Cloning and characterisation of a cystathionine β/γ-lyase from two Oenococcus oeni oenological strains

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dc.contributor.authorKnoll C.
dc.contributor.authorDu Toit M.
dc.contributor.authorSchnell S.
dc.contributor.authorRauhut D.
dc.contributor.authorIrmler S.
dc.date.accessioned2011-05-15T15:56:35Z
dc.date.available2011-05-15T15:56:35Z
dc.date.issued2011
dc.description.abstractSulphur-containing compounds in wine have been extensively studied because of their effect on wine flavour and quality. In this study, an enzyme that degrades sulphur-containing amino acids was cloned and characterised from two Oenococcus oeni strains of oenological origins. The enzyme has features of a cystathionine-γ-lyase (EC 4.4.1.1), a pyridoxal-5-phosphate-dependent enzyme catalysing an α,γ-elimination reaction of l-cystathionine to produce l-cysteine, α-ketobutyrate and ammonia. Moreover, it was able to catalyse an α,β-elimination reaction producing homocysteine, pyruvate and ammonia from l-cystathionine. An elimination reaction of l-cysteine and dl-homocysteine was also efficiently catalysed by the enzyme, resulting in the formation of hydrogen sulphide. Furthermore, the ability to demethiolate methionine into methanethiol, an unfavourable volatile sulphur compound in terms of wine aroma, was observed. The findings of this work suggest that O. oeni seems to play a minor role in the production of volatile sulphur compounds during the vinification process as the optimal conditions were far from the harsh wine environment. © 2011 Springer-Verlag.
dc.description.versionArticle
dc.identifier.citationApplied Microbiology and Biotechnology
dc.identifier.citation89
dc.identifier.citation4
dc.identifier.issn1757598
dc.identifier.other10.1007/s00253-010-2911-x
dc.identifier.urihttp://hdl.handle.net/10019.1/9929
dc.subjectCatalyse
dc.subjectCharacterisation
dc.subjectCystathionine lyase
dc.subjectElimination reaction
dc.subjectHomocysteines
dc.subjectHydrogen sulphide
dc.subjectL-cysteine
dc.subjectMethanethiol
dc.subjectOenococcus oeni
dc.subjectOptimal conditions
dc.subjectPyridoxal 5 phosphates
dc.subjectPyruvates
dc.subjectVolatile sulphur compounds
dc.subjectWine aromas
dc.subjectAmino acids
dc.subjectAmmonia
dc.subjectChemical reactions
dc.subjectCloning
dc.subjectEnzymes
dc.subjectSulfur
dc.subjectSulfur compounds
dc.subjectWine
dc.subjectEnzyme activity
dc.subjectbacterial DNA
dc.subjectcystathionine beta lyase
dc.subjectcystathionine gamma lyase
dc.subjectpolyhistidine tag
dc.subjectsulfur
dc.subjectvolatile agent
dc.subjectamino acid
dc.subjectammonia
dc.subjectbacterium
dc.subjectcatalysis
dc.subjectclone
dc.subjectenzyme activity
dc.subjecthydrogen sulfide
dc.subjectmetabolite
dc.subjectqualitative analysis
dc.subjectsulfur
dc.subjectvolatile substance
dc.subjectarticle
dc.subjectbacterial gene
dc.subjectbacterial growth
dc.subjectbacterial strain
dc.subjectbacterium culture
dc.subjectDNA isolation
dc.subjectDNA sequence
dc.subjectenzyme activity
dc.subjectEscherichia coli
dc.subjectgas chromatography
dc.subjecthigh performance liquid chromatography
dc.subjectmolecular cloning
dc.subjectnonhuman
dc.subjectOenococcus oeni
dc.subjectprotein expression
dc.subjectprotein purification
dc.subjectsequence analysis
dc.subjectviniculture
dc.subjectOenococcus oeni
dc.titleCloning and characterisation of a cystathionine β/γ-lyase from two Oenococcus oeni oenological strains
dc.typeArticle
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