Phenylalanine ammonia lyase: new insights from Piperaceae species

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dc.contributor.authorde Araújo Morandim-Giannetti, Andreia
dc.contributor.authorFelippe, Lidiane Gaspareto [UNESP]
dc.contributor.authorde Freitas Formenton Macedo dos Santos, Vânia Aparecida [UNESP]
dc.contributor.authorKato, Massuo Jorge
dc.contributor.authorFurlan, Maysa [UNESP]
dc.contributor.institutionFEI University Center
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2023-07-29T14:12:36Z
dc.date.available2023-07-29T14:12:36Z
dc.date.issued2022-01-01
dc.description.abstractThe enzyme PAL (phenylalanine ammonia lyase) mediates the key entry point to the general phenylpropanoid pathway, which is involved in the lignification process and in the formation of a myriad of secondary compounds in plants that show a variety of biological activities. Soluble fractions containing PAL extracted from Piper and Peperomia species had the optimal catalytic activity analyzed by statistical design model. This analysis revealed that the best conversion of L-phenylalanine to trans-cinnamic acid was pH 9.3 and 58 °C after 25 h, corroborating interesting thermal stability. Additionally, the pre-purification of PAL using ammonium sulfate precipitation (25-55%) increased its specific activity, approximately 133% in P. aduncum and more than 900% in P. crassinervium. The content of lignin was higher for P. tuberculatum (25.71%), while only a small amount of lignin was observed in Peperomia blanda (11.95%). It is interesting to note that Peperomia plants are succulent and without significant amounts of lignin. However, the phenylpropanoid biosynthetic pathway is apparently addressed to produce predominantly tetrahydrofuran lignans with biological interest.en
dc.description.affiliationFEI University Center Department of Chemical Engeneering
dc.description.affiliationPaulista State University Institute of Chemistry
dc.description.affiliationUniversity of São Paulo Institute of Chemistry
dc.description.affiliationUnespPaulista State University Institute of Chemistry
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipIdFAPESP: 2013/07600-3
dc.description.sponsorshipIdCNPq: 2014/465637-0
dc.description.sponsorshipIdFAPESP: 2014/50926-0
dc.format.extent67-82
dc.identifierhttp://dx.doi.org/10.26850/1678-4618EQJ.V47.2SI.2022.P67-82
dc.identifier.citationEcletica Quimica, v. 47, p. 67-82.
dc.identifier.doi10.26850/1678-4618EQJ.V47.2SI.2022.P67-82
dc.identifier.issn1678-4618
dc.identifier.issn0100-4670
dc.identifier.scopus2-s2.0-85138593366
dc.identifier.urihttp://hdl.handle.net/11449/249186
dc.language.isoeng
dc.relation.ispartofEcletica Quimica
dc.sourceScopus
dc.subjectPeperomia
dc.subjectphenylalanine ammonia lyase
dc.subjectphenylpropanoid derivatives
dc.subjectPiper
dc.subjectThermal stability
dc.titlePhenylalanine ammonia lyase: new insights from Piperaceae speciesen
dc.typeArtigo

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Artigos - Química Orgânica - IQ