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The effects of reformulating buffer species and their concentrations on subtilisin-catalyzed optical resolution of racemic 1-phenylethylamine in 3-methyl-3-pentanol

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Abstract

For the optical resolution of racemic 1-phenylethylamine in 3-methyl-3-pentanol, subtilisin was reformulated by lyophilization with buffer salts. The amide synthesis activity of subtilisin in organic solvent was compared with the hydrolysis activity in aqueous buffer when different buffer species and their concentrations were used in lyophilization. The enzyme activity in organic solvent showed a different pattern from that of the hydrolysis depending upon the species and the concentrations of buffers. Morphology of the reformulated subtilisin was examined by scanning electron microscopy (SEM). The porosity of reformulated subtilisin particles increased up to the optimal buffer concentrations for the amide synthesis in organic solvent. Glassy looks and decrease in porosity developed at high (i.e. above the optimal) buffer concentrations appear to affect the decrease in the synthetic activity in organic media.

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Correspondence to Byung-Gee Kim.

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Kim, J., Kang, BY. & Kim, BG. The effects of reformulating buffer species and their concentrations on subtilisin-catalyzed optical resolution of racemic 1-phenylethylamine in 3-methyl-3-pentanol. Biotechnol. Bioprocess Eng. 2, 43–47 (1997). https://doi.org/10.1007/BF02932462

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