Purification and characterization of barley-aleurone xylanase |
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Authors: | E Benjavongkulchai M S Spencer |
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Institution: | (1) Department of Plant Science, University of Alberta, T6G 2P5 Edmonton, Alta, Canada |
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Abstract: | Xylanase (-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.Abbreviations GA3
gibberellic acid
- kDa
kilodalton
- SDS-PAGE
sodium dodecyl sulfate-polyacrylamide gel electrophoresis |
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Keywords: | Aleurone Hordeum (xylanase) Xylanase |
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