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Cyclodextrin glucanotransferases (CGTases; EC 2.4.1.19) from newly isolated mesophilic, thermophilic, alkalophilic, and halophilic bacilli, as well as from thermoactinomycetes, were purified to homogeneity, and some of their physicochemical and biochemical characteristics (cyclizing, disproportionating, and hydrolytic activities) were studied. Cyclodextrin (CD) production in the presence and absence of compounds favoring formation of complexes had certain specific features. We were able to demonstrate that CGTases of mesophilic and thermophilic strains form mixtures of -, -, and -CDs, whereas the enzymes from halophilic and alkalophilic microorganisms preferentially catalyze the formation of -CD.  相似文献   
2.
—For the first time, microorganisms producing cyclomaltodextrin glucantransferaseglucan transferases (CGT, EC 2.4.1.19) were isolated from soil samples of various ecogeographical regions. These microorganisms were identified asBacillus macerans. The enzymes were purified by affinity chromatography on an α-cyclodextrin polymer and gel filtration on Biogel P-150 and proved to be electrophoretically homogeneous. Some of their physicochemical and biochemical properties are reported.  相似文献   
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