Pectinesterase (EC 3.1.1.11) was extracted and purified from papaya (C
arica papaya L. var. exotica). The procedure adopted for purification
resulted in an approximate 250-fold purification (784 units/mg protein
) with a 45% recovery of the pectinesterase activity. The enzyme was e
luted in a single peak after CM-Sephadex and Sephadex G-100 chromatogr
aphy. The purified enzyme had a uniform specific activity throughout t
he final chromatographic peak. The enzyme preparation was confirmed to
be of homogeneous state by gel filtration and non-denaturing polyacry
lamide gel electrophoresis and it has a molecular weight of approximat
ely 32 000 Da.