Immobilization of laccase in kappa-carrageenan based semi-interpenetrating polymer networks

2010-08-02
Makas, Y. Gizem
KALKAN, NİGAR
AKSOY, SERPİL
ALTINOK, HAYDAR
Hasırcı, Nesrin
Laccase enzyme (L) was immobilized by entrapment into semi-interpenetrating polymer networks (semi-IPNs) prepared from kappa-carrageenan with either poly(acrylamide-acrylic acid) [P(AAm-AA)/kappa-car] or poly(acrylamide-itaconic acid) [P(AAm-IA)/kappa-car]. For both systems, immobilized enzymes achieved the same optimum values observed for free enzyme (pH = 5.0 and T = 40 degrees C), except for P(AAm-IA)/kappa-car system there was a shift to 5.5 in optimum pH value. At the end of 42 days of storage immobilized enzymes retained more than 80% of their original activities while the retained activities of both systems after 10 uses in batch type application were found to be higher than 50%. K-m values were calculated as 2.52 x 10(-2) mM and 1.08 x 10(-2) mM and V-max values were found as 6.8 x 10(-3) mM min(-1) and 4.4 x 10(-3) mM min(-1), for P(AAm-AA)/kappa-car-L and P(AAm-IA)/kappa-car-L, respectively. When methyl orange containing solutions (10 mg/L) were treated with the immobilized laccases (68.2 U), enzymatic decolorization of methyl orange in 6 h was achieved to the level of 35% for both systems. Supplementing the reaction medium with ABTS as the redox mediator increased this value to about 70%. These initial results show that, laccase containing semi-IPNs can find some applications in decolorization of the industrial wastes.
JOURNAL OF BIOTECHNOLOGY

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Citation Formats
Y. G. Makas, N. KALKAN, S. AKSOY, H. ALTINOK, and N. Hasırcı, “Immobilization of laccase in kappa-carrageenan based semi-interpenetrating polymer networks,” JOURNAL OF BIOTECHNOLOGY, pp. 216–220, 2010, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/31561.