Stabilization of penicillin G acylase by immobilization on glutaraldehyde-activated chitosan
The objective of this work was to study enzyme immobilization on chitosan activated with glutaraldehyde, aiming to produce a cheap biocatalyst. Two different immobilization strategies were studied: one-point and multipoint covalent attachment to the solid matrix. The multipoint covalent attachment derivative had an 82% immobilization yield. It was 4.9-fold more stable than the free enzyme at 50°C and 4.5-fold more stable than soluble enzyme at pH 10.0. The one-point derivative had an 85% immobilization yield. It was 2.7-fold more stable than the free enzyme at 50°C and 3.8-fold more stable than soluble PGA at pH 10.0. Results indicated that chitosan can be loaded with PGA above 330 IU/g. Intraparticle diffusive effects, however, limited hydrolysis of penicillin G catalyzed by those derivatives at 37°C and 25°C. Operational stability assays were performed and the multipoint derivative exhibited a half-life of 40 hours.
| Main Authors: | , , , , |
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| Format: | Digital revista |
| Language: | English |
| Published: |
Brazilian Society of Chemical Engineering
2005
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| Online Access: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322005000400005 |
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