Immobilization of commercial cyclomaltodextrin glucanotransferase into controlled pore silica by the anchorage method and covalent bonding

[Display omitted] •CGTase was immobilized on silica by surface anchoring and covalent bonding methods.•Surface anchoring (SCGT-A) immobilized 89.63% of CGTase in terms of activity.•Covalent bonding (SCGT-CB) provided an immobilization yield of 48.44% of CGTase.•CD production increased 60.97% and 34.90% for SCGT-A and SCGT-CB with ethanol.•The use of SCGT-A was more efficient than SCGT-CB and free enzyme in 24 h reaction. Cyclomaltodextrin glucanotransferase (CGTase) is used mainly for the industrial production of cyclodextrins (CDs). Their potential use and availability have played a decisive role in increasing demand for CDs. The aim of the present study was to immobilize the commercial CGTase (Toruzyme® 3.0L) into controlled pore silica by surface anchoring (SCGT-A) and covalent bonding (SCGT-CB) and to apply the immobilized enzymes in the production of CDs. The SCGT-A method proved to be efficient due to its short immobilization time and, it was possible to immobilize 89.63% of CGTase, in terms of activity. Commercial CGTase immobilized by SCGT-CB provided an immobilization yield of 48.44%, also in terms of activity. There was an increase in total CD production of 60.97% and 34.90% for SCGT-A and SCGT-CB, respectively, in a reaction medium with 10% ethanol, compared to the same media without ethanol. Higher CD production occured at 24 and 48 h for SCGT-A and SCGT-CB methods, respectively. The use of SCGT-A was more efficient than SCGT-CB and free enzyme (CGT-F) after 24 h of reaction. The increase production of CDs obtained by the SCGT-A method and the demonstrated continuous production of CDs with the SCGT-CB method make the use of immobilized CGTase viable for industrial applications.