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

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-algi...

Full description

Bibliographic Details
Main Authors: Ahyar Ahmad, Andi Syaiful, Firman AP Firman AP, Abdul Rauf Patong
Format: Article
Language:English
Published: Universitas Gadjah Mada 2010-06-01
Series:Indonesian Journal of Chemistry
Online Access:https://jurnal.ugm.ac.id/ijc/article/view/21721
id doaj-adafa6405d7e4833892c422b577e5e16
record_format Article
spelling doaj-adafa6405d7e4833892c422b577e5e162020-11-25T01:04:37ZengUniversitas Gadjah MadaIndonesian Journal of Chemistry1411-94202460-15782010-06-01719710410.22146/ijc.2172114819IMMOBILIZATION OF GLUCOSE OXIDASE ENZYME FROM Penicillium sp-3 LOCAL STRAINAhyar Ahmad0Andi Syaiful1Firman AP Firman AP2Abdul Rauf Patong3Biochemistry and Biotechnology Laboratory, Department of Chemistry, Faculty of Natural Sciences, Hasanuddin University, Makassar, 90245Biochemistry and Biotechnology Laboratory, Department of Chemistry, Faculty of Natural Sciences, Hasanuddin University, Makassar, 90245Bioprocess Laboratory, Ujung Pandang State Polytechnic, Makassar, 90245.Biochemistry and Biotechnology Laboratory, Department of Chemistry, Faculty of Natural Sciences, Hasanuddin University, Makassar, 90245Immobilization 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 immobilized by 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.   Keywords: immobilization, glucose oxidase, Penicillium sp-3, calcium alginate, sodium  polyacrilate.https://jurnal.ugm.ac.id/ijc/article/view/21721
collection DOAJ
language English
format Article
sources DOAJ
author Ahyar Ahmad
Andi Syaiful
Firman AP Firman AP
Abdul Rauf Patong
spellingShingle Ahyar Ahmad
Andi Syaiful
Firman AP Firman AP
Abdul Rauf Patong
IMMOBILIZATION OF GLUCOSE OXIDASE ENZYME FROM Penicillium sp-3 LOCAL STRAIN
Indonesian Journal of Chemistry
author_facet Ahyar Ahmad
Andi Syaiful
Firman AP Firman AP
Abdul Rauf Patong
author_sort Ahyar Ahmad
title IMMOBILIZATION OF GLUCOSE OXIDASE ENZYME FROM Penicillium sp-3 LOCAL STRAIN
title_short IMMOBILIZATION OF GLUCOSE OXIDASE ENZYME FROM Penicillium sp-3 LOCAL STRAIN
title_full IMMOBILIZATION OF GLUCOSE OXIDASE ENZYME FROM Penicillium sp-3 LOCAL STRAIN
title_fullStr IMMOBILIZATION OF GLUCOSE OXIDASE ENZYME FROM Penicillium sp-3 LOCAL STRAIN
title_full_unstemmed IMMOBILIZATION OF GLUCOSE OXIDASE ENZYME FROM Penicillium sp-3 LOCAL STRAIN
title_sort immobilization of glucose oxidase enzyme from penicillium sp-3 local strain
publisher Universitas Gadjah Mada
series Indonesian Journal of Chemistry
issn 1411-9420
2460-1578
publishDate 2010-06-01
description 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 immobilized by 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.   Keywords: immobilization, glucose oxidase, Penicillium sp-3, calcium alginate, sodium  polyacrilate.
url https://jurnal.ugm.ac.id/ijc/article/view/21721
work_keys_str_mv AT ahyarahmad immobilizationofglucoseoxidaseenzymefrompenicilliumsp3localstrain
AT andisyaiful immobilizationofglucoseoxidaseenzymefrompenicilliumsp3localstrain
AT firmanapfirmanap immobilizationofglucoseoxidaseenzymefrompenicilliumsp3localstrain
AT abdulraufpatong immobilizationofglucoseoxidaseenzymefrompenicilliumsp3localstrain
_version_ 1715861578659659776