LIPASE ACTIVITY IN RIPENING AND MATURE FRUIT OF THE OIL PALM - STABILITY INVIVO AND INVITRO

A quick and reliable method is described for the extraction and assay of active lipase from ripening fruits of the oil palm using glycerol tri[1-C-14]oleate as substrate. The enzyme is lipophilic and is readily inactivated in vitro at temperatures above 0-degrees. In vivo, the enzyme activity increases as ripening proceeds. The lipase of ripe fruit is particularly sensitive to chilling inactivation (8-degrees) with no restoration of activity at 25-degrees but is stable for at least 8 days in fruit held continuously at 20-degrees or for short periods (30 min) at 45-degrees. Extended periods (10 hr) at 45-degrees or 30 min at 55-degrees are sufficient to irreversibly inactive the enzyme in intact fruit. Enzyme induction is coincident with the onset of fruit ripening and would appear to be the ripening-associated expression of a new gene activity.