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Published on: December 12, 2013
Purification and general properties of pectin methyl esterase from Curvularia inaequalis NRRL 13884 in solid state
A F Afifi1, E M Fawzi, M A Foaad
1Department of Biological Sciences, Faculty of Education, Ain Shams University, Heliopolis, Roxy, Cairo, Egypt.
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.
