252
Views
2
CrossRef citations to date
0
Altmetric
Research Articles

Fine-tuned preparation of cross-linked laccase nanoaggregates

ORCID Icon & ORCID Icon
Pages 431-447 | Received 21 Nov 2018, Accepted 24 Mar 2019, Published online: 08 May 2019

References

  • Arsenault A, Cabana H, Jones JP. 2011. Laccase-based CLEAs: chitosan as a novel cross-linking agent. Enzyme Res. 2011:376015.
  • Ba S, Arsenault A, Hassani T, Jones JP, Cabana H. 2013. Laccase immobilization and insolubilization: from fundamentals to applications for the elimination of emerging contaminants in wastewater treatment. Crit Rev Biotechnol. 33:404–418. DOI:10.3109/07388551.2012.725390
  • Barrios-Estrada C, de Jesús Rostro-Alanis M, Muñoz-Gutiérrez BD, Iqbal HMN, Kannan S, Parra-Saldívar R. 2018. Emergent contaminants: endocrine disruptors and their laccase-assisted degradation - A review. Sci Total Environ. 612:1516–1531.
  • Bell DJ, Heywood‐Waddington D, Hoare M, Dunnill P. 1982. The density of protein precipitates and its effect on centrifugal sedimentation. Biotechnol Bioeng. 24:127–141. DOI:10.1002/bit.260240111
  • Berman HM, Westbrook Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov I, Bourne PE. 2000. The Protein Data Bank. Nucleic Acids Res. 122:339–347.
  • Bertrand B, Martínez-Morales F, Tinoco-Valencia R, Rojas S, Acosta-Urdapilleta L, Trejo-Hernández MR. 2015. Biochemical and molecular characterization of laccase isoforms produced by the white-rot fungus Trametes versicolor under submerged culture conditions. J Mol Catal B Enzym. 122:339–347.
  • Bertrand T, Jolivalt C, Briozzo P, Caminade E, Joly N, Madzak C, Mougin C. 2002. Crystal structure of a four-copper laccase complexed with an arylamine: insights into substrate recognition and correlation with kinetics. Biochemistry. 41:7325–7333.
  • Bilal M, Zhao Y, Rasheed T, Iqbal H. 2018. Magnetic nanoparticles as versatile carriers for enzymes immobilization: a review. Int J Biol Macromol. 120:2530–2544.
  • Boutureira O, Bernardes G. 2015. Advances in chemical protein modification. Chem Rev. 115:2174–2195.
  • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 72:248–254.
  • Bujacz A. 2012. Structures of bovine, equine and leporine serum albumin. Acta Crystallogr D Biol Crystallogr. 68:1278–1289.
  • Bujacz A, Zielinski K, Sekula B. 2014. Structural studies of bovine, equine, and leporine serum albumin complexes with naproxen. Proteins Bioinforma. 82:2199–2208.
  • Cabana H, Jones JP, Agathos SN. 2007. Preparation and characterization of cross-linked laccase aggregates and their application to the elimination of endocrine disrupting chemicals. J Biotechnol. 132:23–31.
  • Cao S, Xu P, Ma Y, Yao X, Yao Y, Zong M, Li X, Lou W. 2016. Recent advances in immobilized enzymes on nanocarriers. Cuihua Xuebao/Chinese J Catal. 37:1814–1823.
  • Chen J, Zhang J, Han B, Li Z, Li J, Feng X. 2006. Synthesis of cross-linked enzyme aggregates (CLEAs) in CO 2-expanded micellar solutions. Coll Surf B Biointerfaces. 48:72–76.
  • Choi JM, Han SS, Kim HS. 2015. Industrial applications of enzyme biocatalysis: current status and future aspects. Biotechnol Adv. 33:1443–1454.
  • Cipolatti EP, Silva MJA, Klein M, Feddern V, Feltes MMC, Oliveira JV, Ninow JL, de Oliveira D. 2014. Current status and trends in enzymatic nanoimmobilization. J Mol Catal B Enzym. 99:56–67.
  • Ekici S, Saraydin D. 2004. Synthesis, characterization and evaluation of IPN hydrogels for antibiotic release. Drug Deliv. 11:381–388.
  • Erden E, Ucar MC, Kaymaz Y, Pazarlioglu NK. 2009. New and different lignocellulosic materials from Turkey for laccase and manganese peroxidase production by Trametes versicolor. Eng Life Sci [Internet] 9:60–65. DOI:10.1002/elsc.200700025
  • Fathali Z, Rezaei S, Faramarzi MA, Habibi-Rezaei M. 2019. Catalytic phenol removal using entrapped cross-linked laccase aggregates. Int J Biol Macromol. 122:359–366.
  • Fernández-Fernández M, Sanromán MÁ, Moldes D. 2013. Recent developments and applications of immobilized laccase. Biotechnol Adv. 31:1808–1825.
  • Fischer H, Polikarpov I, Craievich AF. 2009. Average protein density is a molecular-weight-dependent function. Protein Sci. 13:2825–2828.
  • Galisteo-González F, Molina-Bolívar JA. 2014. Systematic study on the preparation of BSA nanoparticles. Coll Surf B Biointerfaces. 123:286–292.
  • Garcia-Galan C, Berenguer-Murcia Á, Fernandez-Lafuente R, Rodrigues RC. 2011. Potential of different enzyme immobilization strategies to improve enzyme performance. Adv Synth Catal. 353:2885–2904.
  • Guzik U, Hupert-Kocurek K, Wojcieszyńska D. 2014. Immobilization as a strategy for improving enzyme properties- Application to oxidoreductases. Molecules. 19:8995–9018.
  • Hegedús I, Hancsók J, Nagy E. 2012. Stabilization of the cellulase enzyme complex as enzyme nanoparticle. Appl Biochem Biotechnol. 168:1372–1383.
  • Hegedus I, Nagy E. 2009. Improvement of chymotrypsin enzyme stability as single enzyme nanoparticles. Chem Eng Sci. 64:1053–1060.
  • Homaei AA, Sariri R, Vianello F, Stevanato R. 2013. Enzyme immobilization: an update. J Chem Biol. 6:185–205.
  • Humphrey W, Dalke A, Schulten K. 1996. VMD: Visual molecular dynamics. J Mol Graph. 14:33–38.
  • Iimura Y, Sonoki T, Habe H. 2018. Heterologous expression of Trametes versicolor laccase in Saccharomyces cerevisiae. Protein Expr Purif. 141:39–43.
  • Johnson T. 1985. Aldehyde fixatives: quantification of acid‐producing reactions. J Elec Microsc Tech. 2:129–138.
  • Kamaly N, Yameen B, Wu J, Farokhzad OC. 2016. Degradable controlled-release polymers and polymeric nanoparticles: mechanisms of controlling drug release. Chem Rev. 116:2602–2663. DOI:10.1021/acs.chemrev.5b00346
  • Kartal F, Janssen MHA, Hollmann F, Sheldon RA, Kılınc A. 2011. Improved esterification activity of Candida rugosa lipase in organic solvent by immobilization as Cross-linked enzyme aggregates (CLEAs). J Mol Catal B Enzym. 71:85–89.
  • Kumar VV, Sivanesan S, Cabana H. 2014. Magnetic cross-linked laccase aggregates - Bioremediation tool for decolorization of distinct classes of recalcitrant dyes. Sci Total Environ. 487:830–839.
  • Laskowski RA. 2001. PDBsum: summaries and analyses of PDB structures. Nucleic Acids Res. 29:221–222. DOI:10.1093/nar/29.1.221
  • Lechner H, Ferruz N, Höcker B. 2018. Strategies for designing non-natural enzymes and binders. Curr Opin Chem Biol. 47:67–76.
  • Li, F-Q, Su, H, Wang, J, Liu, J-Y, Zhu, Q-G, Fei, Y-B, Pan, Y-H, Hu, J-H. 2008. Preparation and characterization of sodium ferulate entrapped bovine serum albumin nanoparticles for liver targeting. Int  J Pharm349:274–282. DOI:10.1016/j.ijpharm.2007.08.001
  • Liu Q, Xun G, Feng Y. 2018. The state-of-the-art strategies of protein engineering for enzyme stabilization. Biotechnol Adv. DOI:10.1016/j.biotechadv.2018.10.011
  • Lu M, Zhao C, Wang Q, You G, Wang Y, Deng H, Chen G, Xia S, Zhao J, Wang B, et al. 2016. Colloids and surfaces B : biointerfaces preparation, characterization and in vivo investigation of blood-compatible hemoglobin-loaded nanoparticles as oxygen carriers. Coll Surf B Biointerfaces. 139:171–179.
  • Majorek KA, Porebski PJ, Dayal A, Zimmerman MD, Jablonska K, Stewart AJ, Chruszcz M, Minor W. 2012. Structural and immunologic characterization of bovine, horse, and rabbit serum albumins. Mol Immunol. 52:174–182.
  • Mate DM, Alcalde M. 2015. Laccase engineering: from rational design to directed evolution. Biotechnol Adv. 33:25–40.
  • Mateo C, Palomo JM, Van Langen LM, Van Rantwijk F, Sheldon RA. 2004. A new, mild cross-linking methodology to prepare cross-linked enzyme aggregates. Biotechnol Bioeng. 86:273–276.
  • Matijošyte I, Arends I, de Vries S, Sheldon RA. 2010. Preparation and use of cross-linked enzyme aggregates (CLEAs) of laccases. J Mol Catal B Enzym. 62:142–148.
  • McWilliam H, Li W, Uludag M, Squizzato S, Park YM, Buso N, Cowley AP, Lopez R. 2013. Analysis tool web services from the EMBL-EBI. Nucleic Acids Res. 41:W597–W600. DOI:10.1093/nar/gkt376
  • Migneault I, Dartiguenave C, Bertrand MJ, Waldron KC. 2004. Glutaraldehyde: behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking. Biotechniques. 37:790–802.
  • Mongay C, Cerda V. 1974. A Britton-Robinson buffer of known ionic strength. Ann Chim. 64:409–412.
  • Morozova OV, Shumakovich GP, Shleev SV, Yaropolov YI. 2007. Laccase-mediator systems and their applications: a review. Appl Biochem Microbiol. 43:523–535.
  • Nguyen LT, Seow N, Yang KL. 2017. Hollow cross-linked enzyme aggregates (h-CLEA) of laccase with high uniformity and activity. Coll Surf B Biointerfaces. 151:88–94.
  • Nunes CS, Kunamneni A. 2018. Laccases—properties and applications. In: Nunes CS, Kumar V, editors. Enzymes in Human and Animal Nutrition. Cambridge (MA): Academic Press; p. 133–161. DOI:10.1016/B978-0-12-805419-2.00007-1
  • Okay O, Lozinsky VI. 2014. Synthesis and structure–property relationships of cryogels. Adv Polym Sci. 263:103–157.
  • Oldfield C. 1994. Enzymes in water-in-oil microemulsions (‘Reversed Micelles’): principles and applications. Biotechnol Genet Eng Rev. 12:255–327.
  • Paik SYR, Nguyen HH, Ryu J, Che JH, Kang TS, Lee JK, Song CW, Ko S. 2013. Robust size control of bovine serum albumin (BSA) nanoparticles by intermittent addition of a desolvating agent and the particle formation mechanism. Food Chem. 141:695–701.
  • Peng ZG, Hidajat K, Uddin MS. 2004. Adsorption of bovine serum albumin on nanosized magnetic particles. J Coll Interf Sci. 271:277–283.
  • Piontek K, Antorini M, Choinowski T. 2002. Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-?? resolution containing a full complement of coppers. J Biol Chem. 277:37663–37669.
  • Roberts E, Eargle J, Wright D, Luthey-Schulten Z. 2006. MultiSeq: unifying sequence and structure data for evolutionary analysis. BMC Bioinformatics. 7:382.
  • Rodrigues RC, Ortiz C, Berenguer-Murcia Á, Torres R, Fernández-Lafuente R. 2013. Modifying enzyme activity and selectivity by immobilization. Chem Soc Rev. 42:6290–6307.
  • Schoevaart R, Wolbers MW, Golubovic M, Ottens M, Kieboom APG, Van Rantwijk F, Van Der Wielen LAM, Sheldon RA. 2004. Preparation, optimization, and structures, of cross-linked enzyme aggregates (CLEAs). Biotechnol Bioeng. 87:754–762.
  • Sekula B, Zielinski K, Bujacz A. 2013. Crystallographic studies of the complexes of bovine and equine serum albumin with 3,5-diiodosalicylic acid. Int J Biol Macromol. 60:316–324.
  • Senthivelan T, Kanagaraj J, Panda RC. 2016. Recent trends in fungal laccase for various industrial applications: an eco-friendly approach - A review. Biotechnol Bioproc E.E. 21:19–38.
  • Sezgintürk MK, Odaci D, Pazarlioğlu N, Pilloton R, Dinçkaya E, Telefoncu A, Timur S. 2010. Construction and comparison of trametes versicolor laccase biosensors capable of detecting xenobiotics. Artif Cells Blood Subs Biotechnol. 38:192–199.
  • Shamlou PA. 1993. Processing of Solid-Liquid Suspensions. Oxford: Butterworth-Heinemann, p. 338.
  • Sheldon RA. 2007. Enzyme immobilization: the quest for optimum performance. Adv Synth Catal. Catal. 349:1289–1307.
  • Sheldon RA. 2011. Cross-linked enzyme aggregates as industrial biocatalysts. Org Process Res Dev. 15:213–223.
  • Sheldon RA, Sorgedrager MJ, Kondors B. 2013. Non-leachable magnetic cross-linked enzyme aggregate. 1:5.
  • Smith PK, Krohn RI, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, Klenk DC. 1985. Measurement of protein using bicinchoninic acid. Anal Biochem. 150:76–85.
  • Solanki K, Gupta MN, Halling PJ. 2012. Examining structure–activity correlations of some high activity enzyme preparations for low water media. Bioresour Technol. 115:147–151.
  • Sóti V, Lenaerts S, Cornet I. 2018. Of enzyme use in cost-effective high solid simultaneous saccharification and fermentation processes. J Biotechnol. 270:70–76.
  • Sundar, S, Kundu, J, Kundu, SC. 2010. Biopolymeric nanoparticles. Sci Technol Adv Mater11:014104. DOI:10.1088/1468-6996/11/1/014104
  • Talekar S, Joshi A, Joshi G, Kamat P, Haripurkar R, Kambale S. 2013. Parameters in preparation and characterization of cross linked enzyme aggregates (CLEAs). RSC Adv. 3:12485.
  • Taralp A. 2014. Crosslinked protein nanocrystals, crosslinked protein nanoaggregates and method of preparation thereof [Internet] 14. https://encrypted.google.com/patents/US8716219
  • Toral AR, de los Ríos AP, Hernández FJ, Janssen MHA, Schoevaart R, van Rantwijk F, Sheldon RA. 2007. Cross-linked Candida antarctica lipase B is active in denaturing ionic liquids. Enzyme Microb Technol. 40:1095–1099.
  • Vinoth Kumar V, Prem Kumar MP, Thiruvenkadaravi KV, Baskaralingam P, Senthil Kumar P, Sivanesan S. 2012. Preparation and characterization of porous cross linked laccase aggregates for the decolorization of triphenyl methane and reactive dyes. Bioresour Technol. 119:28–34.
  • Vlasova IM, Vlasov AA, Grapendaal GR, Saletskii AM. 2018. Association constants in the bovine serum albumin/human serum albumin–tween 20 system in aqueous solutions. Russ J Phys Chem. 92:714–718.
  • Winsor PA. 1956. Solvent properties of amphiphilic compounds. London: Butterworths Scientific Publications. DOI:10.1002/lipi.19560581222
  • Yang J, Xu X, Yang X, Ye X, Lin J. 2016. Cross-linked enzyme aggregates of Cerrena laccase: preparation, enhanced nacl tolerance and decolorization of remazol brilliant blue reactive. J Taiwan Inst Chem Eng. 65:1–7.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.