Purification of polyphenol oxidase from borage (Trachystemon orientalis L.) by using three-phase partitioning and investigation of kinetic properties.
Int J Biol Macromol
; 93(Pt A): 1051-1056, 2016 Dec.
Article
en En
| MEDLINE
| ID: mdl-27664922
ABSTRACT
In this study a Polyphenol oxidase from borage plant was purified with 3.59-fold enrichment in the specific activity and 68.75% recovery of the total activity by using three-phase partitioning purification technique for the first time. Its molecular weight was found around 80kDa with sodium dodecyl sulfate polyacrylamide gel electrophoresis. The optimum pH and temperature values of the enzyme for the used four substrates ranged between the pH 5.0-7.5 and 5-30°C. The kcat/Km values showed that the enzyme has the greatest reactivity toward caffeic acid among the substrates used. Ascorbic acid, l-cysteine and sodium metabisulfite markedly inhibited borage polyphenol oxidase activity.
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Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas de Plantas
/
Catecol Oxidasa
/
Boraginaceae
Idioma:
En
Revista:
Int J Biol Macromol
Año:
2016
Tipo del documento:
Article