Pectinases are today one of the upcoming enzymes of the commercial sector. A lot of this enzymes are commercially available, due to their all-embracing applications in bio scouring of cotton, degumming of plant fibers, with several industrial uses. The aim of the present study is to purify and characterize Pectin methyl esterase (PME) from Aspergillus niger (A. niger) grown on pineapple peel residue in a solid-state fermentation process. The optimum conditions of pectinase production were carried out by growing Aspergillus niger on basal media containing pectin as inducer at a pH 5.5, temperature of 30oC, and fermentation times of 96 h. The optimum pectinase activities were performed at various pH (4.0-9.0), and temperatures (25 to 90oC), The influence of metals ions was conducted using Zn2+, Mg2+, K+, Na+, Ca2+; EDTA and Mercaptoethanol were used as inhibitors at range concentrations from 10 to 50 mM, respectively. The isolated pectin methyl esterase from A. niger, Ion exchange purification gave about 4.2-fold with specific activity of 7.14 U/mg, and 9.5% enzyme recovery the optimum PME activity was at pH 7.5, and temperature of 45oC; the maximum substrate concentration was 4mg/ml with the Km value of 1.321 and Vmax of 5mMol/min; The present of Ca2+, K+ Mg2+, Na+, and Zn2+, ions significantly activated the enzyme activity, however EDTA and Mercaptoethanol inhibits the PME activity greatly. PME from A. niger is a good microbial enzyme source and pineapple residue a neglected agro waste is an alternative source of PME production that can be exploited industrially.