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Use of micro- and ultrafiltration membranes for concentration of laccase-rich enzymatic extract of Pleurotus sajor-caju PS-2001 and application in dye decolorization

  • Simone ZaccariaEmail author
  • Nicole Amanda Boff
  • Fernanda Bettin
  • Aldo José Pinheiro Dillon
Original Paper

Abstract

In the present work, studies of laccase-rich enzymatic extract pretreatment were carried out using granulated activated carbon and/or microfiltration (polyimide hollow fiber membrane, 0.4 µm pore size) prior to ultrafiltration (polyether sulfone spiral membrane, 10 kDa cut-off). Concentration by ultrafiltration without any pretreatment resulted in superior recovery percentage (141%), but under low permeate flow (20 L m−2 h−1) and longer process time. Conversely, a protocol comprising both pretreatments resulted in moderately inferior recovery (109%) and rather higher permeate flux. In order to effectively concentrate about 110 L laccase crude broth, only the microfiltration pretreatment was used, once it decreases overall process time and cost. Volumetric concentration up to a factor of 60 times was obtained, with an enzyme recovery percentage of 183% and an activity concentration factor of 102, producing an extract with laccase activity of ca. 3033 U mL−1. Reaction mixtures containing 150 U mL−1 laccase activity from concentrated enzymatic extracts, associated with 0.3 µmol L−1 mediator syringaldazine granted decolorization percentages of approximately 75% for brilliant green, 68% for acid blue 80 and 52% for reactive red 198.

Keywords

Laccase Activated carbon Microfiltration Ultrafiltration Mediators 

Notes

Acknowledgements

This work was supported by Fundação de Amparo à Pesquisa do Estado do Rio Grande do Sul (FAPERGS, Brazil) and Coordenadoria de Aperfeiçoamento de Pessoal de Nível Superior (CAPES, Brazil).

References

  1. Bagewadi ZK, Mulla SI, Ninnekar HZ (2017) Purification and immobilization of laccase from Trichoderma harzianum strain HZN10 and its application in dye decolorization. J Genet Eng Biotechnol 15:139–150CrossRefGoogle Scholar
  2. Bettin F, Rosa LO, Montanari Q, Calloni R, Gaio TA, Malvessi E, Silveira MM, Dillon AJP (2011) Growth, kinetics, production, and characterization of extracellular laccases from Pleurotus sajor-caju PS-2001. Process Biochem 46:758–764CrossRefGoogle Scholar
  3. Bettin F, Montanari Q, Calloni R, Gaio TA, Silveira MM, Dillon AJP (2014) Additive effects of CuSO4 and aromatic compounds on laccase production by Pleurotus sajor-caju PS-2001 using sucrose as a carbon source. Braz J Chem Eng 31:335–346CrossRefGoogle Scholar
  4. Bradford MM (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254CrossRefGoogle Scholar
  5. Bryjak J, Rekuć A (2010) Effective purification of Cerrena unicolor laccase using microfiltration, ultrafiltration and acetone precipitation. Appl Biochem Biotechnol 160:2219–2235CrossRefGoogle Scholar
  6. Cheryan M (1998) Ultrafiltration and microfiltration handbook, 2nd edn. CRC Press, Boca RatonCrossRefGoogle Scholar
  7. Gottschalk LMF, Bon EPS, Nobrega R (2008) Lignin peroxidase from Streptomyces viridosporus T7A: enzyme concentration using ultrafiltration. Appl Biochem Biotechnol 147:23–32CrossRefGoogle Scholar
  8. Kurniawati S, Nicell JA (2008) Characterization of Trametes versicolor laccase for the transformation of aqueous phenol. Bioresour Technol 99:7825–7834CrossRefGoogle Scholar
  9. Lütz S, Rao NN, Wandrey C (2006) Membranes in biotechnology. Chem Eng Technol 12:1404–1415CrossRefGoogle Scholar
  10. Mandels M, Reese ET (1957) Induction of cellulase in Trichoderma viride as influenced by carbon source and metals. J Bacteriol 73:269–278Google Scholar
  11. Nakkeeran E, Subramanian R, Umesh-Kumar S (2010) Purification of polygalacturonase from solid-state cultures of Aspergillus carbonarius. J Biosci Bioeng 109:101–106CrossRefGoogle Scholar
  12. Poletto P, Renosto DR, Baldasso C, Zeni M, Silveira MM (2015a) Activated charcoal and microfiltration as pretreatment before ultrafiltration of pectinases produced by Aspergillus niger in solid-state cultivation. Sep Purif Technol 151:102–107CrossRefGoogle Scholar
  13. Poletto P, Borsói C, Zeni M, Silveira MM (2015b) Downstream processing of pectinase produced by Aspergillus niger in solid state cultivation and its application to fruit juices clarification. Food Sci. Technol 35(2):391–397CrossRefGoogle Scholar
  14. Rajeeva S, Lele SS (2010) Bioprocessing of laccase produced by submerged culture of Ganoderma sp. WR-1. Sep Purif Technol 76:110–119CrossRefGoogle Scholar
  15. Rancaño G, Lorenzo M, Molares N, Couto SR, Sanromán MA (2003) Production of laccase by Trametes versicolor in an airlift fermentor. Process Biochem 39:467–473CrossRefGoogle Scholar
  16. Riva S (2006) Laccases: blue enzymes for green chemistry. Trends Microbiol 24:221–226Google Scholar
  17. Schliephake K, Mainwaring DE, Lonergan GT, Jones IK, Baker WL (2000) Transformation and degradation of the disazo dye Chicago Sky Blue by a purified laccase from Pycnoporus cinnabarinus. Enzyme Microb Technol 27:100–107CrossRefGoogle Scholar
  18. Schmitt S, Souza R, Bettin F, Dillon AJP, Valle JAB, Andreaus J (2012) Decolorization of aqueous solutions of disperse textile dyes by oxidoreductases. Biocatal Biotransform 30:48–56CrossRefGoogle Scholar
  19. Silva D, Martins ES, Leite RSR, Silva R, Ferreira V, Gomes E (2007) Purification and characterization of an exo-polygalacturonase produced by Penicillium viridicatum RFC3 in solid-state fermentation. Process Biochem 42:1237–1243CrossRefGoogle Scholar
  20. Songulashvili G, Flahaut S, Demarez M, Tricot C, Bauvois C, Debaste F, Penninckx MJ (2016) High yield production in seven days of Coriolopsis gallica 1184 laccase at 50 L scale; enzyme purification and molecular characterization. Fungal Biol 120:481–488CrossRefGoogle Scholar
  21. Viswanath B, Rajesh B, Janardhan A, Kumar AP, Narasimha G (2014) Fungal laccases and their applications in bioremediation. Enzyme Res 2014:1–21CrossRefGoogle Scholar
  22. Wolfenden RS, Willson RL (1982) Radical-cations as reference chromogens in the kinetic studies of one-electron transfer reactions: pulse radiolysis studies of 2,2′-azinobis-(3-ethylbenzthiazoline-6-sulphonate). J Chem Soc Perkin Trans II 02:805–812CrossRefGoogle Scholar
  23. Yang Y, Ding Y, Liao X, Cai Y (2013) Purification and characterization of a new laccase from Shiraia sp. SUPER-H168. Process Biochem 48:351–357CrossRefGoogle Scholar

Copyright information

© Institute of Chemistry, Slovak Academy of Sciences 2019

Authors and Affiliations

  1. 1.Laboratory of Enzymes and Biomasses, Institute of BiotechnologyUniversity of Caxias do SulCaxias do SulBrazil

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