Purification and general properties of pectin methyl esterase from Curvularia inaequalis NRRL 13884 in solid state culture using orange peels as an inducer.
Identifieur interne : 000089 ( Ncbi/Curation ); précédent : 000088; suivant : 000090Purification and general properties of pectin methyl esterase from Curvularia inaequalis NRRL 13884 in solid state culture using orange peels as an inducer.
Auteurs : A F Afifi [Égypte] ; E M Fawzi ; M A FoaadSource :
- Acta microbiologica Polonica [ 0137-1320 ] ; 2002.
English descriptors
- KwdEn :
- MESH :
- chemical , isolation & purification : Carboxylic Ester Hydrolases.
- enzymology : Ascomycota.
- metabolism : Ascomycota, Carboxylic Ester Hydrolases, Citrus sinensis.
- Chromatography, DEAE-Cellulose, Chromatography, Gel, Hydrogen-Ion Concentration, Kinetics, Temperature.
Abstract
Pectin methyl esterase (PME) [E.C.3. 1.1.11] production by Curvularia inaequalis (Shear) Boedijn NRRL 13884 was investigated using solid-state culture. The highest level of extracellular pectin methyl esterase was detected with orange peels as an inducing substrate and as a sole carbon source. The enzyme was partially purified using Sephadex G-100 and DEAE-Cellulose column chromatography. It was purified about 40 fold with optimum activity at pH 4.4 and 45 degrees C. The enzyme was activated by Co++, Mg++, Na+, whereas it was slightly activated in the presence of Cu++, K+, Mn++, Zn++. On the other hand Ag++, Ca++ and Hg++ inhibited the activity of the enzyme. The Km was calculated to be 0.52 mM.
PubMed: 12588098
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pubmed:12588098Le document en format XML
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