Purification and characterization of two thermostable laccases from Pycnoporus sanguineus and potential role in degradation of endocrine disrupting chemicals

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dc.creatorRaúl García Morales
dc.creatorNancy Edith Ornelas Soto
dc.creatorDiana Linda Cárdenas Chávez
dc.creatorRoberto Parra Saldivar
dc.date2014
dc.date.accessioned2018-10-18T22:08:27Z
dc.date.available2018-10-18T22:08:27Z
dc.descriptionIn this study, the purification and characterization of two thermostable laccases produced by Pycnoporus sanguineus CS43 (LacI and LacII) were performed. Also, their biotechnological potential was assessed through the degradation of endocrine disrupting chemicals (EDCs). Laccases were purified by ultrafiltration, ion exchange (IEX) and hydrophobic interaction chromatography achieving specific activities close to 285 U mg-1. The molecular weights of LacI and LacII, determined by SDS-electrophoresis, were 68 and 66 kDa, respectively. Both laccases showed high amino acid sequence similarity (91%) between them and high thermostability, at 50 and 60 °C (half-lives of 277.7 and 18 h for LacI, 35.8 and 2.25 h for LacII). The isoforms oxidized common laccase substrates such as 2,2′-azino-bis (3-ethylbenzthiazoline-6- sulfonate (ABTS), 2,6-dimethoxyphenol (DMP) and guaiacol at acidic pH conditions. ABTS was the most efficient substrate, showing high specificity constants of 74,816 and 36,746 mM-1 s-1 for Lac I and LacII, and Michaelis constants (Km) of 6.9 and 12.2 μM respectively at pH 3. Both purified laccases remained active at high concentrations of organic solvents (acetonitrile, ethanol and acetone), with an IC50 (v/v) of >64%, 55% and 47% for LacI, and 33%, 52% and 31% for LacII, respectively. LacI and LacII were tested to degrade EDCs, nonylphenol and triclosan, with more than 95% removal after 8 h of treatment with 100 U/L at pH 5 as determined by means of HPLC. The high thermostability, unique Michaelis-Menten kinetic parameters, and organic solvent tolerance demonstrated for the isoforms produced by P. sanguineus CS43 render them promising candidates for industrial applications. LacI exerted a higher thermal and pH stability, tolerance against inhibitors and was a more efficient catalyst for ABTS and DMP than LacII. © 2014 The Authors.
dc.identifier.doi10.1016/j.molcatb.2014.06.006
dc.identifier.endpage42
dc.identifier.issn13811177
dc.identifier.startpage32
dc.identifier.urihttp://hdl.handle.net/11285/630585
dc.identifier.volume108
dc.languageeng
dc.publisherElsevier
dc.relationhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84904344133&doi=10.1016%2fj.molcatb.2014.06.006&partnerID=40&md5=f7e0ae7b8cb9cb4c365c1bc10c1c8dcb
dc.relationInvestigadores
dc.relationEstudiantes
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0
dc.sourceJournal of Molecular Catalysis B: Enzymatic
dc.subjectAcetone
dc.subjectAmino acids
dc.subjectCharacterization
dc.subjectChemicals
dc.subjectElectrophoresis
dc.subjectEndocrine disrupters
dc.subjectIndustrial applications
dc.subjectLiquid chromatography
dc.subjectOrganic solvents
dc.subjectpH effects
dc.subjectPurification
dc.subjectStability
dc.subjectSubstrates
dc.subjectBiotechnological potentials
dc.subjectEndocrine disrupting chemicals
dc.subjectHydrophobic interaction chromatography
dc.subjectLaccases
dc.subjectMichaelis-Menten kinetic
dc.subjectOrganic solvent tolerance
dc.subjectPycnoporus sanguineus
dc.subjectThermostability
dc.subjectEnzymes
dc.subjectendocrine disruptor
dc.subjectlaccase
dc.subjectamino acid sequence
dc.subjectaqueous solution
dc.subjectarticle
dc.subjectbinding affinity
dc.subjectbiodegradation
dc.subjectcatalyst
dc.subjectconcentration (parameters)
dc.subjectdeglycosylation
dc.subjectdegradation
dc.subjectenzyme activity
dc.subjectenzyme purification
dc.subjectGanoderma lucidum
dc.subjectglycosylation
dc.subjecthalf life time
dc.subjecthydrophobic interaction chromatography
dc.subjectIC 50
dc.subjectkinetics
dc.subjectMichaelis constant
dc.subjectmolecular weight
dc.subjectnonhuman
dc.subjectnucleotide sequence
dc.subjectpH
dc.subjectPycnoporus
dc.subjectPycnoporus sanguineus
dc.subjecttemperature
dc.subjectthermostability
dc.subjectTrametes hirsuta
dc.subjectwater treatment
dc.subject.classification7 INGENIERÍA Y TECNOLOGÍA
dc.titlePurification and characterization of two thermostable laccases from Pycnoporus sanguineus and potential role in degradation of endocrine disrupting chemicals
dc.typeArtículo
refterms.dateFOA2018-10-18T22:08:27Z

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