Summary
Lipoprotein lipase modified with polyethylene glycol dissolved in benzene, and catalyzed various reactions of ester synthesis, ester exchange and aminolysis. This modified enzyme had a high stability; 50% of the initial enzymic activity were retained after about 3 months-storage in benzene at room temperature. We can repeatedly re-use the enzyme by recovering from benzene solution; the enzyme precipitates upon addition of n-hexane(or petroleum ether).
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Takahashi, K., Nishimura, H., Yoshimoto, T., Saito, Y. and Inada, Y. submitted to Biochem. Biophys. Res. Commun.
Inada, Y., Nishimura, H., Takahashi, Yoshimoto, T., Saha, A.R. and Saito, Y. submitted to Biochim. Biophy. Acta.
Nishimura, Y., Takahashi, K., Sakurai, K., Fujinuma, Y., Imamura, Y., Ooba, M. and Inada, Y. (1983), Life Sci. 33, 1467–1473.
Hill, T.U. (1947), Anal. Chem. 19, 932–933.
Kimura, M., Murayama, K., Nomoto, M. and Fujita, Y. (1969), J. Chromatog. 41, 458–461.
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Yoshimoto, T., Takahashi, K., Nishimura, H. et al. Modified lipase having high stability and various enzymic activities in benzene, and its re-use by recovering from benzene solution. Biotechnol Lett 6, 337–340 (1984). https://doi.org/10.1007/BF00138001
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DOI: https://doi.org/10.1007/BF00138001