Immobilization of glucose isomerase in surface-modified alginate gel beads

Date

2008-04-01

Author

TÜMTÜRK, HAYRETTİN
DEMİREL, Gökhan
ALTINOK, HAYDAR
AKSOY, SERPİL
Hasırcı, Nesrin

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In this study, glucose isomerase enzyme was entrapped into modified and nonmodified calcium alginate gel beads. Various characteristics of free and immobilized enzymes such as the optimum pH, temperature and dependence of activity on storage and operational stability were evaluated. The optimum pH and temperature of free and immobilized glucose isomerase were found to be the same values as 7.5 and 60C, respectively. For free and immobilized enzymes, kinetic parameters were calculated as 1.79 x 10(-2) and 8.27 x 10(-3) mol/L for Km, and 2.39 x 10(-3) and 6.03 x 10(-3) mol/L min for V-max, respectively. After 42 days of storage at 4C, free enzyme retained 56% of its initial activity, while for the immobilized enzyme, this value was observed as 86%. The immobilized samples were used repeatedly 22 times by retaining more than 85% of their initial activity.

Subject Keywords

Enzyme, Encapsulation, Performance, Entrapment, Invertase, Support

URI

https://hdl.handle.net/11511/31051

Journal

JOURNAL OF FOOD BIOCHEMISTRY

DOI

https://doi.org/10.1111/j.1745-4514.2008.00171.x

Collections

Graduate School of Natural and Applied Sciences, Article

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Citation Formats

H. TÜMTÜRK, G. DEMİREL, H. ALTINOK, S. AKSOY, and N. Hasırcı, “Immobilization of glucose isomerase in surface-modified alginate gel beads,” JOURNAL OF FOOD BIOCHEMISTRY, pp. 234–246, 2008, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/31051.