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dc.contributor.authorBarriuso, Jorgees_ES
dc.contributor.authorVaquero, María Eugeniaes_ES
dc.contributor.authorPrieto, Aliciaes_ES
dc.contributor.authorMartínez, María Jesúses_ES
dc.date.accessioned2016-09-20T12:29:55Z-
dc.date.available2016-09-20T12:29:55Z-
dc.date.issued2016-09-
dc.identifier.citationBiotechnology Advances 34 (5) 874–885 (2016 )es_ES
dc.identifier.issn0734-9750-
dc.identifier.urihttp://hdl.handle.net/10261/137065-
dc.description32 p.-4 fig.-1 tab.es_ES
dc.description.abstractLipases and sterol esterases are enzymes with broad biotechnological applications, which catalyze the hydrolysis or synthesis of long-chain acylglycerols and sterol esters, respectively. In this paper, we review the current knowledge on the so-called Candida rugosa-like family of enzymes, whose members display in most cases affinity against the two substrates mentioned above. The family includes proteins with the α/β-hydrolase folding, sharing conserved motifs in their sequences, and common structural features. We will go through their production and purification, relate their described structures and catalytic activity, and discuss the influence of the hydrophobic character of these lipases on their aggregation state and activity. On the basis of the few crystal structures available, the role of each of the functional areas in catalysis will be analyzed. Considering the particular characteristics of this group, we propose their classification as “Versatile Lipases” (EC 3.1.1.x).es_ES
dc.description.sponsorshipThis work was supported by the Spanish projects BIO2012-36372, BIO2015-68387-R, RTC-2014-1777-3 from MINECO and S2013/MAE-2972 from Comunidad de Madrid.es_ES
dc.language.isoenges_ES
dc.publisherElsevieres_ES
dc.relation.isversionofPostprintes_ES
dc.rightsopenAccessen_EN
dc.subjectLipasees_ES
dc.subjectSterol-esterasees_ES
dc.subjectCandida rugosaes_ES
dc.subjectBiocatalystses_ES
dc.subjectHydrophobic enzymeses_ES
dc.titleStructural traits and catalytic versatility of the lipases from the Candida rugosa-like family: A reviewes_ES
dc.typeartículoes_ES
dc.identifier.doi10.1016/j.biotechadv.2016.05.004-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1016/j.biotechadv.2016.05.004es_ES
dc.identifier.e-issn1873-1899-
dc.embargo.terms2017-09-20es_ES
dc.rights.licensehttp://creativecommons.org/licenses/by-nc-nd/4.0/-
dc.contributor.funderMinisterio de Economía y Competitividad (España)es_ES
dc.contributor.funderComunidad de Madrides_ES
dc.relation.csices_ES
oprm.item.hasRevisionno ko 0 false*
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
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