Purification and characterization of barley-aleurone xylanase
- 1 November 1986
- journal article
- research article
- Published by Springer Nature in Planta
- Vol. 169 (3) , 415-419
- https://doi.org/10.1007/bf00392139
Abstract
Xylanase (β-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.This publication has 24 references indexed in Scilit:
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