Purification and characterization of an exo-polygalacturonase produced by Penicillium viridicatum RFC3 in solid-state fermentation


Autoria(s): Silva, Denis; Martins, Eduardo Silva; Leite, Rodrigo Simoes Ribeiro; Da Silva, Roberto; Ferreira, Viviani; Gomes, Eleni
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

20/05/2014

20/05/2014

01/08/2007

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.

Formato

1237-1243

Identificador

http://dx.doi.org/10.1016/j.procbio.2007.05.025

Process Biochemistry. Oxford: Elsevier B.V., v. 42, n. 8, p. 1237-1243, 2007.

1359-5113

http://hdl.handle.net/11449/21742

10.1016/j.procbio.2007.05.025

WOS:000248975400008

Idioma(s)

eng

Publicador

Elsevier B.V.

Relação

Process Biochemistry

Direitos

closedAccess

Palavras-Chave #polygalacturonase #Penicillium #solid-state fermentation #purification
Tipo

info:eu-repo/semantics/article