dc.contributor.author | Tetianec, Lidija | |
dc.contributor.author | Baužienė, Ana | |
dc.contributor.author | Kulys, Juozas | |
dc.contributor.author | Jančienė, Regina | |
dc.contributor.author | Marcinkevičienė, Liucija | |
dc.contributor.author | Meškienė, Rita | |
dc.contributor.author | Stankevičiūtė, Jonita | |
dc.contributor.author | Meškys, Rolandas | |
dc.date.accessioned | 2023-09-18T16:47:04Z | |
dc.date.available | 2023-09-18T16:47:04Z | |
dc.date.issued | 2017 | |
dc.identifier.issn | 1359-5113 | |
dc.identifier.uri | https://etalpykla.vilniustech.lt/handle/123456789/116689 | |
dc.description.abstract | N,N'-dimethyl-4,4'-azopyridinium methyl sulfate (MAZP) was characterized as an electron transfer mediator for oxidation reactions catalyzed by NAD+- and pyrroloquinoline quinone (PQQ)-dependent alcohol dehydrogenases. The bimolecular rate constant of NADH reactivity with MAZP was defined as (2.2 ± 0.1) × 105 M−1 s−1, whereas the bimolecular rate constant of reactivity of the reduced form of PQQ-dependent alcohol dehydrogenase with MAZP was determined to be (4.7 ± 0.1) × 104 M−1 s−1. The use of MAZP for the regeneration of the cofactors was investigated by applying the electrochemical oxidation of the mediator. The total turnover numbers of mediator MAZP and cofactor NADH for ethanol oxidation catalyzed by NAD+-dependent alcohol dehydrogenase depended on the concentration of the substrate and the duration of the electrolysis, and the yield of the reaction was limited by the enzyme inactivation and the electrochemical process. The PQQ-dependent alcohol dehydrogenase was more stable, and the turnover number of the enzyme reached a value of 2.3 × 103. In addition, oxidation of 1,2-propanediol catalyzed by the PQQ-dependent alcohol dehydrogenase proceeded enantioselectively to yield l-lactic acid. | eng |
dc.format | PDF | |
dc.format.extent | p. 41-48 | |
dc.format.medium | tekstas / txt | |
dc.language.iso | eng | |
dc.relation.isreferencedby | SciSearch | |
dc.relation.isreferencedby | Scopus | |
dc.relation.isreferencedby | Science Citation Index | |
dc.relation.isreferencedby | Science Citation Index Expanded (Web of Science) | |
dc.source.uri | http://doi.org/10.1016/j.procbio.2017.01.006 | |
dc.source.uri | https://talpykla.elaba.lt/elaba-fedora/objects/elaba:21284150/datastreams/ATTACHMENT_25365736/content | |
dc.subject | FM01 - Biokatalitinių procesų modeliavimas / Modelling of biocatalytic processes | |
dc.title | Characterization of methylated azopyridine as a potential electron transfer mediator for electroenzymatic systems | |
dc.type | Straipsnis Web of Science DB / Article in Web of Science DB | |
dcterms.references | 53 | |
dc.type.pubtype | S1 - Straipsnis Web of Science DB / Web of Science DB article | |
dc.contributor.institution | Vilniaus Gedimino technikos universitetas Vilniaus universitetas | |
dc.contributor.institution | Vilniaus universitetas | |
dc.contributor.faculty | Fundamentinių mokslų fakultetas / Faculty of Fundamental Sciences | |
dc.subject.researchfield | N 004 - Biochemija / Biochemistry | |
dc.subject.ltspecializations | L105 - Sveikatos technologijos ir biotechnologijos / Health technologies and biotechnologies | |
dc.subject.en | Methylated azopyridine | |
dc.subject.en | Quinoprotein | |
dc.subject.en | Alcohol dehydrogenase | |
dc.subject.en | NADH | |
dc.subject.en | Cofactor regeneration | |
dc.subject.en | Enantioselective conversion | |
dcterms.sourcetitle | Process biochemistry | |
dc.description.volume | Vol. 54 | |
dc.publisher.name | Elsevier | |
dc.publisher.city | Oxford | |
dc.identifier.doi | 000397832800006 | |
dc.identifier.doi | 2-s2.0-85009830143 | |
dc.identifier.doi | 10.1016/j.procbio.2017.01.006 | |
dc.identifier.elaba | 21284150 | |