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Purification and characterization of β-mannanase from Bacillus licheniformis for industrial use

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Abstract

An easily scaled-up technique has been designed to purify β-mannanase from Bacillus licheniformis. Using flocculation, ultrafiltration and ion-exchange chromatography, the enzyme was purified 33-fold with a final recovery of 47% and a specific activity of 4341 U mg−1protein. The enzyme had maximum activity at 60 °C and pH 7.0. It was stable at 50 °C and pH 6.0 for 6 h, but lost all of its activity when held at 70 °C and pH 6.0 for 1 h.

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Authors and Affiliations

  1. Laboratory of Enzyme Technology, Chemical Engineering Research Center, Tianjin University, Tianjin, 300072, P.R. China

    Jun Zhang, Zhimin He & Kun Hu

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  1. Jun Zhang
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  2. Zhimin He
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  3. Kun Hu
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Zhang, J., He, Z. & Hu, K. Purification and characterization of β-mannanase from Bacillus licheniformis for industrial use. Biotechnology Letters 22, 1375–1378 (2000). https://doi.org/10.1023/A:1005644414762

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  • DOI: https://doi.org/10.1023/A:1005644414762

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