Web of Science: 3 cites, Scopus: 3 cites, Google Scholar: cites
Chloroperoxidase-catalyzed aminoalcohol oxidation : substrate specificity and novel strategy for the synthesis of N-Cbz-3-aminopropanal
Masdeu, Gerard (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental)
Pérez Trujillo, Míriam (Universitat Autònoma de Barcelona. Servei de Ressonància Magnètica Nuclear)
López Santín, Josep (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental)
Álvaro Campos, Gregorio (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental)

Data: 2016
Resum: The ability of chloroperoxidase (CPO) to catalyze amino alcohol oxidations was investigated. The oxidations of compounds with different configurations with respect to the amine position towards hydroxyl – using H₂O₂ and tert-butyl hydroperoxide (t-BuOOH) – were analyzed in terms of the initial reaction rate, substrate conversion, and CPO operational stability. It was observed that the further the amino group from the hydroxyl, the lower the initial reaction rate. The effect of the amino-protecting group and other substituents (i. e. , methyl and hydroxyl) was also examined, revealing an increase in steric hindrance due to the effect of bulky substituents. The observed reaction rates were higher with t-BuOOH, whereas CPO was more stable with H₂O₂. Moreover, CPO stability had to be determined case by case as the enzyme activity was modulated by the substrate. The oxidation of N-Cbz-3-aminopropanol (Cbz, carboxybenzyl) to N-Cbz-3-aminopropanal was investigated. Main operational conditions such as the reaction medium, initial amino alcohol concentration, and peroxide nature were studied. The reaction kinetics was determined, and no substrate inhibition was observed. By-products from a chemical reaction between the formed amino aldehyde and the peroxide were identified, and a novel reaction mechanism was proposed. Finally, the biotransformation was achieved by reducing side reactions and identifying the key factors to be addressed to further optimize the product yield.
Nota: Número d'acord de subvenció MINECO/CTQ2014-53114R
Nota: Número d'acord de subvenció AGAUR/2014/SGR-452
Drets: Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial i la comunicació pública de l'obra, sempre que no sigui amb finalitats comercials, i sempre que es reconegui l'autoria de l'obra original. No es permet la creació d'obres derivades. Creative Commons
Llengua: Anglès.
Document: article ; recerca ; acceptedVersion
Matèria: Chloroperoxidase (CPO) ; Amino alcohol oxidation ; Substrate specificity for chloroperoxidase ; N-Cbz-3-aminopropanal synthesis ; Aldehyde–peroxide reaction ; D-Fagomine precursor
Publicat a: Process biochemistry, Vol. 51, issue 9 (Sep. 2016) , p. 1204–1211, ISSN 1359-5113

DOI: 10.1016/j.procbio.2016.05.022


Post-print
25 p, 1.6 MB

El registre apareix a les col·leccions:
Articles > Articles de recerca
Articles > Articles publicats

 Registre creat el 2016-10-28, darrera modificació el 2018-10-27



   Favorit i Compartir