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Biomaterials Degradation and Bioabsorbability: Biomedical Potentials of Marine Enzymes

  • Kelvii Wei GuoEmail author
Reference work entry

Abstract

Biomaterials are most commonly recognized as scaffolds potentially able to perform useful functions such as (i) promoting cell attachment, survival, proliferation, and differentiation while possessing minimum toxicity in the original and biodegraded/bioabsorbed forms; (ii) allowing the transport or delivery of gases, nutrients, and growth factors; and (iii) offering sufficient structural support while being degradable/absorbable at appropriate rates for tissue regeneration.

Biodegradable/Bioabsorbable materials intended to be used as implantable drug eluting scaffolds must fulfill several requirements in order to be considered for clinical integration. They must not elicit abnormal responses in local tissues and should neither produce local nor systemic toxic or carcinogenic side effects. First and foremost, biodegradable/bioabsorbable platforms should serve their intended scaffolding and cell-signaling functions while degrading/absorbing into nontoxic metabolites. Breakdown of artificially manufactured scaffolds requires rigorous toxicological evaluation of each constituent component. Particularly when ambitious strategies involving the use of composite materials with integrated trophic factors are concerned, the importance of material biocompatibility evaluation rises significantly. The desired notion of effecting synergistic actions of GF (growth factor) and other incorporated component requires careful consideration of factor concentrations and release mechanisms in order to avoid potentially harmful overdosing. It therefore remains a priority to conduct systematic and rigorous toxicological studies – both in vitro and in vivo – to (1) eliminate grossly ineffective or toxic delivery platforms in order to (2) narrow down on potentially suitable candidate technologies as well as (3) ascertain any dose or time-dependencies which may influence the materials’ suitabilities.

Actually, the performance of many biomaterials depends largely on their degradation/absorbability behavior since the degradation/absorbability process may affect a range of events, such as cell growth, tissue regeneration, drug release, host response, and material function.

Biodegradable/Bioabsorbable medical materials are materials with the ability of functioning for a temporary period and subsequently degrade/absorb in physiological conditions, under a controlled mechanism, into products easily eliminated in the body’s metabolic pathways.

The demands for biomaterials with above-mentioned characteristics (controlled, predictable degradation/absorbability kinetics) included a wide range of biomedical applications (such as resorbable surgical sutures, matrices for the controlled release of drugs, and scaffolds for tissue engineering) are becoming more and more crucial and urgent.

Therefore, aim to provide promising potentials of marine enzymes for biomedical materials degradation/absorbability, the relevant potential marine enzymes such as amylases, esterases, cellulases, and laccases are reviewed. It indicates that strategies developed to obtain biomaterials with a controlled degradation/absorbability rate should be based on molecular design principles, such as the introduction of hydrolysable bonds into polymer backbones, copolymerization and blending techniques, crosslinking and surface modification methods, and inclusion of certain additives into polymeric matrices (e.g., excipients, drugs, salts).

Meanwhile, controlled degradation/absorbability of biomedical materials by potential marine enzymes will have several advantages considering the high specificity of enzymes for their substrates and also because enzyme activity can be regulated by environmental conditions (e.g., pH, temperature, the presence of certain substances, like metal ions). In addition, the degradation/absorbability kinetics can be adjusted by the amount of encapsulated enzyme into the matrix.

Keywords

Marine enzymes Biomedical Biomaterials Degradation/Bioabsorbability Mylases Esterases Cellulases Laccases 

Notes

Acknowledgment

The work is supported by the Strategic Research Grant (SRG) from City University of Hong Kong (Grant No.: 7004453).

References

  1. 1.
    Crapo PM, Gilbert TW, Badylak SF (2011) An overview of tissue and whole organ decellularization processes. Biomaterials 32:3233–3243Google Scholar
  2. 2.
    Ott HC, Matthiesen TS, Goh SK, Black LD, Kren SM, Netoff TI et al (2008) Perfusion-decellularized matrix: using nature’s platform to engineer a bioartificial heart. Nat Med 14:213–221Google Scholar
  3. 3.
    Petersen TH, Calle EA, Zhao L, Lee EJ, Gui L, Raredon MB et al (2010) Tissue engineered lungs for in vivo implantation. Science 329:538–541Google Scholar
  4. 4.
    Uygun BE, Soto-Gutierrez A, Yagi H, Izamis ML, Guzzardi MA, Shulman C et al (2010) Organ reengineering through development of a transplantable recellularized liver graft using decellularized liver matrix. Nat Med 16:814–820Google Scholar
  5. 5.
    Grayson WL, Frohlich M, Yeager K, Bhumiratana S, Chan ME, Cannizzaro C et al (2010) Engineering anatomically shaped human bone grafts. Proc Natl Acad Sci USA 107:3299–3304Google Scholar
  6. 6.
    Quint C, Kondo Y, Manson RJ, Lawson JH, Dardik A, Niklason LE (2011) Decellularized tissue-engineered blood vessel as an arterial conduit. Proc Natl Acad Sci USA 108:9214–9219Google Scholar
  7. 7.
    Baino F, Vitale-Brovarone C (2011) Three-dimensional glass-derived scaffolds for bone tissue engineering: current trends and forecasts for the future. J Biomed Mater Res A 97:514–535Google Scholar
  8. 8.
    Collier JH, Segura T (2011) Evolving the use of peptides as components of biomaterials. Biomaterials 32:4198–4204Google Scholar
  9. 9.
    Gasiorowski JZ, Collier JH (2011) Directed intermixing in multicomponent self-assembling biomaterials. Biomacromolecules 12:3549–3558Google Scholar
  10. 10.
    DiMarco RL, Heilshorn SC (2012) Multifunctional materials through modular protein engineering. Adv Mater 24:3923–3940Google Scholar
  11. 11.
    Werkmeister JA, Ramshaw JA (2012) Recombinant protein scaffolds for tissue engineering. Biomed Mater 7:012002Google Scholar
  12. 12.
    Huang X, Zauscher S, Klitzman B, Truskey GA, Reichert WM, Kenan DJ et al (2010) Peptide interfacial biomaterials improve endothelial cell adhesion and spreading on synthetic polyglycolic acid materials. Ann Biomed Eng 38:1965–1976Google Scholar
  13. 13.
    Stabenfeldt SE, Gourley M, Krishnan L, Hoying JB, Barker TH (2012) Engineering fibrin polymers through engagement of alternative polymerization mechanisms. Biomaterials 33:535–544Google Scholar
  14. 14.
    Soon AS, Smith MH, Herman ES, Lyon LA, Barker TH (2013) Development of self-assembling mixed protein micelles with temperature-modulated avidities. Adv Healthc Mater 2:1045–1055Google Scholar
  15. 15.
    Wojtowicz AM, Shekaran A, Oest ME, Dupont KM, Templeman KL, Hutmacher DW et al (2010) Coating of biomaterial scaffolds with the collagen-mimetic peptide GFOGER for bone defect repair. Biomaterials 31:2574–2582Google Scholar
  16. 16.
    Kim TG, Park TG (2006) Biomimicking extracellular matrix: cell adhesive RGD peptide modified electrospun poly(d, l-lactic-co-glycolic acid) nanofiber mesh. Tissue Eng 12:221–233Google Scholar
  17. 17.
    Wang PY, Wu TH, Tsai WB, Kuo WH, Wang MJ (2013) Grooved PLGA films incorporated with RGD/YIGSR peptides for potential application on skeletal muscle tissue engineering. Colloids Surf B Biointerfaces 110:88–95Google Scholar
  18. 18.
    Markowski MC, Brown AC, Barker TH (2012) Directing epithelial to mesenchymal transition through engineered microenvironments displaying orthogonal adhesive and mechanical cues. J Biomed Mater Res A 100:2119–2127Google Scholar
  19. 19.
    Chaisri P, Chingsungnoen A, Siri S, Repetitive RGD (2013) Peptide as cell-stimulating agent on electrospun PCL scaffold for tissue engineering. Biotechnol J 8(11):1323–1331Google Scholar
  20. 20.
    Carson AE, Barker TH (2009) Emerging concepts in engineering extracellular matrix variants for directing cell phenotype. Regen Med 4:593–600Google Scholar
  21. 21.
    Barker TH (2011) The role of ECM proteins and protein fragments in guiding cell behavior in regenerative medicine. Biomaterials 32:4211–4214Google Scholar
  22. 22.
    Athanasiou KA, Niederauer GG, Agrawal CM (1996) Sterilization, toxicity, biocompatibility and clinical applications of polylactic acid/polyglycolic acid copolymers. Biomaterials 17:93–102Google Scholar
  23. 23.
    Lotz AS, Havla JB, Richter E, Frolich K, Staudenmaier R, Hagen R et al (2009) Cytotoxic and genotoxic effects of matrices for cartilage tissue engineering. Toxicol Lett 190:128–133Google Scholar
  24. 24.
    Chlapanidas T, Tosca MC, Faragò S, Perteghella S, Galuzzi M, Lucconi G et al (2013) Formulation and characterization of silk fibroin films as a scaffold for adipose-derived stem cells in skin tissue engineering. Int J Immunopathol Pharmacol 26:43–49Google Scholar
  25. 25.
    Lee KH, Chu CC (2000) The role of superoxide ions in the degradation of synthetic absorbable sutures. J Biomed Mater Res 49:25–35Google Scholar
  26. 26.
    Park JS, Yang HN, Woo DG, Jeon SY, Park KH (2012) SOX9 gene plus heparinized TGF-β 3 coated dexamethasone loaded PLGA microspheres for inducement of chondrogenesis of hMSCs. Biomaterials 33:7151–7163Google Scholar
  27. 27.
    Losi P, Briganti E, Errico C, Lisella A, Sanguinetti E, Chiellini F et al (2013) Fibrin-based scaffold incorporating VEGF- and bFGF-loaded nanoparticles stimulates wound healing in diabetic mice. Acta Biomater 9:7814–7821Google Scholar
  28. 28.
    Zeugolis DI, Paul GR, Attenburrow G (2009) Cross-linking of extruded collagen fibers – a biomimetic three-dimensional scaffold for tissue engineering applications. J Biomed Mater Res A 89:895–908Google Scholar
  29. 29.
    Seedevi P, Moovendhan M, Vairamani S, Shanmugam A (2017) Evaluation of antioxidant activities and chemical analysis of sulfated chitosan from Sepia prashadi. Int J Biol Macromol 99:519–529Google Scholar
  30. 30.
    Duan X, Sheardown H (2006) Dendrimer crosslinked collagen as a corneal tissue engineering scaffold: mechanical properties and corneal epithelial cell interactions. Biomaterials 27:4608–4617Google Scholar
  31. 31.
    Park SN, Park JC, Kim HO, Song MJ, Suh H (2002) Characterization of porous collagen/hyaluronic acid scaffold modified by 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide crosslinking. Biomaterials 23:1205–1212Google Scholar
  32. 32.
    Coste O, Malta EJ, López JC, Fernández-Díaz C (2015) Production of sulfated oligosaccharides from the seaweed Ulva sp. using a new ulvan-degrading enzymatic bacterial crude extract. Algal Res 10:224–231Google Scholar
  33. 33.
    Yoshizawa K, Mizuta R, Taguchi T (2015) Enhanced angiogenesis of growth factor-free porous biodegradable adhesive made with hexanoyl group-modified gelatin. Biomaterials 63:14–23Google Scholar
  34. 34.
    Yanto DHY, Hidayat A, Tachibana S (2017) Periodical biostimulation with nutrient addition and bioaugmentation using mixed fungal cultures to maintain enzymatic oxidation during extended bioremediation of oily soil microcosms. Int Biodeter Biodegr 116:112–123Google Scholar
  35. 35.
    Gorczyca G, Tylingo R, Szweda P, Augustin E, Sadowska M, Milewski S (2014) Preparation and characterization of genipin cross-linked porous chitosan–collagen–gelatin scaffolds using chitosan–CO2 solution. Carbohydr Polym 102:901–911Google Scholar
  36. 36.
    Zhang X, Chen X, Yang T, Zhang N, Dong L, Ma S et al (2014) The effects of different crossing-linking conditions of genipin on type I collagen scaffolds: an in vitro evaluation. Cell Tissue Bank 15:531Google Scholar
  37. 37.
    Chuang CH, Lin RZ, Tien HW, Chu YC, Li YC, Melero-Martin JM, Chen YC (2015) Enzymatic regulation of functional vascular networks using gelatin hydrogels. Acta Biomater 19:85–99Google Scholar
  38. 38.
    Azizi N, Najafpour G, Younesi H (2017) Acid pretreatment and enzymatic saccharification of brown seaweed for polyhydroxybutyrate (PHB) production using Cupriavidus necator. Int J Biol Macromol 101:1029–1040Google Scholar
  39. 39.
    Berthod F, Hayek D, Damour O, Collombel C (1993) Collagen synthesis by fibroblasts cultured within a collagen sponge. Biomaterials 14:749–754Google Scholar
  40. 40.
    Nidheesh T, Kumar PG, Suresh PV (2015) Enzymatic degradation of chitosan and production of d-glucosamine by solid substrate fermentation of exo-β-d-glucosaminidase (exochitosanase) by Penicillium decumbens CFRNT15. Int Biodeter Biodegr 97:97–106Google Scholar
  41. 41.
    Suginta W, Sirimontree P, Sritho N, Ohnuma T, Fukamizo T (2016) The chitin-binding domain of a GH-18 chitinase from Vibrio harveyi is crucial for chitin-chitinase interactions. Int J Biol Macromol 93(A):1111–1117Google Scholar
  42. 42.
    Younes I, Hajji S, Rinaudo M, Chaabouni M, Jellouli K, Nasri M (2016) Optimization of proteins and minerals removal from shrimp shells to produce highly acetylated chitin. Int J Biol Macromol 84:246–253Google Scholar
  43. 43.
    Young T, Kesarcodi-Watson A, Alfaro AC, Merien F, Nguyen TV, Mae H, Le DV, Villas-Bôas S (2017) Differential expression of novel metabolic and immunological biomarkers in oysters challenged with a virulent strain of OsHV-1. Dev Comp Immunol 73:229–245Google Scholar
  44. 44.
    Gunatillake PA, Adhikari R (2003) Biodegradable synthetic polymers for tissue engineering. Eur Cell Mater 5:1–16. discussionGoogle Scholar
  45. 45.
    Cutright DE, Beasley JD, Perez B (1971) Histologic comparison of polylactic and polyglycolic acid sutures. Oral Surg Oral Med Oral Pathol 32:165–173Google Scholar
  46. 46.
    Mayer MH, Hollinger JO (1995) Biodegradable bone fixation devices. In: Hollinger JO (ed) Biomedical applications of synthetic biodegradable polymers. CRC Press, Boca Raton, pp 173–195Google Scholar
  47. 47.
    Thomson RC, Yaszemski MJ, Powers JM, Mikos AG (1995) Fabrication of biodegradable polymer scaffolds to engineer trabecular bone. J Biomater Sci Polym Ed 7:23–38Google Scholar
  48. 48.
    Bergsma EJ, Rozema FR, Bos RR, de Bruijn WC (1993) Foreign body reactions to resorbable poly(l-lactide) bone plates and screws used for the fixation of unstable zygomatic fractures. J Oral Maxillofac Surg 51:666–670Google Scholar
  49. 49.
    Böstman OM (1991) Osteolytic changes accompanying degradation of absorbable fracture fixation implants. J Bone Joint Surg 73:679–682Google Scholar
  50. 50.
    Böstman O, Hirvensalo E, Vainionpää S, Mäkelä A, Vihtonen K, Törmälä P et al (1989) Ankle fractures treated using biodegradable internal fixation. Clin Orthop Relat Res:195–203Google Scholar
  51. 51.
    Sollazzo V, Lucchese A, Palmieri A, Zollino I, Iaccarino C, Carnevali G et al (2011) Polylactide-polyglycolide resorbable plates stimulates adipose tissue-derived stem cells towards osteoblasts differentiation. Int J Immunopathol Pharmacol 24:59–64Google Scholar
  52. 52.
    Spivak JM, Ricci JL, Blumenthal NC, Alexander H (1990) A new canine model to evaluate the biological response of intramedullary bone to implant materials and surfaces. J Biomed Mater Res 24:1121–1149Google Scholar
  53. 53.
    Tang YW, Labow RS, Santerre JP (2003) Isolation of methylene dianiline and aqueous-soluble biodegradation products from polycarbonate–polyurethanes. Biomaterials 24:2805–2819Google Scholar
  54. 54.
    Yildirimer L, Thanh NTK, Loizidou M, Seifalian AM (2011) Toxicology and clinical potential of nanoparticles. Nano Today 6:585–607Google Scholar
  55. 55.
    Agrawal CM, Athanasiou KA (1997) Technique to control pH in vicinity of biodegrading PLA-PGA implants. J Biomed Mater Res 38:105–114Google Scholar
  56. 56.
    Pryde CA, Kelleher PG, Hellman MY, Wentz RP (1982) The hydrolytic stability of some commercially available polycarbonates. Polym Eng Sci 22:370–375Google Scholar
  57. 57.
    Labow RS, Meek E, Matheson LA, Santerre JP (2002a) Human macrophage-mediated biodegradation of polyurethanes: assessment of candidate enzyme activities. Biomaterials 23:3969–3975Google Scholar
  58. 58.
    Labow RS, Tang Y, McCloskey CB, Santerre JP (2002b) The effect of oxidation on the enzyme catalyzed hydrolytic biodegradation of poly(urethane)s. J Biomater Sci Polym Ed 13:651–665Google Scholar
  59. 59.
    Tokiwa Y, Calabia BP, Ugwu CU, Aiba S (2009) Biodegradability of plastics. Int J Mol Sci 10:3722–3742Google Scholar
  60. 60.
    Ahmed M, Ghanbari H, Cousins BG, Hamilton G, Seifalian AM (2011) Small calibre polyhedral oligomeric silsesquioxane nanocomposite cardiovascular grafts: influence of porosity on the structure, haemocompatibility and mechanical properties. Acta Biomater 7:3857–3867Google Scholar
  61. 61.
    Kannan RY, Salacinski HJ, De Groot J, Clatworthy I, Bozec L, Horton M et al (2006a) The antithrombogenic potential of a polyhedral oligomeric silsesquioxane (POSS) nanocomposite. Biomacromolecules 7:215–223Google Scholar
  62. 62.
    Kannan RY, Salacinski HJ, Odlyha M, Butler PE, Seifalian AM (2006b) The degradative resistance of polyhedral oligomeric silsesquioxane nanocore integrated polyurethanes: an in vitro study. Biomaterials 27(9):1971Google Scholar
  63. 63.
    Xie X, Eberhart A, Guidoin R, Marois Y, Douville Y, Zhang Z (2010) Five types of polyurethane vascular grafts in dogs: the importance of structural design and material selection. J Biomater Sci Polym Ed 21:1239–1264Google Scholar
  64. 64.
    McGill DB, Motto JD (1974) An industrial outbreak of toxic hepatitis due to methylenedianiline. N Engl J Med 291:278–282Google Scholar
  65. 65.
    Spark JI, Yeluri S, Derham C, Wong YT, Leitch D (2008) Incomplete cellular depopulation may explain the high failure rate of bovine ureteric grafts. Br J Surg 95(5):582Google Scholar
  66. 66.
    Chen FM, An Y, Zhang R, Zhang M (2011) New insights into and novel applications of release technology for periodontal reconstructive therapies. J Control Release 149:92–110Google Scholar
  67. 67.
    Tiruvannamalai-Annamalai R, Armant DR, Matthew HW (2014) A glycosaminoglycan based, modular tissue scaffold system for rapid assembly of perfusable, high cell density, engineered tissues. PLoS One 9:e84287Google Scholar
  68. 68.
    Cui H, Liu Y, Deng M, Pang X, Zhang P, Wang X et al (2012) Synthesis of biodegradable and electroactive tetraaniline grafted poly(ester amide) copolymers for bone tissue engineering. Biomacromolecules 13(9):2881Google Scholar
  69. 69.
    Yildirimer L, Thanh NTK, Seifalian AM (2012) Skin regeneration scaffolds: a multimodal bottom-up approach. Trends Biotechnol 30(12):638–648Google Scholar
  70. 70.
    de Mel A, Bolvin C, Edirisinghe M, Hamilton G, Seifalian AM (2008) Development of cardiovascular bypass grafts: endothelialization and applications of nanotechnology. Expert Rev Cardiovasc Ther 6:1259–1277Google Scholar
  71. 71.
    Ghanbari H, Viatge H, Kidane AG, Burriesci G, Tavakoli M, Seifalian AM (2009) Polymeric heart valves: new materials, emerging hopes. Trends Biotechnol 27:359–367Google Scholar
  72. 72.
    Salacinski HJ, Hamilton G, Seifalian AM (2003) Surface functionalization and grafting of heparin and/or RGD by an aqueous-based process to a poly(carbonate-urea)urethane cardiovascular graft for cellular engineering applications. J Biomed Mater Res A 66:688–697Google Scholar
  73. 73.
    Kannan RY, Salacinski HJ, Butler PE, Seifalian AM (2005) Artificial nerve conduits in peripheral nerve repair. Biotechnol Appl Biochem 41:193–200Google Scholar
  74. 74.
    Pabari A, Yang SY, Mosahebi A, Seifalian AM (2011) Recent advances in artificial nerve conduit design: strategies for the delivery of luminal fillers. J Control Release 156:2–10Google Scholar
  75. 75.
    Sedaghati T, Yang SY, Mosahebi A, Alavijeh MS, Seifalian AM (2011) Nerve regeneration with aid of nanotechnology and cellular engineering. Biotechnol Appl Biochem 58:288–300Google Scholar
  76. 76.
    Tan A, Rajadas J, Seifalian AM (2012) Biochemical engineering nerve conduits using peptide amphiphiles. J Control Release 163:342–352Google Scholar
  77. 77.
    Proksch P, Edrada RA, Ebel R (2002) Drugs from the seas – current status and microbiological implications. Appl Microbiol Biotechnol 59:125–134Google Scholar
  78. 78.
    Boettger D, Hertweck C (2013) Molecular diversity sculpted by fungal PKS-NRPS hybrids. Chembiochem 14:28–42Google Scholar
  79. 79.
    Debashish G, Malay S, Barindra S, Joydeep M (2005) Marine enzymes. Adv Biochem Eng Biotechnol 96:189–218Google Scholar
  80. 80.
    Zhang C, Kim SK (2010) Research and application of marine microbial enzymes: status and prospects. Mar Drugs 8:1920–1934Google Scholar
  81. 81.
    Gribble GW (2004) Amazing organohalogens. Am Sci 92:342–349Google Scholar
  82. 82.
    Butler A, Walker JV (1993) Marine haloperoxidases. Chem Rev 93:1937–1944Google Scholar
  83. 83.
    Carter-Franklin JN, Butler A (2004) Vanadium bromoperoxidase-catalyzed biosynthesis of halogenated marine natural products. J Am Chem Soc 126:15060–15066Google Scholar
  84. 84.
    Barindra S, Debashish G, Malay S, Joydeep M (2006) Purification and characterization of a salt, solvent, detergent and bleach tolerant protease from a new gamma-Proteobacterium isolated from the marine environment of the Sundarbans. Process Biochem 41(1):208–215Google Scholar
  85. 85.
    Stoll GH, Nimmerfall F, Acemoglu M, Bodmer D, Bantle S, Muller I, Mahl A, Kolopp M, Tullberg K (2001) Poly(ethylene carbonate)s: part II. Degradation mechanisms and parenteral delivery of bioactive agents. J Control Release 76:209–225Google Scholar
  86. 86.
    Kokubo T, Kim HM, Kawashita M (2003) Novel bioactive materials with different mechanical properties. Biomaterials 24:2161–2175Google Scholar
  87. 87.
    Hu Y, Catchmark JM (2011) In vitro biodegradability and mechanical properties of bioabsorbable bacterial cellulose incorporating cellulases. Acta Biomater 7:2835–2845Google Scholar
  88. 88.
    Labow RS, Duguay DG, Santerre JP (1994) The enzymatic hydrolysis of a synthetic biomembrane: a new substrate for cholesterol and carboxyl esterases. J Biomater Sci Polym Ed 6:169–179Google Scholar
  89. 89.
    Shalaby WSW, Chen M, Park K (1992) Mechanistic assessment of enzyme-induced degradation of albumin-crosslinked hydrogels. J Bioact Compat Polym 7:257–274Google Scholar
  90. 90.
    Tang YW, Labow RS, Santerre JP (2003) Enzyme induced biodegradation of polycarbonate-polyurethanes: dose dependence effect of cholesterol esterase. Biomaterials 24:2003–2011Google Scholar
  91. 91.
    Jahangir R, McCloskey CB, McClung WG, Labow RS, Brash JL, Santerre JP (2003) The influence of protein adsorption and surface modifying macromolecules on the hydrolytic degradation of a poly(ether–urethane) by cholesterol esterase. Biomaterials 24:121–130Google Scholar
  92. 92.
    Christenson EM, Patel S, Anderson JM, Hiltner A (2006) Enzymatic degradation of poly(ether urethane) and poly(carbonate urethane) by cholesterol esterase. Biomaterials 27:3920–3926Google Scholar
  93. 93.
    Finer Y, Jaffer F, Santerre JP (2004) Mutual influence of cholesterol esterase and pseudocholinesterase on the biodegradation of dental composites. Biomaterials 25:1787–1793Google Scholar
  94. 94.
    Azevedo HS, Reis RL (2009) Encapsulation of α-amylase into starch-based biomaterials: an enzymatic approach to tailor their degradation rate. Acta Biomater 5:3021–3030Google Scholar

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Authors and Affiliations

  1. 1.Department of Mechanical and Biomedical EngineeringCity University of Hong KongKowloonHong Kong

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