Man-tailored cellulose-based carriers for invertase immobilization |
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Authors: | Jolanta Bryjak Jolanta Liesiene Vladimír ?tefuca |
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Institution: | (1) Faculty of Chemistry, Wrocław University of Technology, Wybrzeże Wyspiańskiego 27, 50-373 Wrocław, Poland;(2) Faculty of Chemical Technology, Kaunas University of Technology, Radvilenu pl. 19, 50254 Kaunas, Lithuania;(3) Faculty of Chemical and Food Technology, Slovak University of Technology, Radlinskēho 9, 812 37 Bratislava, Slovak Republic |
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Abstract: | Cellulose-based carriers Granocel were specially prepared and optimised for covalent immobilization of enzymes. The effects
of carrier characteristics such as pore size, chemistry of anchor groups and their density on invertase immobilization efficiency
were evaluated. It was found that the preferential adsorption/binding of the enzyme to a carrier during coupling and its activity
after immobilization depended on microenvironmental effects created by hydrophilic surface of the carrier, functional groups
and their activators. The best preparations (activity approx. 300 U/mL, high storage stability) were obtained for NH2-Granocel activated with glutaraldehyde. It is probably due to Granocel modification with pentaethylenehexamine that gave
a 19-atom spacer arm. The enzyme concentration in coupling mixture was optimised as well. The kinetic parameters of sucrose
hydrolysis for native and immobilized invertase were evaluated. Compared to the native invertase, K
m
value of immobilized enzyme was only twice higher with about three times lower substrate inhibition. Reaction runs in a well
mixed batch reactors with native and immobilized invertase showed slightly slower reaction rate in the case of the enzyme
covalently bound to Granocel. Very good stability of cellulose-based carrier was proved experimentally by 20 successive reaction
runs in a batch reactor. |
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Keywords: | Batch reactor Cellulose-based carriers Covalent attachment Immobilization Invertase Kinetics Stability |
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