Improved conditions for production of recombinant plant sesquiterpene synthases in Escherichia coli

Picaud, Sarah; Olsson, Mikael E.; Brodelius, Peter E.

doi:10.1016/j.pep.2006.06.025

Cited by 33Plant biochemistry and biosynthesisPlant tissue culture and regenerationEnzyme Production and Characterization

Improved conditions for production of recombinant plant sesquiterpene synthases in Escherichia coli

Picaud, Sarah, Olsson, Mikael E., Brodelius, Peter E.·2007·Protein Expression and Purification

DOI 10.1016/j.pep.2006.06.025

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Abstract

Amorpha-4,11-diene synthase (ADS) from Artemisia annua and (+)-germacrene synthase (GDS) from Zingiber officinale were expressed in Escherichia coli under different conditions to optimize the yield of active soluble protein. The cDNAs of these enzymes were inserted into the pET28 vector (Novagen) and expressed in four different bacterial strains; BL21 (DE3), BL21 (DE3) Tuner, BL21 (DE3) pLysS and BL21 (DE3) pLysS Tuner using different inducing agents (IPTG, The Inducer). The effects of induction under osmotic stress in the presence of glycine betaine and sorbitol were investigated. Although background expression for ADS was reduced when using pLysS strains, no significant difference was noted for ADS activity in soluble whole cell lysates after induction with either IPTG or The Inducer. For GDS, on the other hand, the change between BL21 (DE3) cells and BL21 (DE3) Tuner, induced with IPTG, leads to a twofold increase in enzyme activity in the soluble fraction while a reduction in activity is observed when using the pLysS strains. The same doubling of activity is observed for GDS when the commonly used BL.21 (DE3) is induced with The Inducer. Addition of 2.5 mM glycine betaine and 660 mM sorbitol to the bacterial growth media resulted in reduction of growth rate and biomass yield but under these conditions the best overall protein production, for both enzymes, was obtained. Compared to the standard conditions previously used in our laboratory the yield of soluble active protein was increased 7- and 2.5-fold for ADS and GDS, using BL21 (DE3) pLysS Tuner and BL21 (DE3), respectively.

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Both Saccharomyces cerevisiae and Escherichia coli have been used as hosts when attempting to establish a viable recombinant microbial pathway for artemisinin biosynthesis.
“Both Saccharomyces cerevisiae [379,380] and Escherichia coli [381,382,383] have been used as hosts when attempting to establish a viable recombinant microbial pathway for the biosynthesis of artemisinin.”
From The Biosynthesis of Artemisinin (Qinghaosu) and the Phytochemistry of Artemisia annua L. (Qinghao) (2010) · cites this paper as [382]
Dodecane has been incorporated into culture medium to provide a separate hydrophobic layer in which volatile amorpha-4,11-diene produced by microbial fermentation can be trapped.
“Previously, dodecane has been incorporated into the culture medium, in order to provide a separate hydrophobic layer in which volatile amorpha-4,11-diene (451) produced by microbial fermentation can be trapped [382, 385].”
From The Biosynthesis of Artemisinin (Qinghaosu) and the Phytochemistry of Artemisia annua L. (Qinghao) (2010) · cites this paper as [382]

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Authors: Picaud, S., Olsson, M. E., & Brodelius, P. E.
Corresponding author: Brodelius, Peter E.
ORCID: Picaud, Sarah
Olsson, Mikael E.
Brodelius, Peter E.
Venue: Protein Expression and Purification
Publisher: Elsevier BV
Published: 2007-01
Volume: 51
Issue: 1
Pages: 71-79
ISSN: 1046-5928 (ISSN-L)
DOI: 10.1016/j.pep.2006.06.025
OpenAlex: W2082144474
Cited by: 33
References: 45
Citations by year: 2026: 1 · 2024: 1 · 2021: 2 · 2020: 2 · 2018: 2 · 2017: 3 · 2016: 1 · 2015: 1 · 2014: 4 · 2013: 5 · 2012: 3
FWCI: 0.54
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Protein Expression and Purification (publishedVersion)
PubMed (publishedVersion)
Funders: Carl Tryggers Stiftelse för Vetenskaplig Forskning
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Plant biochemistry and biosynthesis
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Plant tissue culture and regeneration
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
Keywords: sesquiterpene synthase, recombinant protein expression, Escherichia coli expression, amorpha-4,11-diene synthase, Artemisia annua, ginger, osmotic stress, betaine, sorbitol, IPTG induction, BL21(DE3) pLysS
MeSH terms: Betaine, Enzyme Induction, Escherichia coli, Isopropyl Thiogalactoside, Molecular Biology, Osmotic Pressure, Recombinant Fusion Proteins, Sorbitol, Protein Folding, Alkyl and Aryl Transferases, Zingiber officinale, Artemisia annua

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Improved conditions for production of recombinant plant sesquiterpene synthases in Escherichia coli

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