Abstract: Penicillium species grew in a synthetic medium with pectin as the sole carbon source producing proteins which expressed alkaline pectin lyase activity. The enzyme was purified by a combination of ammonium sulphate precipitation, dialysis, gel filtration and ion-exchange chromatography. Optimum activity of the enzyme was at 35°C and at pH 80. The enzyme was stimulated by K+, Na+, Ca++ and Mg++ but inhibited by EDTA and Hg++. The enzyme was able to degrade pectin with optimum activity expressed at 16 mg mL‾1.