אסיף מאגר המחקר החקלאי

Single step chromatographic purification and characterization of the endopolygalacturonases and pectinesterases of the fungus, Botrytis cinerea Pers

Year:

1983

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Volume :

23

Co-Authors:

Marcus, L., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Ramat Aviv, 69978, Israel
Schejter, A., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Ramat Aviv, 69978, Israel

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Abstract:

This communication describes the purification, in a single chromatographic step on cross-linked polypectate, of two pectinesterases and two endopolygalacturonases found inthe extracellular fluid of cultures of the fungus, Botrytis cinerea. The endopolygalacturonases, PG-I and PG-II, have molecular weights of 34 000 and 56 000, respectively. They differ in their chromatographic behaviour, PG-II being more strongly retained by the cross-linked polypectate column. The pectinesterases, PE-I and PE-II, have nearly identical molecular weights of about 28 000 and very similar amino acid compositions, suggesting a common genetic origin. It is shown that Michaelis-Menten behaviour is obeyed by all these enzymes. The enzyme kinetic constants of PG-I and PG-II are strongly dependent on the salt concentration of the medium; both polyglutamate and pectin act as competitive inhibitors. The properties of PE-I and PE-II of B. cinerea are found to be strikingly similar to those of the two pectin-esterases purified from oranges. © 1983.

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