Optimization of factors influencing enzyme activity and product selectivity and the role of proton transfer in the catalytic mechanism of patchoulol synthase.
biocatalysis
biocatalytic mechanism
patchouli oil
patchoulol synthase
sesquiterpenes
Journal
Biotechnology progress
ISSN: 1520-6033
Titre abrégé: Biotechnol Prog
Pays: United States
ID NLM: 8506292
Informations de publication
Date de publication:
03 2020
03 2020
Historique:
received:
27
08
2019
revised:
07
10
2019
accepted:
17
10
2019
pubmed:
24
10
2019
medline:
8
6
2021
entrez:
24
10
2019
Statut:
ppublish
Résumé
The patchoulol synthase (PTS) from Pogostemon cablin is a versatile sesquiterpene synthase and produces more than 20 valuable sesquiterpenes by conversion of the natural substrate farnesyl pyrophosphate (FPP). PTS has the potential to be used as a biocatalyst for the production of valuable sesquiterpenes such as (-)-patchoulol. The objective of the present study is to develop an efficient biotransformation and to characterize the biocatalytic mechanism of the PTS in detail. For this purpose, soluble PTS was prepared using an optimized cultivation protocol and continuous downstream process with a purity of 98%. The PTS biotransformation was then optimized regarding buffer composition, pH-value, and temperature for biotransformation as well as functional and kinetic properties to improve productivity. For the bioconversion of FPP, the highest enzyme activity was reached with the 2-(N-morphlino)ethanesulfonic acid (MES) buffer containing 10% (v/v) glycerol and 10 mM MgCl
Substances chimiques
Polyisoprenyl Phosphates
0
Protons
0
Sesquiterpenes
0
farnesyl pyrophosphate
79W6B01D07
Isomerases
EC 5.-
patchoulol synthase
EC 5.-
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2935Informations de copyright
© 2019 The Authors. Biotechnology Progress published by Wiley Periodicals, Inc. on behalf of American Institute of Chemical Engineers.
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