Lipase activity in ripening and mature fruit of the oil palm. Stability in vivo and in vitro. - (:unkn) unknown (Oxford : [Publisher not identified], 1991)
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 -14 C\oleate as substrate. The enzyme is liphilic and is readily inactivaded in ivtro at temnperature above 0. In virto, the enzyme activity increases as repening proceeds. The lipase of ripe fruit is particularly sensitive to chilling inactivation (8) with no restoration of activity at 25 but is stable for at least 8 days in fruit held continously at 20 or for short periods (30 min at 55 are sufficient to irreversibly inactivate 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.
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 -14 C\oleate as substrate. The enzyme is liphilic and is readily inactivaded in ivtro at temnperature above 0. In virto, the enzyme activity increases as repening proceeds. The lipase of ripe fruit is particularly sensitive to chilling inactivation (8) with no restoration of activity at 25 but is stable for at least 8 days in fruit held continously at 20 or for short periods (30 min at 55 are sufficient to irreversibly inactivate 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.
Keywords: Elaeis guineensis.; Enzimas.; Lipasa; Palmae.; Palma de aceite