Advertisement

Journal of Coatings Technology and Research

, Volume 13, Issue 4, pp 597–611 | Cite as

The enzyme-mediated autodeposition of casein: effect of enzyme immobilization on deposition of protein structures

  • Arne A. Ruediger
  • Wolfgang Bremser
  • Oliver I. StrubeEmail author
Article

Abstract

The enzyme-mediated autodeposition on the example of casein is reviewed, and deposition of casein structures is investigated in relation to applied immobilization methods of enzyme. First, casein is described in detail with respect to its structure in aqueous environments, followed by presentation of historical and current nonfood applications of casein. The presented process uses enzymes to trigger deposition of bio-based particles in close proximity to a support surface and allows for a high control over film formation and site-specificity. This is ensured by immobilization of enzyme on the support material. The herein described system is based on casein as protein and chymosin as enzyme. Different immobilization methods are investigated with respect to obtainable casein coatings, layers, and structures. Physical adsorption of enzyme enables the formation of casein coatings with controllable film thickness and is suitable for in situ buildup of adhesive layers due to diffusion of enzyme. The highest control over film formation is provided by covalent attachment of enzyme. Based on the attained results, the enzyme-mediated autodeposition gives new insights into biological material design.

Graphical abstract

Keywords

Enzyme-mediated autodeposition Casein Protein Bio-based coating Enzyme immobilization Structuring 

References

  1. 1.
    Galià, M, De Espinosa, LM, Ronda, JC, Lligadas, G, Cádiz, V, “Vegetable Oil-Based Thermosetting Polymers.” Eur. J. Lipid Sci. Technol., 112 (1) 87–96 (2009)CrossRefGoogle Scholar
  2. 2.
    Vieira, MGA, Da Silva, MA, Dos Santos, LO, “Natural-Based Plasticizers and Biopolymer Films: A Review.” Eur. Polym. J., 47 (3) 254–263 (2011)CrossRefGoogle Scholar
  3. 3.
    Kircher, M, “The Transition to a Bio-Economy: Emerging from the Oil Age.” Biofuels, Bioprod. Biorefin., 6 (4) 369–375 (2012)CrossRefGoogle Scholar
  4. 4.
    Oh, JK, Lee, DI, Park, JM, “Biopolymer-Based Microgels/Nanogels for Drug Delivery Applications.” Prog. Polym. Sci., 34 (12) 1261–1282 (2009)CrossRefGoogle Scholar
  5. 5.
    Tristram, CJ, Mason, JM, Williams, DBG, Hinkley, SFR, “Doubly Renewable Cellulose Polymer for Water-Based Coatings.” ChemSusChem, 8 (1) 63–66 (2015)CrossRefGoogle Scholar
  6. 6.
    Bumgardner, JD, Wiser, R, Gerard, PD, Bergin, P, Chestnutt, B, Marin, M, Ramsey, V, Elder, SH, Gilbert, JA, “Chitosan: Potential Use as a Bioactive Coating for Orthopaedic and Craniofacial/Dental Implants.” Biomater. Sci. Polym. Ed., 14 (5) 423–438 (2003)CrossRefGoogle Scholar
  7. 7.
    Wihodo, M, Moraru, CI, “Physical and Chemical Methods Used to Enhance the Structure and Mechanical Properties of Protein Films: A Review.” J. Food Eng., 114 (3) 292–302 (2013)CrossRefGoogle Scholar
  8. 8.
    Lin, Q, Chen, N, Bian, L, Fan, M, “Development and Mechanism Characterization of High Performance Soy-Based Bio-Adhesives.” Int. J. Adhes. Adhes., 34 11–16 (2012)CrossRefGoogle Scholar
  9. 9.
    Biscarat, J, Charmette, C, Sanchez, J, Pochat-Bohatier, C, “Development of a New Family of Food Packaging Bioplastics from Crosslinked Gelatin Based Films.” Can. J. Chem. Eng., 93 (2) 176–182 (2015)CrossRefGoogle Scholar
  10. 10.
    Zhang, X, Burgar, I, Do, MD, Lourbakos, E, “Intermolecular Interactions and Phase Structures of Plasticized Wheat Proteins Materials.” Biomacromolecules, 6 (3) 1661–1671 (2005)CrossRefGoogle Scholar
  11. 11.
    Picchio, ML, Minari, RJ, Gonzalez, VDG, Passeggi, MCG, Vega, JR, Barandiaran, MJ, Gugliotta, LM, “Waterborne Acrylic-Casein Nanoparticles. Nucleation and Grafting.” Macromol. Symp., 344 (1) 76–85 (2014)CrossRefGoogle Scholar
  12. 12.
    Horne, DS, “Casein Structure, Self-Assembly and Gelation.” Curr. Opin. Colloid Interface Sci., 7 (5–6) 456–461 (2002)CrossRefGoogle Scholar
  13. 13.
    Farrell, HM, Malin, EL, Brown, EM, Qi, PX, “Casein Micelle Structure: What can be Learned from Milk Synthesis and Structural Biology?” Curr. Opin. Colloid Interface Sci., 11 (2–3) 135–147 (2006)CrossRefGoogle Scholar
  14. 14.
    Fox, PF, Brodkorb, A, “The Casein Micelle: Historical Aspects, Current Concepts and Significance.” Int. Dairy J., 18 (7) 677–684 (2008)CrossRefGoogle Scholar
  15. 15.
    Gebhardt, R, Vendrely, C, Kulozik, U, “Structural Characterization of Casein Micelles: Shape Changes during Film Formation.” J. Phys.: Condens. Matter, 23 (44) 444201 (2011)Google Scholar
  16. 16.
    Ruettimann, KW, Ladisch, MR, “Casein Micelles: Structure, Properties and Enzymatic Coagulation.” Enzyme Microb. Technol., 9 (10) 578–589 (1987)CrossRefGoogle Scholar
  17. 17.
    Rao, MB, Tanksale, AM, Ghatge, MS, Deshpande, VV, “Molecular and Biotechnological Aspects of Microbial Proteases.” Microbiol. Mol. Biol. Rev., 62 (3) 597–635 (1998)Google Scholar
  18. 18.
    Burton, SC, Haggarty, NW, Harding, DR, “One Step Purification of Chymosin by Mixed Mode Chromatography.” Biotechnol. Bioeng., 56 (1) 45–55 (1997)CrossRefGoogle Scholar
  19. 19.
    Swaisgood, HE, “Review and Updated of Casein Chemistry.” J. Dairy Sci., 76 (10) 3054–3061 (1993)CrossRefGoogle Scholar
  20. 20.
    Chick, J, Ustunol, Z, “Mechanical and Barrier Properties of Lactic Acid and Rennet Precipitated Casein-Based Edible Films.” J. Food Sci., 63 (6) 1024–1027 (1998)CrossRefGoogle Scholar
  21. 21.
    Picchio, ML, Passeggi, MCG, Barandiaran, MJ, Gugliotta, LM, Minari, RJ, “Waterborne Acrylic-Casein Latexes as Eco-Friendly Binders for Coatings.” Prog. Org. Coat., 88 8–16 (2015)CrossRefGoogle Scholar
  22. 22.
    Chambi, H, Grosso, C, “Edible Films Produced with Gelatin and Casein Crosslinked with Transglutaminase.” Food Res. Int., 39 (4) 458–466 (2006)CrossRefGoogle Scholar
  23. 23.
    Juvonen, H, Smolander, M, Boer, H, Pere, J, Buchert, J, Peltonen, J, “Film Formation and Surface Properties of Enzymatically Crosslinked Casein Films.” J. Appl. Polym. Sci., 119 (4) 2205–2213 (2011)CrossRefGoogle Scholar
  24. 24.
    Müller-Buschbaum, P, Gebhardt, R, Maurer, E, Bauer, E, Gehrke, R, Doster, W, “Thin Casein Films as Prepared by Spin-Coating: Influence of Film Thickness and of pH.” Biomacromolecules, 7 (6) 1773–1780 (2006)CrossRefGoogle Scholar
  25. 25.
    Silva, GA, Vaz, CM, Coutinho, OP, Cunha, AM, Reis, RL, “In Vitro Degradation and Cytocompatibility Evaluation of Novel Soy and Sodium Caseinate-Based Membrane Biomaterials.” J. Mater. Sci.: Mater. Med., 14 1055–1066 (2003)Google Scholar
  26. 26.
    Vaz, CM, Fossen, M, Van Tuil, RF, De Graaf, LA, Reis, RL, Cunha, AM, “Casein and Soybean Protein-Based Thermoplastics and Composites as Alternative Biodegradable Polymers for Biomedical Applications.” J. Biomed. Mater. Res. Part A, 65 60–70 (2003)CrossRefGoogle Scholar
  27. 27.
    Walstra, P, “On the Stability of Casein Micelles.” J. Dairy Sci., 73 (8) 1965–1979 (1990)CrossRefGoogle Scholar
  28. 28.
    Walstra, P, “Casein Sub-Micelles: Do They Exist?” Int. Dairy J., 9 (3–6) 189–192 (1999)CrossRefGoogle Scholar
  29. 29.
    Holt, C, “Structure and Stability of Bovine Casein Micelles.” Adv. Protein Chem., 43 63–151 (1992)CrossRefGoogle Scholar
  30. 30.
    De Kruif, CG, Huppertz, T, Urban, VS, Petukhov, AV, “Casein Micelles and Their Internal Structure.” Adv. Colloid Interface Sci., 171–172 36–52 (2012)CrossRefGoogle Scholar
  31. 31.
    Lucey, J, “Formation and Physical Properties of Milk Protein Gels.” J. Dairy Sci., 85 (2) 281–294 (2002)CrossRefGoogle Scholar
  32. 32.
    Horne, DS, “Casein Interactions: Casting Light on the Black Boxes, the Structure in Dairy Products.” Int. Dairy J., 8 (3) 171–177 (1998)CrossRefGoogle Scholar
  33. 33.
    Horne, DS, “Casein Micelle Structure: Models and Muddles.” Curr. Opin. Colloid Interface Sci., 11 (2–3) 148–153 (2006)CrossRefGoogle Scholar
  34. 34.
    Dalgleish, DG, “Casein Micelles as Colloids: Surface Structures and Stabilities.” J. Dairy Sci., 81 (11) 3013–3018 (1998)CrossRefGoogle Scholar
  35. 35.
    Audic, J-L, Chaufer, B, Daufin, G, “Nonfood Applications of Milk Components and Dairy Co-Products: A Review.” Lait, 83 (6) 417–438 (2003)CrossRefGoogle Scholar
  36. 36.
    Govers, FX, “Casein Glue.” US Patent 799,599, 1905Google Scholar
  37. 37.
    Hall, WA, “Adhesive.” US Patent 695,926, 1902Google Scholar
  38. 38.
    Lambuth, A, “Soybean, Blood, and Casein Glues.” In: Tracton, AA (ed.) Coatings Technology Handbook, pp. 64-7–64-11. CRC Press, Boca Raton (2006)Google Scholar
  39. 39.
    Audic, J-L, Chaufer, B, “Influence of Plasticizers and Crosslinking on the Properties of Biodegradable Films Made from Sodium Caseinate.” Eur. Polym. J., 41 (8) 1934–1942 (2005)CrossRefGoogle Scholar
  40. 40.
    Columbus, PS, Mason, RT, “Labeling Adhesive.” US Patent 3,376,148, 1968Google Scholar
  41. 41.
    Levecke, B, Lipkens, H, “Aqueous Adhesive Compositions, Preparing Adhesive Compositions and Labelling Containers.” WO Patent 2012134281 (A2), 2012Google Scholar
  42. 42.
    De Graaf, LA, Kolster, P, “Industrial Proteins as a Green Alternative for “Petro” Polymers: Potentials and Limitations.” Macromol. Symp., 127 51–58 (1998)CrossRefGoogle Scholar
  43. 43.
    Ferretti, A, “Production of the Artificial Wool Called Lannital form Casein.” Ind. Text., 54 446–447 (1937)Google Scholar
  44. 44.
    De Kruif, CG, “Nonfood Applications of Casein.” Prog. Biotechnol., 23 259–263, 269 (2003)Google Scholar
  45. 45.
    Brother, GH, “Casein Plastics.” Ind. Eng. Chem., 32 31–33 (1940)CrossRefGoogle Scholar
  46. 46.
    Chen, H, “Functional Properties and Applications of Edible Films Made of Milk Proteins.” J. Dairy Sci., 78 (11) 2563–2583 (1995)CrossRefGoogle Scholar
  47. 47.
    Schou, M, Longares, A, Montesinos-Herrero, C, O´Riordan, D, O´Sullivan, M, Monahan, FJ, “Properties of Edible Sodium Caseinate Films and Their Application as Food Wrapping.” LWT–Food Sci. Technol., 38 (6) 605–610 (2005)CrossRefGoogle Scholar
  48. 48.
    Kozempel, M, Tomasula, PM, “Delevopment of a Continuous Process to Make Casein Films.” J. Agric. Food Chem., 52 1190–1195 (2004)CrossRefGoogle Scholar
  49. 49.
    Yang, H, Wen, XL, Guo, SG, Chen, MT, Jiang, AM, Lai, L-S, “Physical, Antioxidant and Structural Characterization of Blend Films Based on Hsian-Tsao Gum (HG) and Casein (CAS).” Carbohydr. Polym., 134 222–229 (2015)CrossRefGoogle Scholar
  50. 50.
    Abu Diak, O, Bani-Jaber, A, Amro, B, Jones, D, Andrews, BP, “The Manufacture and Characterization of Casein Films as Novel Tablet Coatings.” Food Bioprod. Process., 85 (C3) 284–290 (2007)CrossRefGoogle Scholar
  51. 51.
    Luo, Y, Pan, K, Zhong, Q, “Casein/Pectin Nanocomplexes as Potential Oral Delivery Vehicles.” Int. J. Pharm., 486 (1–2) 59–68 (2015)CrossRefGoogle Scholar
  52. 52.
    Song, F, Zhang, L-M, Yang, C, Yan, L, “Genipin-Crosslinked Casein Hydrogels for Controlled Drug Delivery.” Int. J. Pharm., 373 (1–2) 41–47 (2009)CrossRefGoogle Scholar
  53. 53.
    Shindo, K, Arima, S, “Studies on the Immobilized Chymosin Part II.” J. Fac. Agric. Hokkaido Univ., 59 284–293 (1979)Google Scholar
  54. 54.
    Sheldon, RA, “Enzyme Immobilization: The Quest for Optimum Performance.” Adv. Synth. Catal., 349 (8–9) 1289–1307 (2007)CrossRefGoogle Scholar
  55. 55.
    Barbosa, O, Torres, R, Ortiz, C, Berenguer-Murcia, A, Rodrigues, RC, Fernandez-Lafuente, R, “Heterofunctional Supports in Enzyme Immobilization: From Traditional Immobilization Protocols to Opportunities in Tuning Enzyme Properties.” Biomacromolecules, 14 (8) 2433–2462 (2013)CrossRefGoogle Scholar
  56. 56.
    Strube, OI, Ruediger, AA, Bremser, W, “Enzymatically Controlled Material Design with Casein-From Defined Films to Localized Deposition of Particles.” J. Biotechnol., 201 69–74 (2015)CrossRefGoogle Scholar
  57. 57.
    Strube, OI, Ruediger, AA, Bremser, W, “Buildup of Biobased Adhesive Layers by Enzymatically Controlled Deposition on the Example of Casein.” Int. J. Adhes. Adhes., 63 9–13 (2015)CrossRefGoogle Scholar
  58. 58.
    Strube, OI, Buengeler, A, Bremser, W, “Site-Specific In Situ Synthesis of Eumelanin Nanoparticles by an Enzymatic Autodeposition-Like Process.” Biomacromolecules, 16 (5) 1608–1613 (2015)CrossRefGoogle Scholar
  59. 59.
    Tavano, OL, “Protein Hydrolysis Using Proteases: An Important Tool for Food Biotechnology.” J. Mol. Catal. B: Enzym., 90 1–11 (2013)CrossRefGoogle Scholar
  60. 60.
    Provansal, MMP, Cuq, JLA, Cheftel, JC, “Chemical and Nutritional Modifications of Sunflower Proteins due to Alkalline Processing. Formation of Amino Acid Crosslinks and Isomerization of Lysine Residues.” J. Agric. Food Chem., 23 (5) 938–943 (1975)CrossRefGoogle Scholar
  61. 61.
    Maldonado, J, Gil, A, Narbona, E, Molina, JA, “Special Formulas in Infant Nutrition: A Review.” Early Hum. Dev., 53 S23–S32 (1998)CrossRefGoogle Scholar
  62. 62.
    Pessela, BCC, Torres, R, Fuentes, M, Mateo, C, Fernandez-Lafuente, R, Guisan, JM, “Immobilization of Rennet from Mucor Miehei via its Sugar Chain. Its Use in Milk Coagulation.” Biomacromolecules, 5 (5) 2029–2033 (2004)CrossRefGoogle Scholar
  63. 63.
    Mateo, C, Palomo, JM, Fernandez-Lorente, G, Guisan, JM, Fernandez-Lafuente, R, “Improvement of Enzyme Activity, Stability and Selectivity via Immobilization Techniques.” Enzyme Microb. Technol., 40 (6) 1451–1463 (2007)CrossRefGoogle Scholar
  64. 64.
    Iyer, PV, Ananthanarayan, L, “Enzyme Stability and Stabilization-Aqueous and Nonaqueous Environment.” Process Biochem., 43 (10) 1019–1032 (2008)CrossRefGoogle Scholar
  65. 65.
    Hanefeld, U, Gardossi, L, Magner, E, “Understanding Enzyme Immobilisation.” Chem. Soc. Rev., 38 (2) 453–468 (2009)CrossRefGoogle Scholar
  66. 66.
    Brady, D, Jordaan, J, “Advances in Enzyme Immobilisation.” Biotechnol. Lett., 31 (11) 1639–1650 (2009)CrossRefGoogle Scholar
  67. 67.
    Straathof, AJ, Panke, S, Schmid, A, “The Production of Fine Chemicals by Biotransformations.” Curr. Opin. Biotechnol., 13 (6) 548–556 (2002)CrossRefGoogle Scholar
  68. 68.
    Katchalski-Katzir, E, “Immobilized Enzymes: Learning from Past Successes and Failures.” Trends Biotechnol., 11 (11) 471–478 (1993)CrossRefGoogle Scholar
  69. 69.
    Rodrigues, RC, Ortiz, C, Berenguer-Murcia, A, Torres, R, Fernandez-Lafuente, R, “Modifying Enzyme Activity and Selectivity by Immobilization.” Chem. Soc. Rev., 42 (15) 6290–6307 (2013)CrossRefGoogle Scholar
  70. 70.
    Garcia-Galan, C, Berenguer-Murcia, A, Fernandez-Lafuente, R, Rodrigues, RC, “Potential of Different Enzyme Immobilization Strategies to Improve Enzyme Performance.” Adv. Synth. Catal., 353 (16) 2885–2904 (2011)CrossRefGoogle Scholar
  71. 71.
    Montes, T, Grazu, V, Lopez-Gallego, F, Hermoso, JA, Garcia, JL, Manso, I, Galan, B, Gonzalez, R, Fernandez-Lafuente, R, Guisan, JM, “Genetic Modification of the Penicillin G Acylase Surface to Improve Its Reversible Immobilization on Ionic Exchangers.” Appl. Environ. Microbiol., 73 (1) 312–319 (2007)CrossRefGoogle Scholar
  72. 72.
    Hernandez, K, Fernandez-Lafuente, R, “Control of Protein Immobilization: Coupling Immobilization and Site-Directed Mutagenesis to Improve Biocatalyst or Biosensor Performance.” Enzyme Microb. Technol., 48 (2) 107–122 (2011)CrossRefGoogle Scholar
  73. 73.
    Torres, R, Ortiz, C, Pessela, BCC, Palomo, JM, Mateo, C, Guisan, JM, Fernandez-Lafuente, R, “Improvement of the Enantioselectivity of Lipase (Fraction B) from Candida Antarctica via Adsorption on Polyethylenimine-Agarose under Different Experimental Conditions.” Enzyme Microb. Technol., 39 (2) 167–171 (2006)CrossRefGoogle Scholar
  74. 74.
    Mohamad, NR, Marzuki, NHC, Buang, NA, Huyop, F, Abdul Wahab, R, “An Overview of Technologies for Immobilization of Enzymes and Surface Analysis Techniques for Immobilized Enzymes.” Biotechnol. Biotechnol. Equip., 29 (2) 205–220 (2015)CrossRefGoogle Scholar
  75. 75.
    Torres, R, Pessela, BCC, Mateo, C, Ortiz, C, Fuentes, M, Guisan, JM, Fernandez-Lafuente, R, “Reversible Immobilization of Glucoamylase by Ionic Adsorption on Sepabeads Coated with Polyethyleneimine.” Biotechnol. Prog., 20 (4) 1297–1300 (2004)CrossRefGoogle Scholar
  76. 76.
    Cosnier, S, “Biomolecule Immobilization on Electrode Surfaces by Entrapment or Attachment to Electrochemically Polymerized Films. A Review.” Biosens. Bioelectron., 14 (5) 443–456 (1999)CrossRefGoogle Scholar
  77. 77.
    Cao, L, “Immobilised Enzymes: Science or Art?” Curr. Opin. Chem. Biol., 9 (2) 217–226 (2005)CrossRefGoogle Scholar
  78. 78.
    Ichimura, K, Watanabe, S, “Immobilization of Enzymes with Use of Photosensitive Polymers Having the Stilbazolium Group.” J. Polym. Sci. Polym. Chem. Ed., 18 (3) 891–902 (1980)CrossRefGoogle Scholar
  79. 79.
    Reetz, MT, Zonta, A, Simpelkamp, J, “Efficient Immobilization of Lipases by Entrapment in Hydrophobic Sol–Gel Materials.” Biotechnol. Bioeng., 49 (5) 527–534 (1996)CrossRefGoogle Scholar
  80. 80.
    Wilson, L, Illanes, A, Pessela, BCC, Abian, O, Fernandez-Lafuente, R, Guisan, JM, “Encapsulation of Crosslinked Penicillin G Acylase Aggregates in Lentikats: Evaluation of a Novel Biocatalyst in Organic Media.” Biotechnol. Bioeng., 86 (5) 558–562 (2004)CrossRefGoogle Scholar
  81. 81.
    Pierre, AC, “The Sol–Gel Encapsulation of Enzymes.” Biocatal. Biotransform., 22 (3) 145–170 (2004)CrossRefGoogle Scholar
  82. 82.
    Guisan, J, Fernandez-Lafuente, R, Rodriguez, V, Bastida, A, Alvaro, G, “Enzyme Stabilization by Multipoint Covalent Attachment to Activated Pre-Existing Supports.” In: Van der Tweel, W, Harder, A, Buitelar, R (eds.) Stability and Stabilization of Enzymes, pp. 55–62. Elsevier, Amsterdam (1993)CrossRefGoogle Scholar
  83. 83.
    Mateo, C, Grazu, V, Pessela, BCC, Montes, T, Palomo, JM, Torres, R, Lopez-Gallego, F, Fernandez-Lafuente, R, Guisan, JM, “Advances in the Design of New Epoxy Supports for Enzyme Immobilization-Stabilization.” Biochem. Soc. Trans., 35 (6) 1593–1601 (2007)CrossRefGoogle Scholar
  84. 84.
    Mateo, C, Abian, O, Fernandez-Lafuente, R, Guisan, JM, “Increase in Conformational Stability of Enzymes Immobilized on Epoxy-Activated Supports by Favoring Additional Multipoint Covalent Attachment.” Enzyme Microb. Technol., 26 (7) 509–515 (2000)CrossRefGoogle Scholar
  85. 85.
    Lei, L, Bai, Y, Li, Y, Yi, L, Yang, Y, Xia, C, “Study on Immobilization of Lipase onto Magnetic Microspheres with Epoxy Groups.” J. Magn. Magn. Mater., 321 (4) 252–258 (2008)CrossRefGoogle Scholar
  86. 86.
    Mateo, C, Torres, R, Fernandez-Lorente, G, Ortiz, C, Fuentes, M, Hidalgo, A, Lopez-Gallego, F, Abian, O, Polomo, JM, Betancor, L, Pessela, BCC, Guisan, JM, Fernandez-Lafuente, R, “Epoxy-Amino Groups: A New Tool for Improved Immobilization of Proteins by the Epoxy Method.” Biomacromolecules, 4 (3) 772–777 (2003)CrossRefGoogle Scholar
  87. 87.
    Katchalski-Katzir, E, Kraemer, DM, “Eupergit® C, a Carrier for Immobilization of Enzymes of Industrial Potential.” J. Mol. Catal. B: Enzym., 10 (1–3) 157–176 (2000)CrossRefGoogle Scholar
  88. 88.
    Mateo, C, Abian, O, Fernandez-Lorente, G, Pedroche, J, Fernandez-Lafuente, R, Guisan, JM, “Epoxy Sepabeads: A Novel Epoxy Support for Stabilization of Industrial Enzymes via Very Intense Multipoint Covalent Attachment.” Biotechnol. Prog., 18 (3) 629–634 (2002)CrossRefGoogle Scholar
  89. 89.
    Goddard, JM, Erickson, D, “Bioconjugation Techniques for Microfluidic Biosensors.” Anal. Bioanal. Chem., 394 (2) 469–479 (2009)CrossRefGoogle Scholar
  90. 90.
    Walt, DR, Agayn, VI, “The Chemistry of Enzyme and Protein Immobilization with Glutaraldehyde.” TrAC, Trends Anal. Chem., 13 (10) 425–430 (1994)CrossRefGoogle Scholar
  91. 91.
    Migneault, I, Dartiguenave, C, Bertrand, MJ, Waldron, KC, “Glutaraldehyde: Behavior in Aqueous Solution, Reactions with Proteins, and Application to Enzyme Crosslinking.” BioTechniques, 37 (5) 790–802 (2004)Google Scholar
  92. 92.
    Barbosa, O, Torres, R, Ortiz, C, Fernandez-Lafuente, R, “Versatility of Glutaraldehyde to Immobilize Lipases: Effect of the Immobilization Protocol on the Properties of Lipase B from Candida antarctica.” Process Biochem., 47 (8) 1220–1227 (2012)CrossRefGoogle Scholar
  93. 93.
    Barbosa, O, Ortiz, C, Berenguer-Murcia, A, Torres, R, Rodrigues, RC, Fernandez-Lafuente, R, “Glutaraldehyde in Bio-Catalysts Design: A Useful Crosslinker and a Versatile Tool in Enzyme Immobilization.” RCS Adv., 4 (4) 1583–1600 (2014)Google Scholar
  94. 94.
    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 (2007)CrossRefGoogle Scholar
  95. 95.
    Cao, L, Van Rantwijk, F, Sheldon, RA, “Cross-Linked Enzyme Aggregates: A Simple and Effective Method for the Immobilization of Penicillin Acylase.” Org. Lett., 2 (10) 1361–1364 (2000)CrossRefGoogle Scholar
  96. 96.
    Schoevaart, R, Wolbers, MW, Golubovic, M, Ottens, M, Kieboom, APG, Van Rantwijk, F, Van der Wielen, LAM, Sheldon, RA, “Preparation, Optimization, and Structures of Cross-Linked Enzyme Aggregates (CLEAs).” Biotechnol. Bioeng., 87 (6) 754–762 (2004)CrossRefGoogle Scholar
  97. 97.
    Gupta, P, Dutt, K, Misra, S, Raghuwanshi, S, Saxena, RK, “Characterization of Cross-Linked Immobilized Lipase from Thermophilic Mould Thermomyces lanuginosa Using Glutaraldehyde.” Bioresour. Technol., 100 (18) 4074–4076 (2009)CrossRefGoogle Scholar
  98. 98.
    Tatsumoto, K, Oh, KK, Baker, JO, Himmel, ME, “Enhanced Stability of Glucoamylase Through Chemical Crosslinking.” Appl. Biochem. Biotechnol., 20–21 293–308 (1989)CrossRefGoogle Scholar
  99. 99.
    Yamazaki, T, Tsugawa, W, Sode, K, “Increased Thermal Stability of Glucose Dehydrogenase by Cross-Linking Chemical Modification.” Biotechnol. Lett., 21 (3) 199–202 (1999)CrossRefGoogle Scholar
  100. 100.
    Lee, J, Kim, J, Kim, J, Jia, H, Kim, MI, Kwak, JH, Jin, S, Dohnalkova, A, Park, HG, Chang, HN, Wang, P, Grate, JW, Hyeon, T, “Simple Synthesis of Hierarchically Ordered Mesocellular Mesoporous Silica Materials Hosting Crosslinked Enzyme Aggregates.” Small, 1 (7) 744–753 (2005)CrossRefGoogle Scholar
  101. 101.
    Kim, MI, Kim, J, Lee, J, Shin, S, Na, HB, Hyeon, T, Park, HG, Chang, HN, “One-Dimensional Crosslinked Enzyme Aggregates in SBA-15: Superior Catalytic Behavior to Conventional Enzyme Immobilization.” Microporous Mesoporous Mater., 111 (1–3) 18–23 (2008)CrossRefGoogle Scholar
  102. 102.
    Lopez-Gallego, F, Betancor, L, Mateo, C, Hidalgo, A, Alonso-Morales, N, Dellamora-Ortiz, Guisan, JM, Fernandez-Lafuente, R, “Enzyme Stabilization by Glutaraldehyde Crosslinking of Adsorbed Proteins on Aminated Supports.” J. Biotechnol., 119 (1) 70–75 (2005)CrossRefGoogle Scholar
  103. 103.
    Betancor, L, Lopez-Gallego, F, Hidalgo, A, Alonso-Morales, N, Dellamora-Ortiz, G, Mateo, C, Fernandez-Lafuente, Guisan, JM, “Different Mechanisms of Protein Immobilization of Glutaraldehyde Activated Supports: Effect of Support Activation and Immobilization Conditions”.” Enzyme Microb. Technol., 39 (4) 877–882 (2006)CrossRefGoogle Scholar
  104. 104.
    Ruediger, AA, Terborg, E, Bremser, W, Strube, OI, “Influences on the Film Thickness in the Enzymatic Autodeposition Process of Casein.” Prog. Org. Coat., 94 56–61 (2016)CrossRefGoogle Scholar
  105. 105.
    Ruediger, AA, Bremser, W, Strube, OI, “Nanoscaled Biocoatings via Enzyme Mediated Autodeposition of Casein.” Macromol. Mater. Eng., (2016). doi: 10.1002/mame.201600034 Google Scholar
  106. 106.
    Harris, JM, Yoshinaga, K, “Assessment of the Effects of Attaching an Enzyme to Glass by a Poly(ethylene glycol) Tether.” J. Bioact. Compat. Polym., 4 (3) 281–295 (1989)CrossRefGoogle Scholar
  107. 107.
    Wang, Y, Hsieh, Y-L, “Enzyme Immobilization to Ultra-Fine Cellulose Fibers via Amphiphilic Polyethylene Glycol Spacers.” J. Polym. Sci. Part A Polym. Chem., 42 (17) 4289–4299 (2004)CrossRefGoogle Scholar
  108. 108.
    Alcantar, NA, Avdil, ES, Israelachvili, JN, “Polyethylene Glycol-Coated Biocompatible Surfaces.” J. Biomed. Mater. Res., 51 (3) 343–351 (2000)CrossRefGoogle Scholar

Copyright information

© American Coatings Association 2016

Authors and Affiliations

  • Arne A. Ruediger
    • 1
  • Wolfgang Bremser
    • 2
  • Oliver I. Strube
    • 1
    Email author
  1. 1.Department of Chemistry – Biobased and Bioinspired MaterialsUniversity of PaderbornPaderbornGermany
  2. 2.Department of Chemistry – Coatings, Materials and PolymersUniversity of PaderbornPaderbornGermany

Personalised recommendations