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Unnatural Amino Acids pp 37–54Cite as

Enzymatic Production of Enantiopure Amino Acids from Mono-substituted Hydantoin Substrates

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Part of the book series: Methods in Molecular Biology ((MIMB,volume 794))

Abstract

Biocatalytic conversion of 5-substituted hydantoin derivatives is an efficient method for the production of unnatural enantiomerically pure amino acids. The enzymes required to carry out this hydrolysis occur in a wide variety of eubacterial species each of which exhibit variations in substrate selectivity, enantiospecificity, and catalytic efficiency. Screening of the natural environment for bacterial strains capable of utilizing hydantoin as a nutrient source (as opposed to rational protein design of known enzymes) is a cost-effective and valuable approach for isolating microbial species with novel hydantoin-hydrolysing enzyme systems. Once candidate microbial isolates have been identified, characterization and optimization of the activity of target enzyme systems can be achieved by subjecting the hydantoin-hydrolysing system to physicochemical manipulations aimed at the enzymes activity within the natural host cells, expressed in a heterologous host, or as purified enzymes. The latter two options require knowledge of the genes encoding for the hydantoin-hydrolysing enzymes. This chapter describes the methods that can be used in conducting such development of hydantoinase-based biocatalytic routes for production of target amino acids.

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Author information

Authors and Affiliations

  1. Department of Biochemistry, Microbiology and Biotechnology, Rhodes University, Grahanstown, South Africa

    Gwynneth F. Matcher & Rosemary A. Dorrington

  2. Cape Peninsula University of Technology, Bellville, South Africa

    Stephanie G. Burton

  3. Research and Postgraduate Studies, University of Pretoria, Pretoria, South Africa

    Stephanie G. Burton

Authors
  1. Gwynneth F. Matcher
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  2. Rosemary A. Dorrington
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  3. Stephanie G. Burton
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Corresponding author

Correspondence to Stephanie G. Burton .

Editor information

Editors and Affiliations

  1. Dipto. Biotecnologie e di Scienze Mol, Molecolari (DBSM), Università degli Studi dell'Insubria, Via J.H. Dunant 3, Varese, 21100, Italy

    Loredano Pollegioni

  2. Dipto. Chimica, Politecnico di Milano, Via Mancinelli 7, Milano, 20131, Italy

    Stefano Servi

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Matcher, G.F., Dorrington, R.A., Burton, S.G. (2012). Enzymatic Production of Enantiopure Amino Acids from Mono-substituted Hydantoin Substrates. In: Pollegioni, L., Servi, S. (eds) Unnatural Amino Acids. Methods in Molecular Biology, vol 794. Humana Press. https://doi.org/10.1007/978-1-61779-331-8_3

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  • DOI: https://doi.org/10.1007/978-1-61779-331-8_3

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  • Publisher Name: Humana Press

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