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Purification and characterisation of an alkaline protease used in tannery industry from Bacillus licheniformis

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Abstract

An extracellular alkaline protease produced by Bacillus licheniformis AP-1 was purified 76-fold, yielding a single 28 kDa band on SDS-PAGE. It was optimally active at pH 11 and at 60°C (assayed over 10 min). The protease was completely inhibited by phenylmethylsulfonyl fluoride and diodopropyl fluorophosphate, with little increase upon Ca2+ and Mg2+ addition.

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Authors and Affiliations

  1. The Key Laboratory of Industrial Biotechnology, Ministry of Education, Research Center of Industrial Microbiology, Southern Yangtze University, Wuxi, 214036, P.R. China

    Xue-Ming Tang, Wei Shen, Wei-Lan Shao, Hui-Ying Fang, Zheng-Xiang Wang & Jian Zhuge

  2. Department of Microbiology, University of Stellenbosch, Private Bag X1, Matieland, 7602, South Africa Fax

    Xue-Ming Tang, F.M. Lakay & B.A. Prior

Authors
  1. Xue-Ming Tang
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  2. F.M. Lakay
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  3. Wei Shen
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  4. Wei-Lan Shao
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  5. Hui-Ying Fang
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  6. B.A. Prior
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  7. Zheng-Xiang Wang
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  8. Jian Zhuge
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Tang, XM., Lakay, F., Shen, W. et al. Purification and characterisation of an alkaline protease used in tannery industry from Bacillus licheniformis . Biotechnology Letters 26, 1421–1424 (2004). https://doi.org/10.1023/B:BILE.0000045642.19299.3f

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  • DOI: https://doi.org/10.1023/B:BILE.0000045642.19299.3f

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