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. 1989 May;90(1):191–196. doi: 10.1104/pp.90.1.191

Pectic Enzymes in Pectolyase

Separation, Characterization, and Induction of Ethylene in Fruits

Elizabeth A Baldwin 1, Russell Pressey 1
PMCID: PMC1061697  PMID: 16666734

Abstract

The pectic enzymes in Pectolyase were separated by ion exchange chromatography on Q-Sepharose. Three pectin lyases, two polygalacturonases, and a pectinmethylesterase were resolved. The enzymes were further purified on Mono Q and/or Mono S columns to remove traces of cellulase. The enzymes had molecular weights ranging from 25,000 to 36,000 daltons. They were optimally active between pH 4.0 and 6.2 and were not greatly affected by ions. The pectin lyases and polygalacturonases were endo-enzymes. They solubilized uronic acids from washed cell wall fragments, but the lyases were much more effective than the polygalacturonases. The mixture of enzymes constituting Pectolyase increased ethylene production 15- to 25-fold when introduced into tomato and orange fruits. The enzymes purified from Pectolyase all increased ethylene production in the fruits but the lyases were generally more effective than the hydrolases.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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