The production of beta-maltooligosaccharides of glycitein and daidzein using Lactobacillus delbrueckii and cyclodextrin glucanotransferase (CGTase) as biocatalysts was investigated. The cells of L. delbrueckii glucosylated glycitein and daidzein to give their corresponding 4'- and 7-O-beta-glucosides. The beta-glucosides of glycitein and daidzein were converted into the corresponding beta-malto...

In this work 2-O-α-D-glucopyranosyl-L-ascorbic acid (AA-2G) was synthesized by Cyclodextrin glucanotransferase (CGTase) from Bacillus sp. SK 13.002 with L-ascorbic acid (AA) as an acceptor and maltose as a glycosyl donor. AA-2G production was analyzed by HPLC and was confirmed by LC/MS results. The reaction parameters, such as pH (4.0-9.0), temperature (25-50°C), time (0-30 h), substrate ratios...

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...

Cyclodextrin glucanotransferase (CGTase, EC. 2.1.1.19) produced using new alkaliphile Microbacterium terrae KNR 9 has been purified to homogeneity in a single step by the starch adsorption method. The specific activity of the purified CGTase was 45 U/mg compared to crude 0.9 U/mg. This resulted in a 50-fold purification of the enzyme with 33 % yield. The molecular weight of the purified enzyme ...

Cyclodextrin glycosyltransferase (CGTase) is a member of the a-amylase family, a large group of enzymes that act on a-glycosidic bonds in starch and related compounds. Over twenty different reaction and product specificities have been found in this family. Although three-dimensional structure elucidation and the biochemical characterization of site-directed mutants have yielded a detailed insig...

The cyclodextrin glucosyltransferase enzyme (CGTase) is an industrially crucial for the production of β-cyclodextrin (β-CD). CGTase has a high propensity to produce mixture cyclodextrins (CDs). From industrial perspective, that produces only one type CD critical importance. Bacillus sp. PBS1 produced converts starch solely into β-CD. isolated strain was found close similarity with alkaliphilic ...

Crystals of cyclodextrin glycosyltransferase (CGTase) from Bacillus circuluns strain 25 1 were soaked in buffer solutions containing the pseudotetrasaccharide acarbose, a strong amylaseand CGTase inhibitor. The X-ray structure of the complex was elucidated at 2.5-A resolution with a final crystallographic R value of 15.8% for all data between 8.0 and 2.5 A. Acarbose is bound near the catalytic ...

Cyclodextrin glycosyltransferase (CGTase) enzymes from various bacteria catalyze the formation of cyclodextrins from starch. The Bacillus stearothermophilus maltogenic alpha-amylase (G2-amylase is structurally very similar to CGTases, but converts starch into maltose. Comparison of the three-dimensional structures revealed two large differences in the substrate binding clefts. (i) The loop form...

The gene encoding the cyclodextrin glycosyltransferase (CGTase) of Paenibacillus pabuli US132, previously described as efficient antistaling agent and good candidate for cyclodextrins production, was cloned, sequenced, and expressed in Escherichia coli. Sequence analysis showed that the mature enzyme (684 amino acids) was preceded by a signal peptide of 34 residues. The enzyme exhibited the hig...