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lip2, a novel lipase gene cloned from Aspergillus niger exhibits enzymatic characteristics distinct from its previously identified family member

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Abstract

We have cloned a novel lipase gene, lip2, from Aspergillus niger and expressed it in Escherichia coli. Upon purification of the recombinant Lip2 protein, its properties were characterized. In comparison with a previously identified lipase Lip1, both enzymes are acid lipases (optimal pH <6.5), Ca2+-dependent and PMSF-sensitive, but have different molecular weights (35 and 43 kDa), optimal substrate spectra (C10 and C8), optimal reaction temperatures (45 and 50°C) and thermal stability. Circular dichroism spectroscopy revealed that Lip2 contains a typical Ca2+-active site. This first report on the cloning of the Lip2 gene and its enzymatic characteristics may greatly facilitate its potential industrial application.

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Acknowledgements

We thank Dr. S. Arellan for her help on English revision, and Dr. B. Z. Cheng for his help on statistic analysis. This work was supported by Chinese High-tech Research and Development Program (2007AA05Z417).

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Authors and Affiliations

  1. Key Laboratory of Molecular Bio-Physics of Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, 430074, Wuhan, China

    Jiangke Yang & Yunjun Yan

  2. Department of Biology, Hong Kong Baptist University, Hong Kong, China

    Jin Sun

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  1. Jiangke Yang
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  2. Jin Sun
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  3. Yunjun Yan
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Correspondence to Jiangke Yang.

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Yang, J., Sun, J. & Yan, Y. lip2, a novel lipase gene cloned from Aspergillus niger exhibits enzymatic characteristics distinct from its previously identified family member. Biotechnol Lett 32, 951–956 (2010). https://doi.org/10.1007/s10529-010-0238-4

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  • DOI: https://doi.org/10.1007/s10529-010-0238-4

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