Skip to main content

Advertisement

SpringerLink
Log in

Covalent immobilization of xylanase and lysing complex into polymer scaffolds with long-term activity retention

  • Published:
Journal of Coatings Technology and Research Aims and scope Submit manuscript

Abstract

Existing antifouling coatings for marine environments rely on the toxicity of copper and small-molecule additives to prevent organism growth. These come with a myriad of environmental and health-related risks, as these additives inevitably leach into seawater. Enzyme-based antifouling polymers have tremendous potential as part of an environmentally innocuous antifouling strategy, but have not yet been commercially realized. Biofouling begins with small molecules and polymers that initiate settlement for larger organisms. Using an enzymatic coating to rapidly hydrolyze these compounds could reduce the surface concentration of these attractive polymers and prevent organism growth. Here, antifouling xylanase and lysing complex enzymes were covalently tethered to surfaces using isoindolinone groups and click chemistry. We found that xylanase and lysing complex continue to hydrolyze xylosidic bonds in hemicellulose polysaccharides after covalent tethering, and the coating maintained activities of >  80% and  >  50%, respectively, after 2 months while submerged in artificial seawater, demonstrating this material’s potential as an eco-friendly antifouling coating.

Graphical abstract

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4

Similar content being viewed by others

References

  1. Pasmore, M, Costerton, JW, “Biofilms, Bacterial Signaling, and Their Ties to Marine Biology.” J. Ind. Microbiol. Biotechnol., 30 (7) 407–413. https://doi.org/10.1007/s10295-003-0069-6 (2003)

    Article  CAS  Google Scholar 

  2. Molino, PJ, Wetherbee, R, “The Biology of Biofouling Diatoms and Their Role in the Development of Microbial Slimes.” Biofouling, 24 (5) 365–379. https://doi.org/10.1080/08927010802254583 (2008)

    Article  CAS  Google Scholar 

  3. Buskens, P, Wouters, M, Rentrop, C, Vroon, Z, “A Brief Review of Environmentally Benign Antifouling and Foul-Release Coatings for Marine Applications.” J. Coat. Technol. Res., 10 (1) 29–36. https://doi.org/10.1007/s11998-012-9456-0 (2013)

    Article  CAS  Google Scholar 

  4. Briand, J-F, “Marine Antifouling Laboratory Bioassays: An Overview of Their Diversity.” Biofouling, 25 (4) 297–311. https://doi.org/10.1080/08927010902745316 (2009)

    Article  CAS  Google Scholar 

  5. Royer, S-J, Wiggin, K, Kogler, M, Deheyn, DD, “Degradation of Synthetic and Wood-Based Cellulose Fabrics in the Marine Environment: Comparative Assessment of Field, Aquarium, and Bioreactor Experiments.” Sci. Total Environ., 791 148060. https://doi.org/10.1016/j.scitotenv.2021.148060 (2021)

    Article  CAS  Google Scholar 

  6. Kyei, SK, Darko, G, Akaranta, O, “Chemistry and Application of Emerging Ecofriendly Antifouling Paints: A Review.” J. Coat. Technol. Res., 17 (2) 315–332. https://doi.org/10.1007/s11998-019-00294-3 (2020)

    Article  CAS  Google Scholar 

  7. Yebra, DM, Kiil, S, Dam-Johansen, K, “Antifouling Technology—Past, Present and Future Steps Towards Efficient and Environmentally Friendly Antifouling Coatings.” Prog. Org. Coat., 50 (2) 75–104. https://doi.org/10.1016/j.porgcoat.2003.06.001 (2004)

    Article  CAS  Google Scholar 

  8. Aykin, E, Omuzbuken, B, Kacar, A, “Microfouling Bacteria and the Use of Enzymes in Eco-Friendly Antifouling Technology.” J. Coat. Technol. Res., 16 (3) 847–856. https://doi.org/10.1007/s11998-018-00161-7 (2019)

    Article  CAS  Google Scholar 

  9. Cordeiro, AL, Werner, C, “Enzymes for Antifouling Strategies.” J. Adhes. Sci. Technol., 25 (17) 2317–2344. https://doi.org/10.1163/016942411X574961 (2011)

    Article  CAS  Google Scholar 

  10. Lee, J, Lee, I, Nam, J, Hwang, DS, Yeon, K-M, Kim, J, “Immobilization and Stabilization of Acylase on Carboxylated Polyaniline Nanofibers for Highly Effective Antifouling Application via Quorum Quenching.” ACS Appl. Mater. Interfaces, 9 (18) 15424–15432. https://doi.org/10.1021/acsami.7b01528 (2017)

    Article  CAS  Google Scholar 

  11. Olsen, SM, Pedersen, LT, Laursen, MH, Kiil, S, Dam-Johansen, K, “Enzyme-Based Antifouling Coatings: A Review.” Biofouling, 23 (5) 369–383. https://doi.org/10.1080/08927010701566384 (2007)

    Article  CAS  Google Scholar 

  12. Zhang, Y, Liang, Y, Huang, F, Zhang, Y, Li, X, Xia, J, “Site-Selective Lysine Reactions Guided by Protein-Peptide Interaction.” Biochemistry, 58 (7) 1010–1018. https://doi.org/10.1021/acs.biochem.8b01223 (2019)

    Article  CAS  Google Scholar 

  13. Tung, CL, Wong, CTT, Fung, EYM, Li, X, “Traceless and Chemoselective Amine Bioconjugation via Phthalimidine Formation in Native Protein Modification.” Org. Lett., 18 (11) 2600–2603. https://doi.org/10.1021/acs.orglett.6b00983 (2016)

    Article  CAS  Google Scholar 

  14. Zhang, Q, Zhang, Y, Liu, H, Chow, HY, Tian, R, Eva Fung, YM, Li, X, “OPA-Based Bifunctional Linker for Protein Labeling and Profiling.” Biochemistry, 59 (2) 175–178. https://doi.org/10.1021/acs.biochem.9b00787 (2020)

    Article  CAS  Google Scholar 

  15. Pickens, CJ, Johnson, SN, Pressnall, MM, Leon, MA, Berkland, CJ, “Practical Considerations, Challenges, and Limitations of Bioconjugation via Azide-Alkyne Cycloaddition.” Bioconjug. Chem., 29 (3) 686–701. https://doi.org/10.1021/acs.bioconjchem.7b00633 (2018)

    Article  CAS  Google Scholar 

  16. Bartlett, ME, Shuler, SA, Rose, DJ, Gilbert, LM, Hegab, RA, Lawton, TJ, Messersmith, RE, “Paintable Proteins: Biofunctional Coatings via Covalent Incorporation of Proteins into a Polymer Network.” New J. Chem., 45 (47) 22084–22092. https://doi.org/10.1039/D1NJ04687J (2021)

    Article  CAS  Google Scholar 

  17. Wine, Y, Cohen-Hadar, N, Freeman, A, Frolow, F, “Elucidation of the Mechanism and End Products of Glutaraldehyde Crosslinking Reaction by X-Ray Structure Analysis.” Biotechnol. Bioeng., 98 (3) 711–718. https://doi.org/10.1002/bit.21459 (2007)

    Article  CAS  Google Scholar 

  18. Hu, J, Davies, J, Mok, YK, Arato, C, Saddler, JN, “The Potential of Using Immobilized Xylanases to Enhance the Hydrolysis of Soluble, Biomass Derived Xylooligomers.” Materials, 11 (10) 2005 (2018)

    Article  Google Scholar 

  19. Kapoor, M, Kuhad, RC, “Immobilization of Xylanase from Bacillus pumilus Strain MK001 and its Application in Production of Xylo-oligosaccharides.” Appl. Biochem. Biotechnol., 142 (2) 125–138. https://doi.org/10.1007/s12010-007-0013-8 (2007)

    Article  CAS  Google Scholar 

  20. Pal, A, Khanum, F, “Covalent Immobilization of Xylanase on Glutaraldehyde Activated Alginate Beads Using Response Surface Methodology: Characterization of Immobilized Enzyme.” Process Biochem., 46 (6) 1315–1322. https://doi.org/10.1016/j.procbio.2011.02.024 (2011)

    Article  CAS  Google Scholar 

  21. Hu, J, Davies, J, Mok, YK, Arato, C, Saddler, JN, “The Potential of Using Immobilized Xylanases to Enhance the Hydrolysis of Soluble, Biomass Derived Xylooligomers.” Materials, 11 (10) 2005. https://doi.org/10.3390/ma11102005 (2018)

    Article  CAS  Google Scholar 

  22. Kumar, L, Nagar, S, Mittal, A, Garg, N, Gupta, VK, “Immobilization of Xylanase Purified from Bacillus pumilus VLK-1 and its Application in Enrichment of Orange and Grape Juices.” J. Food Sci. Technol., 51 (9) 1737–1749. https://doi.org/10.1007/s13197-014-1268-z (2014)

    Article  CAS  Google Scholar 

  23. Hlady, V, Buijs, J, “Protein Adsorption on Solid Surfaces.” Curr. Opin. Biotechnol., 7 (1) 72–77. https://doi.org/10.1016/S0958-1669(96)80098-X (1996)

    Article  CAS  Google Scholar 

  24. Rabe, M, Verdes, D, Seeger, S, “Understanding Protein Adsorption Phenomena at Solid Surfaces.” Adv. Colloid Interface Sci., 162 (1) 87–106. https://doi.org/10.1016/j.cis.2010.12.007 (2011)

    Article  CAS  Google Scholar 

  25. Le Droumaguet, B, Velonia, K, “Click Chemistry: A Powerful Tool to Create Polymer-Based Macromolecular Chimeras.” Macromol. Rapid Commun., 29 (12–13) 1073–1089. https://doi.org/10.1002/marc.200800155 (2008)

    Article  CAS  Google Scholar 

  26. Thordarson, P, Le Droumaguet, B, Velonia, K, “Well-Defined Protein–Polymer Conjugates—Synthesis and Potential Applications.” Appl. Microbiol. Biotechnol., 73 (2) 243–254. https://doi.org/10.1007/s00253-006-0574-4 (2006)

    Article  CAS  Google Scholar 

  27. Fontaine, SD, Reid, R, Robinson, L, Ashley, GW, Santi, DV, “Long-Term Stabilization of Maleimide-Thiol Conjugates.” Bioconjugate Chem., 26 (1) 145–152. https://doi.org/10.1021/bc5005262 (2015)

    Article  CAS  Google Scholar 

  28. Weltz, JS, Kienle, DF, Schwartz, DK, Kaar, JL, “Reduced Enzyme Dynamics Upon Multipoint Covalent Immobilization Leads to Stability-Activity Trade-off.” J. Am. Chem. Soc., 142 (7) 3463–3471. https://doi.org/10.1021/jacs.9b11707 (2020)

    Article  CAS  Google Scholar 

  29. Bey, H, Gtari, W, Aschi, A, Othman, T, “Structure and Properties of Native and Unfolded Lysing Enzyme from T. Harzianum: Chemical and pH Denaturation.” Int. J. Biol. Macromol., 92 860–866. https://doi.org/10.1016/j.ijbiomac.2016.08.001 (2016)

    Article  CAS  Google Scholar 

  30. Horta, MAC, Filho, JAF, Murad, NF, de Oliveira Santos, E, dos Santos, CA, Mendes, JS, Brandão, MM, Azzoni, SF, de Souza, AP, “Network of Proteins, Enzymes and Genes Linked to Biomass Degradation Shared by Trichoderma Species.” Sci. Rep., 8 (1) 1341. https://doi.org/10.1038/s41598-018-19671-w (2018)

    Article  CAS  Google Scholar 

  31. Kristensen, JB, Meyer, RL, Laursen, BS, Shipovskov, S, Besenbacher, F, Poulsen, CH, “Antifouling Enzymes and the Biochemistry of Marine Settlement.” Biotechnol. Adv., 26 (5) 471–481. https://doi.org/10.1016/j.biotechadv.2008.05.005 (2008)

    Article  CAS  Google Scholar 

Download references

Acknowledgments

Johns Hopkins University Applied Physics Laboratory Research and Exploratory Development Department provided internal research funding for this work.

Author information

Authors and Affiliations

  1. Research and Exploratory Development Department, The Johns Hopkins University Applied Physics Laboratory, 11100 Johns Hopkins Rd, Laurel, MD, 20723, USA

    Ryan W. Baker-Branstetter, Mairead E. Bartlett, Scott A. Shuler & Reid E. Messersmith

Authors
  1. Ryan W. Baker-Branstetter
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Mairead E. Bartlett
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Scott A. Shuler
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Reid E. Messersmith
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Reid E. Messersmith.

Ethics declarations

Conflict of interest

All authors declare that they have no conflicts of interest.

Additional information

Publisher's Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Rights and permissions

Springer Nature or its licensor holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Baker-Branstetter, R.W., Bartlett, M.E., Shuler, S.A. et al. Covalent immobilization of xylanase and lysing complex into polymer scaffolds with long-term activity retention. J Coat Technol Res 20, 973–978 (2023). https://doi.org/10.1007/s11998-022-00717-8

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11998-022-00717-8

Keywords

Search

Navigation