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Polyethylene glycol-modified papain catalyzes peptide bond formation in benzene

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Summary

Papain modified with 2,4-bis(O-methoxypolyethylene glycol)-6-chloro-s-triazine (activated PEG2) was soluble in benzene and retained the enzymic activity. Acid-amide bond formation by the modified enzyme proceeded efficiently in benzene; N-benzoyl-L-alanine alkylamides were synthesized from N-benzoyl-L-alanine methyl ester and various alkylamines, and N-benzoyl-L-alaninyl(oligo)leucine ethyl ester was formed from N-benzoyl-L-alanine methyl ester and L-leucine ethyl ester.

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Authors and Affiliations

  1. Laboratory of Biological Chemistry, Tokyo Institute of Technology Ookayama, Meguroku, Tokyo 152, Japan

    H. Lee, K. Takahashi, Y. Kodera, K. Ohwada, T. Tsuzuki, A. Matsushima & Y. Inada

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  1. H. Lee
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  2. K. Takahashi
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  3. Y. Kodera
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  4. K. Ohwada
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  5. T. Tsuzuki
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  6. A. Matsushima
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  7. Y. Inada
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Lee, H., Takahashi, K., Kodera, Y. et al. Polyethylene glycol-modified papain catalyzes peptide bond formation in benzene. Biotechnol Lett 10, 403–407 (1988). https://doi.org/10.1007/BF01087438

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