Your browser doesn't support javascript.
loading
Purification and characterization of barley-aleurone xylanase.
Benjavongkulchai, E; Spencer, M S.
Afiliação
  • Benjavongkulchai E; Department of Plant Science, University of Alberta, T6G 2P5, Edmonton, Alta, Canada.
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).

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: Planta Ano de publicação: 1986 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: Planta Ano de publicação: 1986 Tipo de documento: Article