Pregled bibliografske jedinice broj: 632723
D-amino acid oxidase: molecular and process-related determinants of enzyme stability - Pro-Bio Faraday Poster Prize
D-amino acid oxidase: molecular and process-related determinants of enzyme stability - Pro-Bio Faraday Poster Prize // Biocatalysis: Enzymes, Mechanisms and Bioprocesses - a Biochemical Society Focused Meeting in association with Pro-Bio Faraday Annual Conference 2005
Manchester: Biochemical Society Adavancing Molecular Bioscience, 2005. str. P012-P012 (poster, međunarodna recenzija, sažetak, znanstveni)
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Naslov
D-amino acid oxidase: molecular and process-related determinants of enzyme stability - Pro-Bio Faraday Poster Prize
(D-amino acid oxidase: molecular and process-related determinants of enzyme stability)
Autori
Dib, Iskanadar ; Slavica, Anita ; Nidetzky, Bernd
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
Biocatalysis: Enzymes, Mechanisms and Bioprocesses - a Biochemical Society Focused Meeting in association with Pro-Bio Faraday Annual Conference 2005
/ - Manchester : Biochemical Society Adavancing Molecular Bioscience, 2005, P012-P012
Skup
Biocatalysis: Enzymes, Mechanisms and Bioprocesses - a Biochemical Society Focused Meeting in association with Pro-Bio Faraday Annual Conference 2005
Mjesto i datum
Manchester, Ujedinjeno Kraljevstvo, 21.11.2005. - 22.11.2005
Vrsta sudjelovanja
Poster
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
D-amino acid oxidase; enzyme inactivation
Sažetak
An outstanding example for the implementation of an oxidizing enzyme in an industrial multi-ton-per-year process is the use of immobilized D-amino acid oxidase from the yeast Trigonopsis variabilis (TvDAO) for the conversion of cephalosporin C. TvDAO is a FAD-dependent enzyme that catalyzes the strictly stereospecific oxidative deamination of α-D-amino acids to the corresponding α-keto acids with the concomitant release of ammonia and H2O2. The enzyme displays absolute enantioselectivity and broad side chain specificity as a combination of properties that is much desired for the chiral synthesis of fine chemicals. Although TvDAO is considered to be a comparably robust O2-dependent biocatalyst, its operational stability is not completely satisfactory from an economical point of view. We have therefore performed a detailed kinetic analysis of the thermal inactivation of TvDAO and - using evidence from experiments and mathematical modeling - we have identified and characterized three major pathways of inactivation. This study on TvDAO stability was complemented by experiments in a miniaturized reactor system under process-near conditions. The identification of molecular and process related determinants of TvDAO stability could provide a mechanistic tool for rational stabilization of this industrially important enzyme for improved process performance.
Izvorni jezik
Engleski
Napomena
Pro-Bio Faraday Poster Prize