IMMOBILIZATION OF GLUCOSE OXIDASE ENZYME FROM Penicillium sp-3 LOCAL STRAIN

Ahyar Ahmad (Biochemistry and Biotechnology Laboratory, Department of Chemistry, Faculty of Natural Sciences, Hasanuddin University, Makassar, 90245)
Andi Syaiful (Biochemistry and Biotechnology Laboratory, Department of Chemistry, Faculty of Natural Sciences, Hasanuddin University, Makassar, 90245)
Firman AP Firman AP (Bioprocess Laboratory, Ujung Pandang State Polytechnic, Makassar, 90245.)
Abdul Rauf Patong (Biochemistry and Biotechnology Laboratory, Department of Chemistry, Faculty of Natural Sciences, Hasanuddin University, Makassar, 90245)

Indonesian Journal of Chemistry
Vol 7, No 1 (2007)

Immobilization of glucose oxidase (GOD) enzyme from Penicillium sp-3 local strain has been carried out using ionotropically entrapping method in  Ca-alginate membrane coupled with Na-polyacrilate. The entrapment of the enzyme in diffusion membrane occur spontaneously by cross-linking between Na-alginate/Na-polyacrilate and CaCl2. The GOD enzyme immobilizedby addition of 1 % Na-polyacrilate has the highest encapsulation efficiency, that is 87.13 % with the smallest percentage of diffusion, i.e. 23.37% and the relative activity of 50%. The GOD immobilized enzyme had good stability at the pH range 4 - 7 during 30 minutes of storage and was stable at a temperature of 20 oC. The activity of the GOD enzyme after being utilized continuously for 5 times only decrease up to 47,06 % compared to that in the initial utilization.