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Purification and properties of mannanase fromBacillus subtilis

✍ Scribed by N. S. Mendoza; M. Arai; T. Kawaguchi; T. Yoshida; L. M. Joson

Publisher
Springer
Year
1994
Tongue
English
Weight
334 KB
Volume
10
Category
Article
ISSN
1573-0972

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✦ Synopsis

Extracellular mannanase from Bacillus subtilis NM-39, an isolate from Philippine soil, was purified about 240-fold with a yield of 7.3% by ammonium sulphate fractionation, DEAE-Toyopearl chromatography and Sephacryl S-200 gel filtration. Its Mr was 38 kDa and it had a pI of 4.8 and optimum activity at pH 5.0 and 55Β°C. It was stable at pH 4 to 9 and below 55Β°C. The amino acid composition of the enzyme was in the order Gly > Glx > Ser and Asx > Ala.

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