Phenylalanine ammonia lyase: new insights from Piperaceae species

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dc.contributor.authorAndreia de Araújo Morandim Giannetti
dc.contributor.authorFELIPPE, L. G.
dc.contributor.authorSANTOS, V. AP. de F. F. M. dos
dc.contributor.authorKATO, M. J.
dc.contributor.authorFURLAN, M.
dc.contributor.authorOrcidhttps://orcid.org/0000-0002-5428-768X
dc.date.accessioned2022-11-01T06:04:32Z
dc.date.available2022-11-01T06:04:32Z
dc.date.issued2022-08-17
dc.description.abstract© 2022 Atlantis Livros Ltda.. All rights reserved.The 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.
dc.description.firstpage67
dc.description.lastpage82
dc.description.volume47
dc.identifier.citationGIANNETTI, A. DE A. M.; FELIPPE, L. G.; SANTOS, V. AP. de F. F. M. dos; KATO, M. J.; FURLAN, M. Phenylalanine ammonia lyase: new insights from Piperaceae species Ecletica Quimica, v. 47, n. 2, p. 67-82, Aug. 2022.
dc.identifier.doi10.26850/1678-4618EQJ.V47.2SI.2022.P67-82
dc.identifier.issn1678-4618
dc.identifier.urihttps://repositorio.fei.edu.br/handle/FEI/4634
dc.relation.ispartofEcletica Quimica
dc.rightsAcesso Aberto
dc.rights.licenseCreative Commons "Este é um artigo publicado em acesso aberto sob uma licença Creative commons (CC BY 4.0). Fonte: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85138593366&origin=inward. Acesso em: 29 nov. 2022.
dc.subject.otherlanguagePeperomia
dc.subject.otherlanguagephenylalanine ammonia lyase
dc.subject.otherlanguagephenylpropanoid derivatives
dc.subject.otherlanguagePiper
dc.subject.otherlanguageThermal stability
dc.titlePhenylalanine ammonia lyase: new insights from Piperaceae species
dc.typeArtigo
fei.scopus.citations0
fei.scopus.eid2-s2.0-85138593366
fei.scopus.updated2024-07-01
fei.scopus.urlhttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85138593366&origin=inward
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