Purification and characterisation of two pectinmethylesterase from persimmon (Diospyros kaki)

Two pectinmethylesterase isoforms, PME I and PME II, have been separated and purified from persimmon using chromatography techniques. Both isoforms presented differences in molecular weight (PME I: 51 kDa, PME II: 30 kDa), isoelectric point (PME I: 8·4, PME II: 6·9) and K_m values (PME I: 54 μg ml⁻¹, PME II: 31 μg ml⁻¹). They differed in their optimum pH and thermal stability, PME I being the more thermostable isoform. Both isoforms exhibited similar behaviour with respect to Ca²⁺ and Na⁺ concentrations and were strongly inhibited by CaCl₂ concentrations of over 80 mM and by NaCl concentrations of over 500 mM . Both isoforms were activated by low concentrations of polygalacturonic acid and were competitively inhibited by D -galacturonic acid and high concentrations of polygalacturonic acid. ©1997 SCI