Lipase activity in ripening and mature fruit of the oil palm. Stability in vivo and in vitro.
Henderson, J. and Osborne, D.J.
Phytochemistry, Volume 30, Number 4, 1991. Pages 1073-1078.
1991
บทคัดย่อ
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[1-14C]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 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.