α-Galactosidases and their applications in biotransformations

Weignerova, Lenka, Simerska, Pavla and Kren, Vladimir (2009) α-Galactosidases and their applications in biotransformations. Biocatalysis and Biotransformation, 27 2: 79-89. doi:10.1080/10242420802583416


Author Weignerova, Lenka
Simerska, Pavla
Kren, Vladimir
Title α-Galactosidases and their applications in biotransformations
Journal name Biocatalysis and Biotransformation   Check publisher's open access policy
ISSN 1029-2446
1024-2422
Publication date 2009-03
Sub-type Article (original research)
DOI 10.1080/10242420802583416
Volume 27
Issue 2
Start page 79
End page 89
Total pages 11
Place of publication London, United Kingdom
Publisher Informa Healthcare
Language eng
Abstract α-d-Galactosidases (α-d-galactoside galactohydrolase, E.C. 3.2.1.22) are exoglycosidases, which in vivo catalyze the hydrolysis of simple and complex oligo- and polysaccharides containing terminal α-d-galactosyl groups. A number of industrial applications of α-d-galactosidases are known, mainly in the sugar industry, pulp and paper industry or medicine. Although α-d-galactosidases occur in all living systems, microbial and possibly plant enzymes are preferred for practical applications. The regioselectivity of glycosidases is somewhat poor. Selective protection of oligosaccharides and development of new modified donors/acceptors is a promising method to overcome this problem. Genetic engineering has enabled the creation of glycosynthases from the hydrolytic glycosidases, which are highly complementary to glycosyltransferases. The present review summarizes recent advances in the application of α-d-galactosidases in synthetic and biotransformation applications.
Keyword α-Galactosidase
Enzyme
Transglycosylation
Purification
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
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Created: Tue, 27 Sep 2011, 16:20:48 EST by Dr Pavla Simerska on behalf of School of Chemistry & Molecular Biosciences