Hydrolase-catalysed synthesis of peroxycarboxylic acids: Biocatalytic promiscuity for practical applications
| Autor: | Chiara Carboni-Oerlemans, Ab van der Meer, Robert W. van Gemert, Pablo Domínguez de María, Bernard Tuin, Gerrald Bargeman |
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| Přispěvatelé: | University of Twente |
| Rok vydání: | 2006 |
| Předmět: |
chemistry.chemical_classification
biology Hydrolases Carboxylic Acids Active site Bioengineering General Medicine Applied Microbiology and Biotechnology Catalysis Substrate Specificity Enzyme Activation Serine IR-103695 Enzyme chemistry Biocatalysis Catalytic triad Hydrolase biology.protein Organic chemistry Biotechnology |
| Zdroj: | Journal of biotechnology, 126(2), 140-151. Elsevier |
| ISSN: | 0168-1656 |
| Popis: | The enzymatic promiscuity concept involves the possibility that one active site of an enzyme can catalyse several different chemical transformations. A rational understanding of the mechanistic reasons for this catalytic performance could lead to new practical applications. The capability of certain hydrolases to perform the perhydrolysis was described more than a decade ago, and recently its molecular basis has been elucidated. Remarkably, a similarity between perhydrolases (cofactor-free haloperoxidases) and serine hydrolases was found, with both groups of enzymes sharing a common catalytic triad, which suggests an evolution from a common ancestor. On the other hand, several biotechnological applications derived from the capability of hydrolases to catalyse the synthesis of peracids have been reported: the use of hydrolases as bleaching agents via in situ generation of peracids; (self)-epoxidation of unsaturated fatty acids, olefins, or plant oils, via Prileshajev epoxidation; Baeyer-Villiger reactions. In the present review, the molecular basis for this promiscuous hydrolase capability, as well as identified applications are reviewed and described in detail. |
| Databáze: | OpenAIRE |
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