Abstract
An alkaline cellulase from Bacillus sp. HSH-810 was purified 8.7-fold with a 30% yield and a specific activity of 71 U mg−1 protein. It was optimally active at pH 10 and 50 °C and was stable from pH 6 to 10 with more than 60% activity remaining after heating at 60 °C for 60 min. The molecular mass of cellulase was 80 kDa. It was inhibited by 50% by Fe3+ (1 mM) and Mn2+ (0.1 mM) but was relatively insensitive to Hg2+ and Pb2+ at 1 mM.
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Revisions requested: 8 October 2004/1 December 2004; Revisions received 29 November 2004/5 January 2005
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Kim, JY., Hur, SH. & Hong, JH. Purification and characterization of an alkaline cellulase from a newly isolated alkalophilic Bacillus sp. HSH-810. Biotechnol Lett 27, 313–316 (2005). https://doi.org/10.1007/s10529-005-0685-5
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DOI: https://doi.org/10.1007/s10529-005-0685-5