Stabilization of penicillin G acylase by immobilization on glutaraldehyde-activated chitosan
Autor: | Luciana Rocha Barros Gonçalves, James A. Silva, Edilson Holanda Costa Filho, Wellington Sabino Adriano, Raquel L. C. Giordano |
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Předmět: |
chemistry.chemical_classification
Chromatography Immobilized enzyme General Chemical Engineering lcsh:TP155-156 Catalysis Chitosan Stabilization of enzymes Chitosan and immobilization of enzymes chemistry.chemical_compound Hydrolysis Enzyme chemistry Penicillin G acylase Biocatalysis Covalent bond Glutaraldehyde lcsh:Chemical engineering |
Zdroj: | Scopus-Elsevier Brazilian Journal of Chemical Engineering, Vol 22, Iss 4, Pp 529-538 (2005) Goncalves LRB Brazilian Journal of Chemical Engineering, Volume: 22, Issue: 4, Pages: 529-538, Published: DEC 2005 Brazilian Journal of Chemical Engineering v.22 n.4 2005 Brazilian Journal of Chemical Engineering Associação Brasileira de Engenharia Química (ABEQ) instacron:ABEQ |
Popis: | 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. |
Databáze: | OpenAIRE |
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