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Microbiology and Molecular Biology Reviews, June 2005, p. 306-325, Vol. 69, No. 2
1092-2172/05/$08.00+0     doi:10.1128/MMBR.69.2.306-325.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Microbial Dextran-Hydrolyzing Enzymes: Fundamentals and Applications

Elvira Khalikova,1,2 Petri Susi,1,{dagger} and Timo Korpela1*

Joint Biotechnology Laboratory, Department of Chemistry, University of Turku, 20520 Turku, Finland,1 Institute of Biology, Department of Biotechnology, 450054 Ufa, Russia2

Dextran is a chemically and physically complex polymer, breakdown of which is carried out by a variety of endo- and exodextranases. Enzymes in many groups can be classified as dextranases according to function: such enzymes include dextranhydrolases, glucodextranases, exoisomaltohydrolases, exoisomaltotriohydrases, and branched-dextran exo-1,2-{alpha}-glucosidases. Cycloisomalto-oligosaccharide glucanotransferase does not formally belong to the dextranases even though its side reaction produces hydrolyzed dextrans. A new classification system for glycosylhydrolases and glycosyltransferases, which is based on amino acid sequence similarities, divides the dextranases into five families. However, this classification is still incomplete since sequence information is missing for many of the enzymes that have been biochemically characterized as dextranases. Dextran-degrading enzymes have been isolated from a wide range of microorganisms. The major characteristics of these enzymes, the methods for analyzing their activities and biological roles, analysis of primary sequence data, and three-dimensional structures of dextranases have been dealt with in this review. Dextranases are promising for future use in various scientific and biotechnological applications.


* Corresponding author. Mailing address: Tykistökatu 6 A 6, 20520 Turku, Finland. Phone: 358-2-3338066. Fax: 358-2-3338080. E-mail: timokor{at}utu.fi.

{dagger} Present address: Department of Virology, Kiinamyllynkatu 13, 20520 Turku, Finland.


Microbiology and Molecular Biology Reviews, June 2005, p. 306-325, Vol. 69, No. 2
1092-2172/05/$08.00+0     doi:10.1128/MMBR.69.2.306-325.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.







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