Lipases are enzymes capable of catalyzing a great variety of reactions that are interesting to food, pharmaceutical, chemical, and other industries. This versatility is also due to the different substrate specificity possibilities that lipases from various sources. For this reason, lipase producing microorganisms are being searched by research groups around the world. This paper presents the properties of a extracellular lipase produced by a newly isolated strain of Rhizopus sp. The crude enzyme showed optimal activity at 40ºC, between 6.0 and 6.5 pH values and kept 50% of it´s activity after treatment between 40ºC and 55ºC for 60 minutes. The hydrolytic activity of the crude extract was greater when coconut fat was used as substrate. This shows the affinity of the lipase to saturated medium chain fatty acids. The fractions I and II, that were obtained after the partial purification of the lipase, showed biochemical characteristics similar to the crude extract.
enzyme; lipase; Rhizopus sp.; biochemical characterization
