Abstract
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 M r was 38 kDa and it had a pI of 4.8 and optimum activity at pH 5.0 and 55°C. It was stable at pH 4 to 9 and below 55°C. The amino acid composition of the enzyme was in the order Gly>Glx>Ser and Asx>Ala.
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Additional information
N.S. Mendoza and L.M. Joson are with Industrial Technology Development Institute, Department of Science and Technology, Manila, Philippines. M. Arai and T. Kawaguchi are with Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture, Sakai, Osaka 593, Japan; T. Yoshida is with Faculty of Engineering, Osaka University, Suita, Osaka 565, Japan.
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Mendoza, N.S., Arai, M., Kawaguchi, T. et al. Purification and properties of mannanase from Bacillus subtilis . World J Microbiol Biotechnol 10, 551–555 (1994). https://doi.org/10.1007/BF00367665
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DOI: https://doi.org/10.1007/BF00367665