhydrolase family 47.

1 To whom correspondence should be addressed; e-mail: floresca{at}quijote.ugto.mx


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