Microbial Cyclodextrin Glycosyltransferases: Sources, Production, and Application in Cyclodextrin Synthesis

Cyclodextrin glycosyltransferase (CGTase) is a multifunctional enzyme that hydrolyzes the <em>α</em>-glycosidic bond between two sugar molecules and synthesizes cyclodextrins (CDs) other transglycosylation products. It ubiquitously present extracellular offers CGTase-producing organism sole right onto starch substrates over microbes. The review provides brief account of diversity among microbes, CGTase production in different heterologous hosts (wherein secretion highly desired), physicochemical properties CGTases. Overall, 52 crystal structures highlight five domain tertiary structure CGTases have been discovered so far. On basis these structures, catalytic mechanism reactions has discussed, three residues, namely Glu257, Asp229, Asp328, identified at active site all Moreover, constituted by least nine sugar-binding sites, denoted as -7 to +2. Furthermore, sequence alignment selected highlighted conserved regions sequential differences <em>α</em>-CGTases, <em>β</em>-CGTases, <em>γ</em>-CGTases. Various biotechnological applications immobilization on variety support matrices are briefly discussed. This also encompasses detailed CDs, their enzymatic production, extraction, industrial sectors.