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Purification and characterization of barley-aleurone xylanase

✍ Scribed by E. Benjavongkulchai; M. S. Spencer

Publisher
Springer-Verlag
Year
1986
Tongue
English
Weight
590 KB
Volume
169
Category
Article
ISSN
0032-0935

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✦ Synopsis

Xylanase (fl-l,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 K m was 0.86 mg xylan'm1-1.

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