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Benjavongkulchai E, Spencer MS. Purification and characterization of barley-aleurone xylanase. Planta. 1986;169(3):415-9doi: 10.1007/BF00392139.
Benjavongkulchai, E., & Spencer, M. S. (1986). Purification and characterization of barley-aleurone xylanase. Planta, 169(3), 415-9. https://doi.org/10.1007/BF00392139
Benjavongkulchai, E, and Spencer, M S. "Purification and characterization of barley-aleurone xylanase." Planta vol. 169,3 (1986): 415-9. doi: https://doi.org/10.1007/BF00392139
Benjavongkulchai E, Spencer MS. Purification and characterization of barley-aleurone xylanase. Planta. 1986 Nov;169(3):415-9. doi: 10.1007/BF00392139. PMID: 24232655.
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Planta. 1986 Nov;169(3):415-9. doi: 10.1007/BF00392139.

Purification and characterization of barley-aleurone xylanase.

Planta

E Benjavongkulchai, M S Spencer

Affiliations

  1. Department of Plant Science, University of Alberta, T6G 2P5, Edmonton, Alta, Canada.

PMID: 24232655 DOI: 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).

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