Purification and characterization of barley-aleurone xylanase.
Planta
; 169(3): 415-9, 1986 Nov.
Article
em En
| MEDLINE
| ID: mdl-24232655
ABSTRACT
Xylanase (ß-1,4-D-xylan xylanohydrolase; EC 3.2.1.8) from aleurone layers of barley (Hordeum vulgare L. cv. Himalaya) was purified and characterized. Purification was by preparative isoelectric focusing and a Sephadex G-200 column. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the enzyme showed a single protein band with an apparent molecular weight (Mr)=34000 daltons. The isoelectric point of the enzyme was 4.6. The enzyme had maximum activity on xylan at pH 5.5 and at 35° C. It was most stable between pH 5 and 6 and at temperatures between 0 and 4° C. The Km was 0.86 mg xylan·ml(-1).
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Coleções:
01-internacional
Base de dados:
MEDLINE
Idioma:
En
Revista:
Planta
Ano de publicação:
1986
Tipo de documento:
Article