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Purification and characterization of barley-aleurone xylanase

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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.

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Abbreviations

GA3 :

gibberellic acid

kDa:

kilodalton

SDS-PAGE:

sodium dodecyl sulfate-polyacrylamide gel electrophoresis

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Benjavongkulchai, E., Spencer, M.S. Purification and characterization of barley-aleurone xylanase. Planta 169, 415–419 (1986). https://doi.org/10.1007/BF00392139

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  • DOI: https://doi.org/10.1007/BF00392139

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