Cyclomaltodextrin glucanotransferase (CGTase)

Cyclomaltodextrin glucanotransferase (CGTase) is a bacterial enzyme belonging to the glycoside hydrolase family 13, primarily produced by species of the genus Bacillus [1, 8]. It is uniquely characterized by its ability to catalyze the cyclization of starch and related 1,4-alpha-D-glucans into cyclic oligosaccharides known as cyclodextrins (alpha, beta, and gamma-CDs) [1, 5]. In addition to cyclization, the enzyme performs coupling, disproportionation, and weak hydrolytic reactions [1, 7]. While CGTase is not a direct therapeutic target for treating human diseases, it plays a critical role in the pharmaceutical industry [11, 14]. It is used to synthesize cyclodextrins, which serve as essential drug delivery vehicles that enhance the solubility, stability, and bioavailability of hydrophobic medicinal compounds [7, 19]. The enzyme is also a subject of protein engineering to optimize the production of specific cyclodextrin sizes for various industrial applications [10, 14].

Other names

Cyclodextrin glucanotransferaseCyclodextrin glycosyltransferaseBacillus macerans amylaseBMA1,4-alpha-D-glucan 4-alpha-D-(1,4-alpha-D-glucano)-transferase (cyclizing)KonchizaimuCyclomaltodextrin glucotransferaseCyclomaltodextrin glycosyltransferase

Acarbose acts as a competitive or mixed non-competitive inhibitor of CGTase by mimicking the transition state of the enzymatic reaction, although this interaction is primarily studied in a biochemical or industrial context rather than for human therapy [15, 16].