Immobilization of glucoamylase onto activated pHEMA/EGDMA microspheres: properties and application to a packed-bed reactor

Date

1998-02-15

Author

Arica, MY
Alaeddinoglu, NG
Hasırcı, Vasıf Nejat

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Glucoamylase was covalently immobilized onto pHEMA/EGDMA microspheres of two different sizes: 50-100 mu m and 100-200 mu m in diameter. The activity of the enzyme on smaller microspheres was found to be almost twice that of the larger microspheres. A higher enzyme lending was observed on small microspheres (0.64 mg g(-1) support) as compared to large spheres (0.40 mg g(-1) support). The K-m of glucoamylase was significantly increased (approximately five times) upon immobilization, indicating decreased affinity by the enzyme for its substrate. V-max of the enzyme was, however, not as significantly altered upon immobilization as the K-m. More significantly, the V-max was much higher with the large substrate (dextrin) than it was with the small substrate (maltose). Activity of the immobilized enzyme was quite stable. In 120 h, only 9.0% of the immobilized glucoamylase activity was lost. (C) 1998 Elsevier Science Inc.

Subject Keywords

pHEMA/EGDMA microspheres, Covalent bonding, Enzyme immobilization, Glucoamylase, Enzyme reactor

URI

https://hdl.handle.net/11511/32674

Journal

ENZYME AND MICROBIAL TECHNOLOGY

DOI

https://doi.org/10.1016/s0141-0229(97)00139-7

Collections

Graduate School of Natural and Applied Sciences, Article

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Citation Formats

M. Arica, N. Alaeddinoglu, and V. N. Hasırcı, “Immobilization of glucoamylase onto activated pHEMA/EGDMA microspheres: properties and application to a packed-bed reactor,” ENZYME AND MICROBIAL TECHNOLOGY, pp. 152–157, 1998, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/32674.