Journal of the Serbian Chemical Society 2014 Volume 79, Issue 5, Pages: 533-543
https://doi.org/10.2298/JSC131004154I
Full text ( 1745 KB)
Cited by
Immobilization of β-glucosidase onto mesoporous silica support: Physical adsorption and covalent binding of enzyme
Ivetić Darjana Ž. (Faculty of Technology, Novi Sad)
Srdić Vladimir V. (Faculty of Technology, Novi Sad)
Antov Mirjana G. (Faculty of Technology, Novi Sad)
This paper investigates β-glucosidase immobilization onto mesoporous silica
support by physical adsorption and covalent binding. The immobilization was
carried out onto micro-size silica aggregates with the average pore size of
29 nm. During physical adsorption the highest yield of immobilized
β-glucosidase was obtained at initial protein concentration of 0.9 mg ml-1.
Addition of NaCl increased 1.7-fold, while Triton X-100 addition decreased
6-fold yield of adsorption in comparison to the one obtained without any
addition. Covalently bonded β-glucosidase, via glutaraldehyde previously
bonded to silanized silica, had higher yield of immobilized enzyme as well as
higher activity and substrate affinity in comparison to the one physically
adsorbed. Covalent binding did not considerably changed pH and temperature
stability of obtained biocatalyst in range of values that are commonly used
in reactions in comparison to unbounded enzyme. Furthermore, covalent binding
provided biocatalyst which retained over 70% of its activity after 10 cycles
of reuse.
Keywords: β-glucosidase, immobilization, physical adsorption, chemical binding, mesoporous silica
Projekat Ministarstva nauke Republike Srbije, br. III 45021