Studies on cyclodextrin glycosyltransferase. II. Action of cyclodextrin glycosyltransferase from Bacillus megaterium strain No. 5 on starch.

Integral Use of Amaranth Starch to Obtain Cyclodextrin Glycosyltransferase, by Bacillus megaterium, to Produce β-Cyclodextrin

Cyclodextrin glycosyltransferase (CGTase) is an enzyme that produces cyclodextrins (CDs) from starch and related carbohydrates, producing a mixture of α-, β-, and γ-CDs in different amounts. CGTase production, mainly by Bacillus sp., depends on fermentation conditions such as pH, temperature, concentration of nutrients, carbon and nitrogen sources, among others. Bacillus megaterium CGTase produ...

The raw starch binding domain of cyclodextrin glycosyltransferase from Bacillus circulans strain 251.

The E-domain of cyclodextrin glycosyltransferase (CGTase) (EC 2.4.1.19) from Bacillus circulans strain 251 is a putative raw starch binding domain. Analysis of the maltose-dependent CGTase crystal structure revealed that each enzyme molecule contained three maltose molecules, situated at contact points between protein molecules. Two of these maltoses were bound to specific sites in the E-domain...

Investigation on Cyclodextrin Production with Cyclodextrin Glucanotransferase from Bacillus megaterium

The process of producing cyclodextrins from starch with cyclodextrin glucanotransferase from Bacillus megaterium has been studied. The effect of starch and enzyme concentrations was evaluated using optimal composite designs and the response surface methodology. Mathematical models describing the process in two overlapping areas of variation of the independent variables were developed. The model...

University of Groningen Protein engineering of cyclodextrin glycosyltransferase from Bacillus circulans strain

Site-directed mutations in tyrosine 195 of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 affect activity and product specificity.

Tyrosine 195 is located in the center of the active site cleft of cyclodextrin glycosyltransferase (EC 2.4.1.19) from Bacillus circulans strain 251. Alignment of amino acid sequences of CGTases and alpha-amylases, and the analysis of the binding mode of the substrate analogue acarbose in the active site cleft [Strokopytov, B., et al. (1995) Biochemistry 34, (in press)], suggested that Tyr195 pl...