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Transglycosylation Capabilities of Wild-Type α-l-Fucosidase iso1 from Paenibacillus thiaminolyticus and Its Engineered Mutants: Preparation of Fucosylated Oligosaccharides.

Λεπτομέρειες βιβλιογραφικής εγγραφής
Τίτλος: Transglycosylation Capabilities of Wild-Type α-l-Fucosidase iso1 from Paenibacillus thiaminolyticus and Its Engineered Mutants: Preparation of Fucosylated Oligosaccharides.
Συγγραφείς: Vodičková P; Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic., Klimešová L; Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic.; Institute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic., Nekvasilová P; Institute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic.; Department of Genetics and Microbiology, Faculty of Science, Charles University, Prague, Czech Republic., Petrásková L; Institute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic., Pelantová H; Institute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic., Kovaľová T; Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic., Lipovová P; Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic., Bojarová P; Institute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic., Benešová E; Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic.
Πηγή: Microbial biotechnology [Microb Biotechnol] 2026 Apr; Vol. 19 (4), pp. e70354.
Τύπος έκδοσης: Journal Article
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: Wiley-Blackwell Country of Publication: United States NLM ID: 101316335 Publication Model: Print Cited Medium: Internet ISSN: 1751-7915 (Electronic) Linking ISSN: 17517915 NLM ISO Abbreviation: Microb Biotechnol Subsets: MEDLINE
Imprint Name(s): Publication: Hoboken, NJ : Wiley-Blackwell
Original Publication: Oxford : Blackwell, c2008-
Ιατρικοί όροι (MeSH): Paenibacillus*/enzymology , Paenibacillus*/genetics , alpha-L-Fucosidase*/genetics , alpha-L-Fucosidase*/metabolism , alpha-L-Fucosidase*/chemistry , Fucose*/metabolism , Oligosaccharides*/metabolism , Oligosaccharides*/chemistry, Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Mutant Proteins/metabolism ; Mutant Proteins/genetics ; Mutagenesis, Site-Directed ; Glycosylation
Περίληψη: To enhance the yield of l-fucosylated molecules synthesized via transfucosylation, we employed α-l-transfucosidases, enzymes engineered from α-l-fucosidases to favour transglycosylation over hydrolysis. This study investigated the transglycosylation potential of mutated variants of α-l-fucosidase iso1 from Paenibacillus thiaminolyticus designed by structural comparison with Thermotoga maritima α-l-transfucosidase. Using site-directed mutagenesis, point mutations (S237A, S237G, S237P, S237V, Y189F) were introduced, and the corresponding recombinant proteins were successfully expressed and purified. Among them, the S237V variant achieved the highest overall yield of fucosylated lactose and increased the transglycosylation/hydrolysis ratio more than 20-fold compared to the wild-type enzyme. This variant enabled regioselective synthesis of 3'-and 6'-fucosyllactose, as well as a functionalized 3'-fucosyllactose bearing a Boc-protected ethylthioureidyl linker (3'-FucLac-tBoc), with all structures confirmed by NMR spectroscopy. The engineered α-l-transfucosidase iso1 from Paenibacillus thiaminolyticus catalysed the regioselective synthesis of structurally defined fucosyllactose derivatives, including C-1 functionalized analogs suitable for immobilization on biosensor surfaces or macromolecular scaffolds, thus expanding the biocatalytic toolbox and demonstrating the potential of semi-rational enzyme design for targeted HMO-based glycoengineering applications.
(© 2026 The Author(s). Microbial Biotechnology published by John Wiley & Sons Ltd.)
References: Molecules. 2023 May 11;28(10):. (PMID: 37241779)
Glycobiology. 2003 Jul;13(7):41R-53R. (PMID: 12651883)
Nat Commun. 2020 Dec 4;11(1):6204. (PMID: 33277506)
J Microbiol Methods. 2014 Nov;106:67-71. (PMID: 25149690)
Glycobiology. 2023 Jun 3;33(5):396-410. (PMID: 37014745)
Curr Opin Chem Biol. 2009 Dec;13(5-6):592-600. (PMID: 19766528)
Appl Environ Microbiol. 2013 Jun;79(12):3847-50. (PMID: 23542622)
Extremophiles. 2021 May;25(3):311-317. (PMID: 33938983)
J Biol Chem. 2004 Mar 26;279(13):13119-28. (PMID: 14715651)
Biomolecules. 2012 Jan 30;2(1):34-45. (PMID: 24970126)
Curr Opin Chem Biol. 2006 Oct;10(5):509-19. (PMID: 16905354)
Appl Microbiol Biotechnol. 2024 May 21;108(1):338. (PMID: 38771321)
Food Chem (Oxf). 2025 Feb 11;10:100244. (PMID: 40034538)
PLoS One. 2016 Jan 22;11(1):e0147438. (PMID: 26800369)
Biochemistry. 2004 Jun 22;43(24):7881-91. (PMID: 15196032)
FEBS Lett. 2008 Nov 12;582(27):3739-43. (PMID: 18845150)
Curr Opin Struct Biol. 1997 Oct;7(5):652-60. (PMID: 9345623)
Trends Biotechnol. 2009 Apr;27(4):199-209. (PMID: 19250692)
Glycobiology. 2016 Mar;26(3):261-9. (PMID: 26582607)
Carbohydr Res. 2004 Dec 27;339(18):2851-7. (PMID: 15582611)
Extremophiles. 2018 Nov;22(6):889-894. (PMID: 30088105)
Carbohydr Res. 2019 Apr 1;476:71-77. (PMID: 30921739)
Food Chem. 2022 Feb 1;369:130942. (PMID: 34479010)
Appl Biochem Biotechnol. 2018 Nov;186(3):681-691. (PMID: 29717409)
Sci Rep. 2022 Jun 27;12(1):10846. (PMID: 35760821)
Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501. (PMID: 20383002)
Appl Microbiol Biotechnol. 2020 Jul;104(13):5619-5631. (PMID: 32356197)
Molecules. 2019 Feb 08;24(3):. (PMID: 30743988)
Glycobiology. 2019 Jan 1;29(1):59-73. (PMID: 30544181)
J Fungi (Basel). 2020 Nov 18;6(4):. (PMID: 33217923)
Molecules. 2019 Jun 29;24(13):. (PMID: 31261855)
J Am Chem Soc. 2017 Oct 25;139(42):15074-15087. (PMID: 28990779)
Glycobiology. 2013 Sep;23(9):1052-65. (PMID: 23723440)
Food Res Int. 2025 May;209:116328. (PMID: 40253162)
Appl Microbiol Biotechnol. 2015 Sep;99(17):7165-76. (PMID: 25977209)
J Nanobiotechnology. 2018 Sep 20;16(1):73. (PMID: 30236114)
J Bacteriol. 2014 Jun;196(11):1941-9. (PMID: 24610710)
Glycobiology. 2006 Dec;16(12):158R-184R. (PMID: 16973733)
Biochemistry. 2007 Jan 30;46(4):1022-33. (PMID: 17240986)
Biochim Biophys Acta. 1999 Dec 6;1473(1):216-36. (PMID: 10580141)
Appl Microbiol Biotechnol. 2020 Jul;104(13):5813-5826. (PMID: 32388762)
BMC Biotechnol. 2015 May 27;15:36. (PMID: 26013545)
Grant Information: LUC24024 Ministerstvo Školství, Mládeže a Tělovýchovy; 25-16301K Grantová Agentura České Republiky
Contributed Indexing: Keywords: Paenibacillus thiaminolyticus; fucosidase; fucosyllactose; human milk oligosaccharide; site‐directed mutagenesis; transglycosidase; transglycosylation
Substance Nomenclature: EC 3.2.1.51 (alpha-L-Fucosidase)
28RYY2IV3F (Fucose)
0 (Oligosaccharides)
0 (Recombinant Proteins)
0 (Mutant Proteins)
Entry Date(s): Date Created: 20260423 Date Completed: 20260715 Latest Revision: 20260813
Update Code: 20260813
PubMed Central ID: PMC13103868
DOI: 10.1111/1751-7915.70354
PMID: 42023498
Βάση Δεδομένων: MEDLINE
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  Label: Title
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  Data: Transglycosylation Capabilities of Wild-Type α-l-Fucosidase iso1 from Paenibacillus thiaminolyticus and Its Engineered Mutants: Preparation of Fucosylated Oligosaccharides.
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  Data: <searchLink fieldCode="AU" term="%22Vodičková+P%22">Vodičková P</searchLink>; Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic.<br /><searchLink fieldCode="AU" term="%22Klimešová+L%22">Klimešová L</searchLink>; Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic.; Institute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic.<br /><searchLink fieldCode="AU" term="%22Nekvasilová+P%22">Nekvasilová P</searchLink>; Institute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic.; Department of Genetics and Microbiology, Faculty of Science, Charles University, Prague, Czech Republic.<br /><searchLink fieldCode="AU" term="%22Petrásková+L%22">Petrásková L</searchLink>; Institute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic.<br /><searchLink fieldCode="AU" term="%22Pelantová+H%22">Pelantová H</searchLink>; Institute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic.<br /><searchLink fieldCode="AU" term="%22Kovaľová+T%22">Kovaľová T</searchLink>; Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic.<br /><searchLink fieldCode="AU" term="%22Lipovová+P%22">Lipovová P</searchLink>; Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic.<br /><searchLink fieldCode="AU" term="%22Bojarová+P%22">Bojarová P</searchLink>; Institute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic.<br /><searchLink fieldCode="AU" term="%22Benešová+E%22">Benešová E</searchLink>; Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic.
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  Data: <searchLink fieldCode="JN" term="%22101316335%22">Microbial biotechnology</searchLink> [Microb Biotechnol] 2026 Apr; Vol. 19 (4), pp. e70354.
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  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Wiley-Blackwell%22">Wiley-Blackwell </searchLink><i>Country of Publication: </i>United States <i>NLM ID: </i>101316335 <i>Publication Model: </i>Print <i>Cited Medium: </i>Internet <i>ISSN: </i>1751-7915 (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2217517915%22">17517915 </searchLink><i>NLM ISO Abbreviation: </i>Microb Biotechnol <i>Subsets: </i>MEDLINE
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– Name: SubjectMESH
  Label: MeSH Terms
  Group: Su
  Data: <searchLink fieldCode="MM" term="%22Paenibacillus%22">Paenibacillus*</searchLink>/<searchLink fieldCode="MM" term="%22Paenibacillus+enzymology%22">enzymology</searchLink> <br /><searchLink fieldCode="MM" term="%22Paenibacillus%22">Paenibacillus*</searchLink>/<searchLink fieldCode="MM" term="%22Paenibacillus+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22alpha-L-Fucosidase%22">alpha-L-Fucosidase*</searchLink>/<searchLink fieldCode="MM" term="%22alpha-L-Fucosidase+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22alpha-L-Fucosidase%22">alpha-L-Fucosidase*</searchLink>/<searchLink fieldCode="MM" term="%22alpha-L-Fucosidase+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22alpha-L-Fucosidase%22">alpha-L-Fucosidase*</searchLink>/<searchLink fieldCode="MM" term="%22alpha-L-Fucosidase+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Fucose%22">Fucose*</searchLink>/<searchLink fieldCode="MM" term="%22Fucose+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Oligosaccharides%22">Oligosaccharides*</searchLink>/<searchLink fieldCode="MM" term="%22Oligosaccharides+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Oligosaccharides%22">Oligosaccharides*</searchLink>/<searchLink fieldCode="MM" term="%22Oligosaccharides+chemistry%22">chemistry</searchLink><br /><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="%22Mutant+Proteins%22">Mutant Proteins</searchLink>/<searchLink fieldCode="MH" term="%22Mutant+Proteins+metabolism%22">metabolism</searchLink> ; <searchLink fieldCode="MH" term="%22Mutant+Proteins%22">Mutant Proteins</searchLink>/<searchLink fieldCode="MH" term="%22Mutant+Proteins+genetics%22">genetics</searchLink> ; <searchLink fieldCode="MH" term="%22Mutagenesis%2C+Site-Directed%22">Mutagenesis, Site-Directed</searchLink> ; <searchLink fieldCode="MH" term="%22Glycosylation%22">Glycosylation</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: To enhance the yield of l-fucosylated molecules synthesized via transfucosylation, we employed α-l-transfucosidases, enzymes engineered from α-l-fucosidases to favour transglycosylation over hydrolysis. This study investigated the transglycosylation potential of mutated variants of α-l-fucosidase iso1 from Paenibacillus thiaminolyticus designed by structural comparison with Thermotoga maritima α-l-transfucosidase. Using site-directed mutagenesis, point mutations (S237A, S237G, S237P, S237V, Y189F) were introduced, and the corresponding recombinant proteins were successfully expressed and purified. Among them, the S237V variant achieved the highest overall yield of fucosylated lactose and increased the transglycosylation/hydrolysis ratio more than 20-fold compared to the wild-type enzyme. This variant enabled regioselective synthesis of 3'-and 6'-fucosyllactose, as well as a functionalized 3'-fucosyllactose bearing a Boc-protected ethylthioureidyl linker (3'-FucLac-tBoc), with all structures confirmed by NMR spectroscopy. The engineered α-l-transfucosidase iso1 from Paenibacillus thiaminolyticus catalysed the regioselective synthesis of structurally defined fucosyllactose derivatives, including C-1 functionalized analogs suitable for immobilization on biosensor surfaces or macromolecular scaffolds, thus expanding the biocatalytic toolbox and demonstrating the potential of semi-rational enzyme design for targeted HMO-based glycoengineering applications.<br /> (© 2026 The Author(s). Microbial Biotechnology published by John Wiley & Sons Ltd.)
– Name: Ref
  Label: References
  Group: RefInfo
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(PMID: <searchLink fieldCode="PM" term="%2233938983%22">33938983)</searchLink><br />J Biol Chem. 2004 Mar 26;279(13):13119-28. (PMID: <searchLink fieldCode="PM" term="%2214715651%22">14715651)</searchLink><br />Biomolecules. 2012 Jan 30;2(1):34-45. (PMID: <searchLink fieldCode="PM" term="%2224970126%22">24970126)</searchLink><br />Curr Opin Chem Biol. 2006 Oct;10(5):509-19. (PMID: <searchLink fieldCode="PM" term="%2216905354%22">16905354)</searchLink><br />Appl Microbiol Biotechnol. 2024 May 21;108(1):338. (PMID: <searchLink fieldCode="PM" term="%2238771321%22">38771321)</searchLink><br />Food Chem (Oxf). 2025 Feb 11;10:100244. (PMID: <searchLink fieldCode="PM" term="%2240034538%22">40034538)</searchLink><br />PLoS One. 2016 Jan 22;11(1):e0147438. (PMID: <searchLink fieldCode="PM" term="%2226800369%22">26800369)</searchLink><br />Biochemistry. 2004 Jun 22;43(24):7881-91. (PMID: <searchLink fieldCode="PM" term="%2215196032%22">15196032)</searchLink><br />FEBS Lett. 2008 Nov 12;582(27):3739-43. (PMID: <searchLink fieldCode="PM" term="%2218845150%22">18845150)</searchLink><br />Curr Opin Struct Biol. 1997 Oct;7(5):652-60. (PMID: <searchLink fieldCode="PM" term="%229345623%22">9345623)</searchLink><br />Trends Biotechnol. 2009 Apr;27(4):199-209. (PMID: <searchLink fieldCode="PM" term="%2219250692%22">19250692)</searchLink><br />Glycobiology. 2016 Mar;26(3):261-9. (PMID: <searchLink fieldCode="PM" term="%2226582607%22">26582607)</searchLink><br />Carbohydr Res. 2004 Dec 27;339(18):2851-7. (PMID: <searchLink fieldCode="PM" term="%2215582611%22">15582611)</searchLink><br />Extremophiles. 2018 Nov;22(6):889-894. (PMID: <searchLink fieldCode="PM" term="%2230088105%22">30088105)</searchLink><br />Carbohydr Res. 2019 Apr 1;476:71-77. (PMID: <searchLink fieldCode="PM" term="%2230921739%22">30921739)</searchLink><br />Food Chem. 2022 Feb 1;369:130942. 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(PMID: <searchLink fieldCode="PM" term="%2233217923%22">33217923)</searchLink><br />Molecules. 2019 Jun 29;24(13):. (PMID: <searchLink fieldCode="PM" term="%2231261855%22">31261855)</searchLink><br />J Am Chem Soc. 2017 Oct 25;139(42):15074-15087. (PMID: <searchLink fieldCode="PM" term="%2228990779%22">28990779)</searchLink><br />Glycobiology. 2013 Sep;23(9):1052-65. (PMID: <searchLink fieldCode="PM" term="%2223723440%22">23723440)</searchLink><br />Food Res Int. 2025 May;209:116328. (PMID: <searchLink fieldCode="PM" term="%2240253162%22">40253162)</searchLink><br />Appl Microbiol Biotechnol. 2015 Sep;99(17):7165-76. (PMID: <searchLink fieldCode="PM" term="%2225977209%22">25977209)</searchLink><br />J Nanobiotechnology. 2018 Sep 20;16(1):73. (PMID: <searchLink fieldCode="PM" term="%2230236114%22">30236114)</searchLink><br />J Bacteriol. 2014 Jun;196(11):1941-9. (PMID: <searchLink fieldCode="PM" term="%2224610710%22">24610710)</searchLink><br />Glycobiology. 2006 Dec;16(12):158R-184R. (PMID: <searchLink fieldCode="PM" term="%2216973733%22">16973733)</searchLink><br />Biochemistry. 2007 Jan 30;46(4):1022-33. (PMID: <searchLink fieldCode="PM" term="%2217240986%22">17240986)</searchLink><br />Biochim Biophys Acta. 1999 Dec 6;1473(1):216-36. (PMID: <searchLink fieldCode="PM" term="%2210580141%22">10580141)</searchLink><br />Appl Microbiol Biotechnol. 2020 Jul;104(13):5813-5826. (PMID: <searchLink fieldCode="PM" term="%2232388762%22">32388762)</searchLink><br />BMC Biotechnol. 2015 May 27;15:36. (PMID: <searchLink fieldCode="PM" term="%2226013545%22">26013545)</searchLink>
– Name: GrantInfo
  Label: Grant Information
  Group: Grant
  Data: LUC24024 Ministerstvo Školství, Mládeže a Tělovýchovy; 25-16301K Grantová Agentura České Republiky
– Name: SubjectMinor
  Label: Contributed Indexing
  Group:
  Data: <i>Keywords: </i>Paenibacillus thiaminolyticus; fucosidase; fucosyllactose; human milk oligosaccharide; site‐directed mutagenesis; transglycosidase; transglycosylation
– Name: NumberCAS
  Label: Substance Nomenclature
  Group: ID
  Data: EC 3.2.1.51 (alpha-L-Fucosidase)<br />28RYY2IV3F (Fucose)<br />0 (Oligosaccharides)<br />0 (Recombinant Proteins)<br />0 (Mutant Proteins)
– Name: DateEntry
  Label: Entry Date(s)
  Group: Date
  Data: <i>Date Created: </i>20260423 <i>Date Completed: </i>20260715 <i>Latest Revision: </i>20260813
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  Label: Update Code
  Group: Date
  Data: 20260813
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  Label: PubMed Central ID
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  Data: PMC13103868
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  Label: DOI
  Group: ID
  Data: 10.1111/1751-7915.70354
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  Label: PMID
  Group: ID
  Data: 42023498
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=cmedm&AN=42023498
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1111/1751-7915.70354
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        StartPage: e70354
    Subjects:
      – SubjectFull: Recombinant Proteins genetics
        Type: general
      – SubjectFull: Recombinant Proteins metabolism
        Type: general
      – SubjectFull: Mutant Proteins metabolism
        Type: general
      – SubjectFull: Mutant Proteins genetics
        Type: general
      – SubjectFull: Mutagenesis, Site-Directed
        Type: general
      – SubjectFull: Glycosylation
        Type: general
      – SubjectFull: Paenibacillus enzymology
        Type: general
      – SubjectFull: Paenibacillus genetics
        Type: general
      – SubjectFull: alpha-L-Fucosidase genetics
        Type: general
      – SubjectFull: alpha-L-Fucosidase metabolism
        Type: general
      – SubjectFull: alpha-L-Fucosidase chemistry
        Type: general
      – SubjectFull: Fucose metabolism
        Type: general
      – SubjectFull: Oligosaccharides metabolism
        Type: general
      – SubjectFull: Oligosaccharides chemistry
        Type: general
    Titles:
      – TitleFull: Transglycosylation Capabilities of Wild-Type α-l-Fucosidase iso1 from Paenibacillus thiaminolyticus and Its Engineered Mutants: Preparation of Fucosylated Oligosaccharides.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Vodičková P
      – PersonEntity:
          Name:
            NameFull: Klimešová L
      – PersonEntity:
          Name:
            NameFull: Nekvasilová P
      – PersonEntity:
          Name:
            NameFull: Petrásková L
      – PersonEntity:
          Name:
            NameFull: Pelantová H
      – PersonEntity:
          Name:
            NameFull: Kovaľová T
      – PersonEntity:
          Name:
            NameFull: Lipovová P
      – PersonEntity:
          Name:
            NameFull: Bojarová P
      – PersonEntity:
          Name:
            NameFull: Benešová E
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 01
              M: 04
              Text: 2026 Apr
              Type: published
              Y: 2026
          Identifiers:
            – Type: issn-electronic
              Value: 1751-7915
          Numbering:
            – Type: volume
              Value: 19
            – Type: issue
              Value: 4
          Titles:
            – TitleFull: Microbial biotechnology
              Type: main
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