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Production, purification and characterization of an endopolygalacturonase from Mucor rouxii NRRL 1894

Paper ID Volume ID Publish Year Pages File Format Full-Text
18090 42711 2007 6 PDF Available
Title
Production, purification and characterization of an endopolygalacturonase from Mucor rouxii NRRL 1894
Abstract

An extracellular polygalacturonase (PGase) from Mucor rouxii NRRL 1894 was purified to homogeneity by two chromatographic steps using CM-Sepharose and Superdex 75. The purified enzyme was a monomer with a molecular weight of 43100 Da and a pI of 6. The PGase was optimally active at 35 °C and at pH 4.5. It was stable up to 30 °C and stability of PGase decrease rapidly above 60 °C. The extent of hydrolysis of different pectins was decreased with increasing of degrees of esterification. Except Mn2+, all the examined metal cations showed inhibitory effects on the enzyme activity. The apparent Km and Vmax values for hydrolyze of polygalacturonic acid (PGA) were 1.88 mg/ml and 0.045 μmol/ml/min, respectively. The enzyme released a series of oligogalacturonates from polygalacturonic acid indicating that it had an endo-action. Its N-terminal sequence showed homologies with the endopolygalacturonase from the psychrophilic fungus Mucor flavus.

Keywords
Mucor rouxii; Pectin; Polygalacturonase
First Page Preview
Production, purification and characterization of an endopolygalacturonase from Mucor rouxii NRRL 1894
Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 41, Issues 6–7, 1 November 2007, Pages 800–805
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering