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Highly secretory ex...
Highly secretory expression of recombinant cowpea chlorotic mottle virus capsid proteins in Pichia pastoris and in-vitro encapsulation of ruthenium nanoparticles for catalysis
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- Zhu, Jie (författare)
- Changzhou Univ, Natl Local Joint Engn Res Ctr Biomass Refining &, Changzhou 213164, Peoples R China
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- Yang, Kun (författare)
- Changzhou Univ, Natl Local Joint Engn Res Ctr Biomass Refining &, Changzhou 213164, Peoples R China
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- Liu, Aijie (författare)
- Uppsala universitet,Fysikalisk kemi,Univ Twente, MESA Inst Nanotechnol, Dept Biomol Nanotechnol, NL-7500 AE Enschede, Netherlands
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- Lu, Xiaoxue (författare)
- Changzhou Univ, Natl Local Joint Engn Res Ctr Biomass Refining &, Changzhou 213164, Peoples R China
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- Yang, Linsong (författare)
- Changzhou Univ, Natl Local Joint Engn Res Ctr Biomass Refining &, Changzhou 213164, Peoples R China
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- Zhao, Qinghuan (författare)
- Changzhou Univ, Natl Local Joint Engn Res Ctr Biomass Refining &, Changzhou 213164, Peoples R China; Suzhou BioTOP Tech Serv Co Ltd, Suzhou Ind Pk, Suzhou 215123, Peoples R China
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(creator_code:org_t)
- Elsevier BV, 2020
- 2020
- Engelska.
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Ingår i: Protein Expression and Purification. - : Elsevier BV. - 1046-5928 .- 1096-0279. ; 174
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- The applications of viral protein cages have expanded rapidly into the fields of bionanotechnology and materials science. However, the low-cost production of viral capsid proteins (CPs) on a large scale is always a challenge. Herein, we develop a highly efficient expression system by constructing recombinant Pichia pastoris cells as a “factory” for the secretion of soluble cowpea chlorotic mottle virus (CCMV) CPs. Under optimal induction conditions (0.9 mg/mL of methanol concentration at 30 °C for 96 h), a high yield of approximately 95 mg/L of CCMV CPs was harvested from the fermentation supernatant with CPs purity >90%, which has significantly simplified the rest of the purification process. The resultant CPs are employed to encapsulate Ruthenium (Ru) nanoparticles (NPs) via in-vitro self-assembly to prepare hybrid nanocatalyst, i.e. Ru@virus-like particles (VLPs). The catalytic activity over Ru@VLPs was evaluated by reducing 4-nitrophenol (4-NP) to 4-aminophenol (4-AP). The results indicate that, with the protection of protein cages, Ru NPs were highly stabilized during the catalytic reaction. This results in enhanced catalytic activity (reaction rate constant k = 0.14 min−1) in comparison with unsupported citrate-stabilized Ru NPs (Ru-CA) (k = 0.08 min−1). Additionally, comparatively lower activation energy over Ru@VLPs (approximately 32 kJ/mol) than that over Ru-CA (approximately 39 kJ/mol) could be attributed to the synergistic effect between Ru NPs and some functional groups such as amino groups (–NH2) on CPs that weakened the activation barrier of 4-NP reduction. Therefore, enhanced activity and decreased activation energy over Ru@VLPs demonstrated the superiority of Ru@VLPs to unsupported Ru-CA.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- Pichiapastoris
- Cowpeachloroticmottlevirus
- Secretion
- Virus-likeparticles
- Hybridnanocatalyst
- 4-Nitrophenolreduction
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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