Comparative characteristics of cyclodextrin glycosyltransferases from various groups of microorganisms

• Published in: Biokhimiia (Moscow, Russia) Vol. 57; no. 3; p. 430
• Main Authors: Abelian, V A, Avakian, Z G, Melkumian, A G, Balaian, A M, Uzunian, L V, Gasparian, A V
• Format: Journal Article
• Language: Russian
• Published: Russia (Federation) 01-03-1992
• Subjects: Amino Acids - analysis; Amylopectin - metabolism; Amylose - metabolism; Bacteria - enzymology; Glucosyltransferases - metabolism; Maltose - metabolism; Melibiose - metabolism; Starch - metabolism; Trisaccharides - metabolism
• ISSN: 0320-9725

Cyclodextrin glycosyltransferases (CGT-ase, 1.4-alpha-glucanotransferase, cyclizing, EC 2.4.1.19) produced by some thermophilic, alkalophilic and mesophilic bacterial strains, were isolated and characterized. It was shown that thermophilic and mesophilic CGT-ases represent a mixture of alpha-, beta- and gamma-cyclodextrins (CD), alpha-cyclodextrin being the predominant component. Alkalophilic enzymes produce only beta-CD and are able to produce CD not only from starch but also from maltose, melibiose, maltotriose, amylose and amylopectin. The optimal conditions for the catalytic activity of the enzymes were determined. It was found that calcium, magnesium and zinc ions have a beneficial effect on the specific activity of these enzymes. The amino acid composition of the enzymes was studied.