ABSTRACT The use of proteases for peptide bond formation is now a well established procedure which is complementary considered along with the chemical methods for two main reasons: The first one is related to the mildness of the process as compared to the chemical carboxylic activation, avoiding thus any racemization problem which is often a drawback during the chemical coupling of peptide fragments. The second advantage presented by this biocatalysis can be related to the high regiospecificity of enzymes which allows the use of unprotected side chain components. This review describes recent trends in protease catalysed peptide synthesis in either high or low water content media: briefly, in the former case, the utilization of new specific or site-modified proteases has been reported whereas in the second one, native or modified enzymes have been applied as biocatalysts in organic solvent. Prospects about the newly field of abzymatic peptide synthesis are drawn at the end of this article.
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