Characterization of tyrosine ammonia lyases from Flavobacterium johnsonian and Herpetosiphon aurantiacus.
biocatalysis
bioprocess engineering
modeling
protein stability
Journal
Biotechnology journal
ISSN: 1860-7314
Titre abrégé: Biotechnol J
Pays: Germany
ID NLM: 101265833
Informations de publication
Date de publication:
Nov 2023
Nov 2023
Historique:
revised:
12
06
2023
received:
09
03
2023
accepted:
12
07
2023
medline:
13
11
2023
pubmed:
24
7
2023
entrez:
24
7
2023
Statut:
ppublish
Résumé
p-Coumaric acid (pCA) can be produced via bioprocessing and is a promising chemical precursor to making organic thin film transistors. However, the required tyrosine ammonia lyase (TAL) enzyme generally has a low specific activity and suffers from competitive product inhibition. Here we characterized the purified TAL variants from Flavobacterium johnsoniae and Herpetosiphon aurantiacus in terms of their susceptibility to product inhibition and their activity and stability across pH and temperature via initial rate experiments. FjTAL was found to be more active than previously described and to have a relatively weak affinity for pCA, but modeling revealed that product inhibition would still be problematic at industrially relevant product concentrations, due to the low solubility of the substrate tyrosine. The activity of both variants increased with temperature when tested up to 45°C, but HaTAL1 was more stable at elevated temperature. FjTAL is a promising biocatalyst for pCA production, but enzyme or bioprocess engineering are required to stabilize FjTAL and reduce product inhibition.
Identifiants
pubmed: 37486789
doi: 10.1002/biot.202300111
doi:
Substances chimiques
Ammonia-Lyases
EC 4.3.1.-
p-coumaric acid
IBS9D1EU3J
Tyrosine
42HK56048U
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2300111Subventions
Organisme : Novo Nordisk Foundation
ID : NNF17SA0031362
Informations de copyright
© 2023 The Authors. Biotechnology Journal published by Wiley-VCH GmbH.
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