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- W2023691646 abstract "Carboxypeptidase Y was immobilized by glutaraldehyde onto microparticulate aminopropyl-silica and subsequently modified with mercuric derivatives and phenacyl-bromide. The chemically modified immobilized enzymes were used in stirred batch and recirculating packed-bed reactors to catalyse peptide synthesis and deamidation. Mercuric derivatives of the immobilized enzyme were used to synthesize peptide esters from N-benzoyl-l-alanine methyl esters and various amino acid methyl esters. While these reactions resulted in generally higher yields than those obtained with the unmodified enzyme, the mercuric derivatives of the immobilized enzyme were unstable, rendering their use in immobilized form impractical. On the other hand, phenacyl-bromide-modified immobilized carboxypeptidase Y was stable under deamidation conditions and was used to catalyse the deamidations of N-benzoyl-l-arginyl-l-methioninamide, N-benzoyl-l-arginyl-l-methionyl-l-leucinamide, and N-benzoyl-l-arginyl-l-methionyl-l-leucyl-l-phenylalaninamide in higher yields than the unmodified immobilized enzyme. Immobilized phenacylated carboxypeptidase Y offers an efficient means to deamidate peptide amide intermediates in enzymatic peptide synthesis." @default.
- W2023691646 created "2016-06-24" @default.
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- W2023691646 date "1989-02-01" @default.
- W2023691646 modified "2023-10-17" @default.
- W2023691646 title "Peptide synthesis and deamidation with chemically modified immobilized carboxypeptidase Y" @default.
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- W2023691646 doi "https://doi.org/10.1016/0141-0229(89)90063-x" @default.
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