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Enhancing Soluble Expression and Post-Translational Modification of Mussel Foot Protein in E. coli.

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Τίτλος: Enhancing Soluble Expression and Post-Translational Modification of Mussel Foot Protein in E. coli.
Συγγραφείς: Zhang R; School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, P. R. China.; Institute of Future Food Technology, JITRI, Yixing 214200, P. R. China., Xue D; School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, P. R. China.; Wuxi Children's Hospital, Wuxi 214023, P. R. China., Chen JP; School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, P. R. China.; Institute of Future Food Technology, JITRI, Yixing 214200, P. R. China., Su C; School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, P. R. China.; Institute of Future Food Technology, JITRI, Yixing 214200, P. R. China., Li H; School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, P. R. China., Gong JS; School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, P. R. China.; Institute of Future Food Technology, JITRI, Yixing 214200, P. R. China., Xu ZH; National Engineering Research Center for Cereal Fermentation and Food Biomanufacturing, School of Biotechnology, Jiangnan University, Wuxi 214122, P. R. China.; College of Biomass Science and Engineering, Sichuan University, Chengdu 610065, P. R. China.; Institute of Future Food Technology, JITRI, Yixing 214200, P. R. China., Shi JS; School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, P. R. China.; Institute of Future Food Technology, JITRI, Yixing 214200, P. R. China.
Πηγή: Journal of agricultural and food chemistry [J Agric Food Chem] 2026 Jun 17; Vol. 74 (23), pp. 18179-18188. Date of Electronic Publication: 2026 Jun 02.
Τύπος έκδοσης: Journal Article
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: American Chemical Society Country of Publication: United States NLM ID: 0374755 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-5118 (Electronic) Linking ISSN: 00218561 NLM ISO Abbreviation: J Agric Food Chem Subsets: MEDLINE
Imprint Name(s): Original Publication: Washington, American Chemical Society.
Ιατρικοί όροι (MeSH): Escherichia coli*/genetics , Escherichia coli*/metabolism , Proteins*/genetics , Proteins*/chemistry , Proteins*/metabolism , Bivalvia*/genetics , Bivalvia*/metabolism , Bivalvia*/chemistry, Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Monophenol Monooxygenase/metabolism ; Monophenol Monooxygenase/genetics ; Animals ; Solubility ; Protein Processing, Post-Translational ; Gene Expression
Περίληψη: Due to intrinsically low solubility and stability, recombinant mussel foot proteins (Mfps) require an efficient system that supports large-scale production of dopanized-Mfps. Here, we engineered a 39-aa peptide tag, termed T7B9M3, to increase the solubility of Mfps in Escherichia coli. The absence of net charged residues, rather than the copy number or the predicted α-helical structure of the T7B9M3 tag, contributes to the solubility enhancement. T7B9M3-fp-3B achieved a 365.96 mg/L soluble protein titer with a 98.75% soluble rate in a shake flask. Coupling the tyrosinase coexpression to endow Mfps with a dopaminization capability, the tyrosine hydroxylation efficiency reached 19.82%. Moreover, dopanized-Mfps tended to form stronger interactions with various substrates, including glass, polypropylene, and polyethylene, than the unmodified version. Our findings suggest that the combined strategy may contribute to establishing a scalable and low-cost protein expression platform with the potential for batch production of functional Mfps.
Contributed Indexing: Keywords: adhesion performance; mussel foot protein; recombinant fp-3B; soluble expression; tyrosinase
Substance Nomenclature: 0 (Recombinant Proteins)
EC 1.14.18.1 (Monophenol Monooxygenase)
0 (Proteins)
Entry Date(s): Date Created: 20260602 Date Completed: 20260617 Latest Revision: 20260617
Update Code: 20260617
DOI: 10.1021/acs.jafc.6c03491
PMID: 42227823
Βάση Δεδομένων: MEDLINE
FullText Text:
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Header DbId: cmedm
DbLabel: MEDLINE
An: 42227823
AccessLevel: 3
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Enhancing Soluble Expression and Post-Translational Modification of Mussel Foot Protein in E. coli.
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  Label: Authors
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  Data: <searchLink fieldCode="AU" term="%22Zhang+R%22">Zhang R</searchLink>; School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, P. R. China.; Institute of Future Food Technology, JITRI, Yixing 214200, P. R. China.<br /><searchLink fieldCode="AU" term="%22Xue+D%22">Xue D</searchLink>; School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, P. R. China.; Wuxi Children's Hospital, Wuxi 214023, P. R. China.<br /><searchLink fieldCode="AU" term="%22Chen+JP%22">Chen JP</searchLink>; School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, P. R. China.; Institute of Future Food Technology, JITRI, Yixing 214200, P. R. China.<br /><searchLink fieldCode="AU" term="%22Su+C%22">Su C</searchLink>; School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, P. R. China.; Institute of Future Food Technology, JITRI, Yixing 214200, P. R. China.<br /><searchLink fieldCode="AU" term="%22Li+H%22">Li H</searchLink>; School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, P. R. China.<br /><searchLink fieldCode="AU" term="%22Gong+JS%22">Gong JS</searchLink>; School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, P. R. China.; Institute of Future Food Technology, JITRI, Yixing 214200, P. R. China.<br /><searchLink fieldCode="AU" term="%22Xu+ZH%22">Xu ZH</searchLink>; National Engineering Research Center for Cereal Fermentation and Food Biomanufacturing, School of Biotechnology, Jiangnan University, Wuxi 214122, P. R. China.; College of Biomass Science and Engineering, Sichuan University, Chengdu 610065, P. R. China.; Institute of Future Food Technology, JITRI, Yixing 214200, P. R. China.<br /><searchLink fieldCode="AU" term="%22Shi+JS%22">Shi JS</searchLink>; School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, P. R. China.; Institute of Future Food Technology, JITRI, Yixing 214200, P. R. China.
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  Data: <searchLink fieldCode="JN" term="%220374755%22">Journal of agricultural and food chemistry</searchLink> [J Agric Food Chem] 2026 Jun 17; Vol. 74 (23), pp. 18179-18188. <i>Date of Electronic Publication: </i>2026 Jun 02.
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  Data: Journal Article
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  Data: English
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  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22American+Chemical+Society%22">American Chemical Society </searchLink><i>Country of Publication: </i>United States <i>NLM ID: </i>0374755 <i>Publication Model: </i>Print-Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>1520-5118 (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2200218561%22">00218561 </searchLink><i>NLM ISO Abbreviation: </i>J Agric Food Chem <i>Subsets: </i>MEDLINE
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  Data: <i>Original Publication</i>: Washington, American Chemical Society.
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  Data: <searchLink fieldCode="MM" term="%22Escherichia+coli%22">Escherichia coli*</searchLink>/<searchLink fieldCode="MM" term="%22Escherichia+coli+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Escherichia+coli%22">Escherichia coli*</searchLink>/<searchLink fieldCode="MM" term="%22Escherichia+coli+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Proteins%22">Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Proteins+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Proteins%22">Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Proteins+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Proteins%22">Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Proteins+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Bivalvia%22">Bivalvia*</searchLink>/<searchLink fieldCode="MM" term="%22Bivalvia+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Bivalvia%22">Bivalvia*</searchLink>/<searchLink fieldCode="MM" term="%22Bivalvia+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Bivalvia%22">Bivalvia*</searchLink>/<searchLink fieldCode="MM" term="%22Bivalvia+chemistry%22">chemistry</searchLink><br /><searchLink fieldCode="MH" term="%22Recombinant+Proteins%22">Recombinant Proteins</searchLink>/<searchLink fieldCode="MH" term="%22Recombinant+Proteins+chemistry%22">chemistry</searchLink> ; <searchLink fieldCode="MH" term="%22Recombinant+Proteins%22">Recombinant Proteins</searchLink>/<searchLink fieldCode="MH" term="%22Recombinant+Proteins+genetics%22">genetics</searchLink> ; <searchLink fieldCode="MH" term="%22Recombinant+Proteins%22">Recombinant Proteins</searchLink>/<searchLink fieldCode="MH" term="%22Recombinant+Proteins+metabolism%22">metabolism</searchLink> ; <searchLink fieldCode="MH" term="%22Monophenol+Monooxygenase%22">Monophenol Monooxygenase</searchLink>/<searchLink fieldCode="MH" term="%22Monophenol+Monooxygenase+metabolism%22">metabolism</searchLink> ; <searchLink fieldCode="MH" term="%22Monophenol+Monooxygenase%22">Monophenol Monooxygenase</searchLink>/<searchLink fieldCode="MH" term="%22Monophenol+Monooxygenase+genetics%22">genetics</searchLink> ; <searchLink fieldCode="MH" term="%22Animals%22">Animals</searchLink> ; <searchLink fieldCode="MH" term="%22Solubility%22">Solubility</searchLink> ; <searchLink fieldCode="MH" term="%22Protein+Processing%2C+Post-Translational%22">Protein Processing, Post-Translational</searchLink> ; <searchLink fieldCode="MH" term="%22Gene+Expression%22">Gene Expression</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Due to intrinsically low solubility and stability, recombinant mussel foot proteins (Mfps) require an efficient system that supports large-scale production of dopanized-Mfps. Here, we engineered a 39-aa peptide tag, termed T7B9M3, to increase the solubility of Mfps in Escherichia coli. The absence of net charged residues, rather than the copy number or the predicted α-helical structure of the T7B9M3 tag, contributes to the solubility enhancement. T7B9M3-fp-3B achieved a 365.96 mg/L soluble protein titer with a 98.75% soluble rate in a shake flask. Coupling the tyrosinase coexpression to endow Mfps with a dopaminization capability, the tyrosine hydroxylation efficiency reached 19.82%. Moreover, dopanized-Mfps tended to form stronger interactions with various substrates, including glass, polypropylene, and polyethylene, than the unmodified version. Our findings suggest that the combined strategy may contribute to establishing a scalable and low-cost protein expression platform with the potential for batch production of functional Mfps.
– Name: SubjectMinor
  Label: Contributed Indexing
  Group:
  Data: <i>Keywords: </i>adhesion performance; mussel foot protein; recombinant fp-3B; soluble expression; tyrosinase
– Name: NumberCAS
  Label: Substance Nomenclature
  Group: ID
  Data: 0 (Recombinant Proteins)<br />EC 1.14.18.1 (Monophenol Monooxygenase)<br />0 (Proteins)
– Name: DateEntry
  Label: Entry Date(s)
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  Data: <i>Date Created: </i>20260602 <i>Date Completed: </i>20260617 <i>Latest Revision: </i>20260617
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  Data: 20260617
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  Data: 10.1021/acs.jafc.6c03491
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  Data: 42227823
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=cmedm&AN=42227823
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        Value: 10.1021/acs.jafc.6c03491
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      – Code: eng
        Text: English
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        StartPage: 18179
    Subjects:
      – SubjectFull: Recombinant Proteins chemistry
        Type: general
      – SubjectFull: Recombinant Proteins genetics
        Type: general
      – SubjectFull: Recombinant Proteins metabolism
        Type: general
      – SubjectFull: Monophenol Monooxygenase metabolism
        Type: general
      – SubjectFull: Monophenol Monooxygenase genetics
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      – SubjectFull: Animals
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      – SubjectFull: Gene Expression
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      – SubjectFull: Escherichia coli genetics
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      – SubjectFull: Escherichia coli metabolism
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      – SubjectFull: Proteins genetics
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      – SubjectFull: Proteins metabolism
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      – SubjectFull: Bivalvia metabolism
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      – TitleFull: Enhancing Soluble Expression and Post-Translational Modification of Mussel Foot Protein in E. coli.
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              Text: 2026 Jun 17
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