Bacteriocin release protein mediated secretory expression of recombinant chalcone synthase in Escherichia coli

Flavonoids are secondary metabolites synthesized by plants shown to exhibit health benefits such as anti-inflammatory, antioxidant, and anti-tumor effects. Thus, due to the importance of this compound, several enzymes involved in the flavonoid pathway have been cloned and characterized in Escherichi...

Full description

Bibliographic Details
Main Authors: Zakaria, Iffah Izzati, Raja Abdul Rahman, Raja Noor Zaliha, Salleh, Abu Bakar, Basri, Mahiran
Format: Article
Language:English
Published: Springer 2011
Online Access:http://psasir.upm.edu.my/id/eprint/22324/1/Bacteriocin%20release%20protein%20mediated%20secretory%20expression%20of%20recombinant%20chalcone%20synthase%20in%20Escherichia%20coli.pdf
_version_ 1796970138968260608
author Zakaria, Iffah Izzati
Raja Abdul Rahman, Raja Noor Zaliha
Salleh, Abu Bakar
Basri, Mahiran
author_facet Zakaria, Iffah Izzati
Raja Abdul Rahman, Raja Noor Zaliha
Salleh, Abu Bakar
Basri, Mahiran
author_sort Zakaria, Iffah Izzati
collection UPM
description Flavonoids are secondary metabolites synthesized by plants shown to exhibit health benefits such as anti-inflammatory, antioxidant, and anti-tumor effects. Thus, due to the importance of this compound, several enzymes involved in the flavonoid pathway have been cloned and characterized in Escherichia coli. However, the formation of inclusion bodies has become a major disadvantage of this approach. As an alternative, chalcone synthase from Physcomitrella patens was secreted into the medium using a bacteriocin release protein expression vector. Secretion of P. patens chalcone synthase into the culture media was achieved by co-expression with a psW1 plasmid encoding bacteriocin release protein in E. coli Tuner (DE3) plysS. The optimized conditions, which include the incubation of cells for 20 h with 40 ng/ml mitomycin C at OD600 induction time of 0.5 was found to be the best condition for chalcone synthase secretion.
first_indexed 2024-03-06T07:53:37Z
format Article
id upm.eprints-22324
institution Universiti Putra Malaysia
language English
last_indexed 2024-03-06T07:53:37Z
publishDate 2011
publisher Springer
record_format dspace
spelling upm.eprints-223242016-09-26T07:09:14Z http://psasir.upm.edu.my/id/eprint/22324/ Bacteriocin release protein mediated secretory expression of recombinant chalcone synthase in Escherichia coli Zakaria, Iffah Izzati Raja Abdul Rahman, Raja Noor Zaliha Salleh, Abu Bakar Basri, Mahiran Flavonoids are secondary metabolites synthesized by plants shown to exhibit health benefits such as anti-inflammatory, antioxidant, and anti-tumor effects. Thus, due to the importance of this compound, several enzymes involved in the flavonoid pathway have been cloned and characterized in Escherichia coli. However, the formation of inclusion bodies has become a major disadvantage of this approach. As an alternative, chalcone synthase from Physcomitrella patens was secreted into the medium using a bacteriocin release protein expression vector. Secretion of P. patens chalcone synthase into the culture media was achieved by co-expression with a psW1 plasmid encoding bacteriocin release protein in E. coli Tuner (DE3) plysS. The optimized conditions, which include the incubation of cells for 20 h with 40 ng/ml mitomycin C at OD600 induction time of 0.5 was found to be the best condition for chalcone synthase secretion. Springer 2011 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/22324/1/Bacteriocin%20release%20protein%20mediated%20secretory%20expression%20of%20recombinant%20chalcone%20synthase%20in%20Escherichia%20coli.pdf Zakaria, Iffah Izzati and Raja Abdul Rahman, Raja Noor Zaliha and Salleh, Abu Bakar and Basri, Mahiran (2011) Bacteriocin release protein mediated secretory expression of recombinant chalcone synthase in Escherichia coli. Applied Biochemistry and Biotechnology, 165 (2). pp. 737-747. ISSN 0273-2289; ESSN: 1559-0291 http://link.springer.com/article/10.1007/s12010-011-9292-1?view=classic 10.1007/s12010-011-9292-1
spellingShingle Zakaria, Iffah Izzati
Raja Abdul Rahman, Raja Noor Zaliha
Salleh, Abu Bakar
Basri, Mahiran
Bacteriocin release protein mediated secretory expression of recombinant chalcone synthase in Escherichia coli
title Bacteriocin release protein mediated secretory expression of recombinant chalcone synthase in Escherichia coli
title_full Bacteriocin release protein mediated secretory expression of recombinant chalcone synthase in Escherichia coli
title_fullStr Bacteriocin release protein mediated secretory expression of recombinant chalcone synthase in Escherichia coli
title_full_unstemmed Bacteriocin release protein mediated secretory expression of recombinant chalcone synthase in Escherichia coli
title_short Bacteriocin release protein mediated secretory expression of recombinant chalcone synthase in Escherichia coli
title_sort bacteriocin release protein mediated secretory expression of recombinant chalcone synthase in escherichia coli
url http://psasir.upm.edu.my/id/eprint/22324/1/Bacteriocin%20release%20protein%20mediated%20secretory%20expression%20of%20recombinant%20chalcone%20synthase%20in%20Escherichia%20coli.pdf
work_keys_str_mv AT zakariaiffahizzati bacteriocinreleaseproteinmediatedsecretoryexpressionofrecombinantchalconesynthaseinescherichiacoli
AT rajaabdulrahmanrajanoorzaliha bacteriocinreleaseproteinmediatedsecretoryexpressionofrecombinantchalconesynthaseinescherichiacoli
AT sallehabubakar bacteriocinreleaseproteinmediatedsecretoryexpressionofrecombinantchalconesynthaseinescherichiacoli
AT basrimahiran bacteriocinreleaseproteinmediatedsecretoryexpressionofrecombinantchalconesynthaseinescherichiacoli