Advanced Search
Syntax
Search...
Volcani treasures
About
Terms of use
Manage
Community:
אסיף מאגר המחקר החקלאי
Powered by ClearMash Solutions Ltd -
Polyphenol oxidase isoenzymes in avocado
Year:
1976
Source of publication :
Phytochemistry
Authors :
Kahn, Varda
;
.
Volume :
15
Co-Authors:
Kahn, V., Division of Food Technology, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel
Facilitators :
From page:
267
To page:
272
(
Total pages:
6
)
Abstract:
Avocado polyphenol oxidase (PPO) was precipitated mainly in the 30-90% saturated ammonium sulfate fraction. The 40-75% saturated ammonium sulfate fraction (the partially purified enzyme) had the highest specific activity in the cultivars Lerman, Horeshim and Fuerte. The PPO was active towards o-dihydroxyphenols. Six active enzymes (a-f) were detected with D,L-DOPA, 4-methylcatechol, catechol, caffeic acid or chlorogenic acid. Band e was the most active in all cases. More isoenzyme bands (fast-moving) were observed with caffeic acid than with 4-methylcatechol. Furthermore, the isoenzyme patterns of the partially purified extracts of the cultivars could be distinguished with respect to caffeic acid. © 1976.
Note:
Related Files :
Avocado
isoenzymes.
Lauraceae
Persea americana
polyphenoloxidase
Show More
Related Content
More details
DOI :
10.1016/S0031-9422(00)89001-9
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
19469
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:29
Scientific Publication
Polyphenol oxidase isoenzymes in avocado
15
Kahn, V., Division of Food Technology, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel
Polyphenol oxidase isoenzymes in avocado
Avocado polyphenol oxidase (PPO) was precipitated mainly in the 30-90% saturated ammonium sulfate fraction. The 40-75% saturated ammonium sulfate fraction (the partially purified enzyme) had the highest specific activity in the cultivars Lerman, Horeshim and Fuerte. The PPO was active towards o-dihydroxyphenols. Six active enzymes (a-f) were detected with D,L-DOPA, 4-methylcatechol, catechol, caffeic acid or chlorogenic acid. Band e was the most active in all cases. More isoenzyme bands (fast-moving) were observed with caffeic acid than with 4-methylcatechol. Furthermore, the isoenzyme patterns of the partially purified extracts of the cultivars could be distinguished with respect to caffeic acid. © 1976.
Scientific Publication
נגישות
menu      
You may also be interested in