Pectic Enzymes in Pectolyase
Open Access
- 1 May 1989
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 90 (1) , 191-196
- https://doi.org/10.1104/pp.90.1.191
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.This publication has 12 references indexed in Scilit:
- The Induction of Ethylene Production from Pear Cell Culture by Cell Wall FragmentsPlant Physiology, 1986
- Induction of ethylene biosynthesis in tobacco leaf discs by cell wall digesting enzymesBiochemical and Biophysical Research Communications, 1982
- A rapid method for isolation of mesophyll protoplastsCanadian Journal of Botany, 1979
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- Pectic EnzymesAdvances in Carbohydrate Chemistry and Biochemistry, 1976
- Enzymatic Maceration of Plant Tissues by Endo-Pectin Lyase and Endo-Polygalacturonase from Aspergillus japonicusPhytopathology®, 1976
- Evidence for a Factor that Stimulates Tissue Maceration by Pectolytic EnzymesPhytopathology®, 1976
- New method for quantitative determination of uronic acidsAnalytical Biochemistry, 1973
- Purification and Properties of a Polygalacturonic Acid-trans-eliminase Produced by Clostridium multifermentans*Biochemistry, 1964
- Studies relating to the purification and properties of pectin transeliminaseArchives of Biochemistry and Biophysics, 1962