Purification and characterization of an exo-polygalacturonase produced by Penicillium viridicatum RFC3 in solid-state fermentation
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Data
2007-08-01
Autores
Silva, Denis
Martins, Eduardo Silva
Leite, Rodrigo Simoes Ribeiro
Da Silva, Roberto
Ferreira, Viviani
Gomes, Eleni
Título da Revista
ISSN da Revista
Título de Volume
Editor
Elsevier B.V.
Resumo
The pectinolytic enzyme obtained from Penicillium viridicatum RFC by solid-state fermentation was purified to homogeneity by pretreatment with kaolin (40 mg mL(-1) ) and ultrafiltration. followed by chromatography on a Sephadex G50 column. The apparent molecular weight of the enzyme was 24 kDa. Maximal activity occurred at pH 6.0 and at 60 degrees C. The enzyme proved to be an exo-polygalacturonase, releasing galacturonic acid by hydrolysis of highly esterified pectin. The presence of 10 mM Ba2+ increased the enzyme activity by 96% and its thermal stability by 30%. besides increasing its stability at acid pH. The apparent K-m with apple pectin as substrate was 1.82 mg mL(-1) and the V-max was 81 mu mol min(-1). (c) 2007 Elsevier Ltd. All rights reserved.
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Palavras-chave
polygalacturonase, Penicillium, solid-state fermentation, purification
Como citar
Process Biochemistry. Oxford: Elsevier B.V., v. 42, n. 8, p. 1237-1243, 2007.