Purification and characterization of pectinmethylesterase from Ficus awkeotsang Makino achenes

• Published in: Plant physiology (Bethesda) Vol. 91; no. 4; pp. 1445 - 1453
• Main Authors: Lin, T.P, Liu, C.C, Chen, S.W, Wang, W.Y
• Format: Journal Article
• Language: English
• Published: Rockville, MD American Society of Plant Physiologists 01.12.1989
• Subjects: Achenes; Amino acids; Antiserum; biochemistry; Biological and medical sciences; characterization; Citrus; cross reaction; enzyme activity; Enzymes; esterases; Ficus; Fundamental and applied biological sciences. Psychology; Gels; immunochemistry; isoelectric point; Metabolism; Metabolism and Enzymology; molecular weight; pectins; pericarp; physicochemical properties; Plant physiology and development; Proteins; purification; Room temperature; Seed germination; seeds; Solanum lycopersicum var. lycopersicum; Sugars; Water purification; Purification; Fruit; Pectin; Moraceae; Immunochemistry; Molecular weight; Thermal stability; Inorganic cation; Isoelectric point; Dicotyledones; Angiospermae; Spermatophyta; Kinetics; Optimum pH; Pectinesterase; Aminoacid sequence

Pectinmethylesterase from the pericarp of jelly fig (Ficus awkeotsang) achenes was extracted and purified to a specific activity of 289 micromole proton produced per minute per milligram protein. Pectinmethylesterase, a major protein with high specific activity in the crude extract, was monomeric wi...