Isolation and characterization of a thermostable lipase from Bacillus thermoamylovorans NB501
Author:
Affiliation:
1. Department of Biotechnology, The University of Tokyo
2. Kanseigiken Engineering
Publisher
Microbiology Research Foundation
Subject
Applied Microbiology and Biotechnology,Microbiology
Link
https://www.jstage.jst.go.jp/article/jgam/62/6/62_2016.06.002/_pdf
Reference18 articles.
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2. Arpigny, J. L. and Jaeger, K. E. (1999) Bacterial lipolytic enzymes: classification and properties. Biochem. J., 343, 177–183.
3. Brzozowski, A. M., Derewenda, U., Derewenda, Z. S., Dodson, G. G., Lawson, D. M. et al. (1991) A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. Nature, 351, 491–494.
4. Chahinian, H., Ali, Y. B., Abousalham, A., Petry, S., Mandrich, L. et al. (2005) Substrate specificity and kinetic properties of enzymes belonging to the hormone-sensitive lipase family: comparison with non-lipolytic and lipolytic carboxylesterases. Biochim. Biophys. Acta, 1738, 29–36.
5. Chow, J., Kovacic, F., Dall Antonia, Y., Krauss, U., Fersini, F. et al. (2012) The metagenome-derived enzymes LipS and LipT increase the diversity of known lipases. PLoS ONE, 7, e47665.
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