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- W1974208049 abstract "Abstract Erwinia chrysanthemi produced extracellular enzymes which degrade pectic acid in a trans -eliminative manner. Isolate 307, from carnation, produced at least two, and isolate EC 23 , from Philodendron , produced at least four polygalacturonic acid trans -eliminases. The enzymes produced by each isolate were separated from each other and purified by ammonium sulfate fractionation, diethylaminoethylcellulose column chromatography, and electrofocusing. Molecular weights for the six enzymes ranged between 30,000 and 36,000 as determined by gel filtration in Sephadex G-75 and sucrose density gradient centrifugation. The isoelectric points of two enzyme fractions from isolate 307 were pH 9·1 and 7·9 and those for the four enzyme fractions from isolate EC 23 were pH 9·4, 8·4, 7·9 and 4·6. Random cleavage of pectic acid was greatest with the enzyme fractions having isoelectric points at pH 9·4 and 9·1, intermediate for the fraction with an isoelectric point at pH 4·6, and least with the fractions with isoelectric points at pH 8·4 and 7·9. All of the trans -eliminases exhibited a Ca 2+ requirement and had pH optima between pH 8·2 and 9·8. All but one of the purified polygalacturonic acid trans -eliminase fractions from both E. chrysanthemi isolates induced electrolyte loss, maceration and cell death of potato tissue. The enzyme fraction with an isoelectric point at pH 4·6 from isolate EC 23 did not macerate potato, carrot or cucumber tissue even though it readily degraded pectic acid prepared from onion, carrot and cucumber as well as commercial sources of sodium polypectate, polygalacturonic acid and pectin N.F." @default.
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- W1974208049 date "1971-01-01" @default.
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- W1974208049 title "Pectic enzymes produced by Erwinia chrysanthemi and their effects on plant tissue" @default.
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- W1974208049 doi "https://doi.org/10.1016/0048-4059(71)90037-3" @default.
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