Lipase activity in ripening and mature fruit of the oil palm. Stability in vivo and in vitro.

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.

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Bibliographic Details
Main Authors: Henderson, Janice 43612, autor. aut, Osborne, Daphne J. 43611.
Format: Texto biblioteca
Language:n d
Published: Oxford : [Publisher not identified], 1991
Subjects:Elaeis guineensis., Enzimas., Lipasa, Palmae., Palma de aceite,
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spelling cat-fedepalma-149422022-08-04T23:40:44ZLipase activity in ripening and mature fruit of the oil palm. Stability in vivo and in vitro. Henderson, Janice 43612, autor. aut Osborne, Daphne J. 43611. textOxford : [Publisher not identified],1991.n dA 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.Elaeis guineensis.Enzimas.LipasaPalmae.Palma de aceiteURN:ISBN:031-9422/91
institution FEDEPALMA
collection Koha
country Colombia
countrycode CO
component Bibliográfico
access En linea
Fisico
databasecode cat-fedepalma
tag biblioteca
region America del Sur
libraryname Centro de Información y Documentación Palmero
language n d
topic Elaeis guineensis.
Enzimas.
Lipasa
Palmae.
Palma de aceite
Elaeis guineensis.
Enzimas.
Lipasa
Palmae.
Palma de aceite
spellingShingle Elaeis guineensis.
Enzimas.
Lipasa
Palmae.
Palma de aceite
Elaeis guineensis.
Enzimas.
Lipasa
Palmae.
Palma de aceite
Henderson, Janice 43612, autor. aut
Osborne, Daphne J. 43611.
Lipase activity in ripening and mature fruit of the oil palm. Stability in vivo and in vitro.
description 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.
format Texto
topic_facet Elaeis guineensis.
Enzimas.
Lipasa
Palmae.
Palma de aceite
author Henderson, Janice 43612, autor. aut
Osborne, Daphne J. 43611.
author_facet Henderson, Janice 43612, autor. aut
Osborne, Daphne J. 43611.
author_sort Henderson, Janice 43612, autor. aut
title Lipase activity in ripening and mature fruit of the oil palm. Stability in vivo and in vitro.
title_short Lipase activity in ripening and mature fruit of the oil palm. Stability in vivo and in vitro.
title_full Lipase activity in ripening and mature fruit of the oil palm. Stability in vivo and in vitro.
title_fullStr Lipase activity in ripening and mature fruit of the oil palm. Stability in vivo and in vitro.
title_full_unstemmed Lipase activity in ripening and mature fruit of the oil palm. Stability in vivo and in vitro.
title_sort lipase activity in ripening and mature fruit of the oil palm. stability in vivo and in vitro.
publisher Oxford : [Publisher not identified],
publishDate 1991
work_keys_str_mv AT hendersonjanice43612autoraut lipaseactivityinripeningandmaturefruitoftheoilpalmstabilityinvivoandinvitro
AT osbornedaphnej43611 lipaseactivityinripeningandmaturefruitoftheoilpalmstabilityinvivoandinvitro
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