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Enzymatic transesterification of monosaccharides and amino acid esters in organic solvents

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Summary

Lipases and proteases from different sources were screened for their ability to catalyze the transesterification of glucose and activated N-blocked phenylalanine. A commercial protease from Bacillus licheniformis was found to be most effective for this purpose. On a basis of 13C-NMR analysis, glucose was acylated at the C-6 position. The enzyme showed a broad substrate specificity toward various monosaccharides.

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Authors and Affiliations

  1. BioProcess Engineering Research Center and Department of Chemical Engineering, Korea Advanced Institute of Science and Technology(KAIST), 305-701, Taedok Science Town, Taejon, Korea

    Oh-Jin Park, Hyun Gyu Park & Ji-Won Yang

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  1. Oh-Jin Park
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  2. Hyun Gyu Park
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  3. Ji-Won Yang
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Park, OJ., Park, H.G. & Yang, JW. Enzymatic transesterification of monosaccharides and amino acid esters in organic solvents. Biotechnol Lett 18, 473–478 (1996). https://doi.org/10.1007/BF00143473

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  • DOI: https://doi.org/10.1007/BF00143473

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