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. 1973 Sep;52(3):252–256. doi: 10.1104/pp.52.3.252

Separation and Characterization of Endopolygalacturonase and Exopolygalacturonase from Peaches

R Pressey a, J K Avants a
PMCID: PMC366480  PMID: 16658542

Abstract

Two polygalacturonases (PG I and PG II) have been separated from extracts of ripe peaches (Prunus persica) by chromatography on Sephadex G-100. PG I hydrolyzes polygalacturonic acid from the nonreducing ends of the molecules, releasing galacturonic acid as the product. It functions optimally at pH 5.5, requires Ca2+ for activity, and hydrolyzes low molecular weight substrates most rapidly. In contrast, PG II cleaves the molecular chain of the substrate randomly with a pH optimum at about 4. This enzyme is most reactive with substrates of intermediate molecular weight. It catalyzes the release of water-soluble, but 70% ethanol-insoluble, pectin from washed peach cell walls.

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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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