Hydrolase-catalysed synthesis of peroxycarboxylic acids: Biocatalytic promiscuity for practical applications

Chiara Carboni-Oerlemans, Pablo Dominguez de Maria, Bernard Tuin, Gerrald Bargeman, Ab van der Meer, Robert van Gemert

Research output: Contribution to journalArticleAcademic

77 Citations (Scopus)

Abstract

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.
Original languageUndefined
Pages (from-to)140-151
JournalJournal of biotechnology
Volume126
Issue number2
DOIs
Publication statusPublished - 2006

Keywords

  • IR-103695

Cite this

Carboni-Oerlemans, C., Dominguez de Maria, P., Tuin, B., Bargeman, G., van der Meer, A., & van Gemert, R. (2006). Hydrolase-catalysed synthesis of peroxycarboxylic acids: Biocatalytic promiscuity for practical applications. Journal of biotechnology, 126(2), 140-151. https://doi.org/10.1016/j.jbiotec.2006.04.008
Carboni-Oerlemans, Chiara ; Dominguez de Maria, Pablo ; Tuin, Bernard ; Bargeman, Gerrald ; van der Meer, Ab ; van Gemert, Robert. / Hydrolase-catalysed synthesis of peroxycarboxylic acids: Biocatalytic promiscuity for practical applications. In: Journal of biotechnology. 2006 ; Vol. 126, No. 2. pp. 140-151.
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abstract = "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.",
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Carboni-Oerlemans, C, Dominguez de Maria, P, Tuin, B, Bargeman, G, van der Meer, A & van Gemert, R 2006, 'Hydrolase-catalysed synthesis of peroxycarboxylic acids: Biocatalytic promiscuity for practical applications' Journal of biotechnology, vol. 126, no. 2, pp. 140-151. https://doi.org/10.1016/j.jbiotec.2006.04.008

Hydrolase-catalysed synthesis of peroxycarboxylic acids: Biocatalytic promiscuity for practical applications. / Carboni-Oerlemans, Chiara; Dominguez de Maria, Pablo; Tuin, Bernard; Bargeman, Gerrald; van der Meer, Ab; van Gemert, Robert.

In: Journal of biotechnology, Vol. 126, No. 2, 2006, p. 140-151.

Research output: Contribution to journalArticleAcademic

TY - JOUR

T1 - Hydrolase-catalysed synthesis of peroxycarboxylic acids: Biocatalytic promiscuity for practical applications

AU - Carboni-Oerlemans, Chiara

AU - Dominguez de Maria, Pablo

AU - Tuin, Bernard

AU - Bargeman, Gerrald

AU - van der Meer, Ab

AU - van Gemert, Robert

PY - 2006

Y1 - 2006

N2 - 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.

AB - 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.

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JO - Journal of biotechnology

JF - Journal of biotechnology

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Carboni-Oerlemans C, Dominguez de Maria P, Tuin B, Bargeman G, van der Meer A, van Gemert R. Hydrolase-catalysed synthesis of peroxycarboxylic acids: Biocatalytic promiscuity for practical applications. Journal of biotechnology. 2006;126(2):140-151. https://doi.org/10.1016/j.jbiotec.2006.04.008