Methods and supports for immobilization and stabilization of cyclomaltodextrin glucanotransferase from Thermoanaerobacter.
Thermoanaerobacter cyclomaltodextrin glucanotransferase (CGTase) was immobilized using different supports and immobilization methods to study the effect on activity recovery. The enzyme covalently attached into glyoxyl-silica showed low activity recovery of 1.5%. The hydrophobic adsorption of the enzyme on Octadecyl-Sepabeads yielded also low activity recovery, 3.83%, and the enzyme could easily leak from the support at low ionic strength, although the immobilization yield was satisfactory, approximately 76%. The CGTase encapsulated in a sol-gel matrix gave an activity recovery of 6.94% and maximum cyclization activity at 60 degrees C, at pH 6.0. The half-time life at 60 degrees C, pH 6.0, in the presence of substrate was 100 min, which was lower than that of the free enzyme. The best activity recovery in this work (6.94%) is approximately five times smaller than that obtained previously using glyoxyl-agarose as support and covalent immobilization. Thus, the best support and method we tested so far for immobilization of CGTase is covalent attachment on glyoxyl-agarose.
Amud
Ana Elisa
AE
Chemical Engineering Department, State University of Maringa, Maringa, PR, Brazil.
da Silva
Gercio Rodrigo Presa
GR
Tardioli
Paulo Waldir
PW
Soares
Cleide Mara Faria
CM
Moraes
Flavio Faria
FF
Zanin
Gisella Maria
GM
D000327:Adsorption; D004789:Enzyme Activation; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry; D005964:Glucosyltransferases / Q000737:chemistry*; D013379:Substrate Specificity; D046968:Thermoanaerobacter / Q000201:enzymology*
D004800:Enzymes, Immobilized; D005964:Glucosyltransferases; C019963:cyclomaltodextrin glucanotransferase