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dc.contributor.authorRivera Rodríguez, Diana Marcela
dc.contributor.authorRommi, Katariina
dc.contributor.authorMacedo Fernandes, Margarida Maria
dc.contributor.authorLantto, Raija
dc.contributor.authorTzanov, Tzanko
dc.contributor.otherUniversitat Politècnica de Catalunya. Departament d'Enginyeria Química
dc.date.accessioned2016-02-01T12:55:42Z
dc.date.available2016-05-04T00:32:07Z
dc.date.issued2015-10-01
dc.identifier.citationRivera, D., Rommi, K., Macedo, M.M., Lantto, R., Tzanov, T. Biocompounds from rapeseed oil industry co-stream as active ingredients for skin care applications. "INTERNATIONAL JOURNAL OF COSMETIC SCIENCE", 01 Octubre 2015, vol. 37, núm. 5, p. 496-505.
dc.identifier.issn0142-5463
dc.identifier.urihttp://hdl.handle.net/2117/82347
dc.description.abstractOBJECTIVE: Despite the great number of substances produced by the skincare industry, very few of them seem to truly have an effect on the skin. Therefore, given the social implications surrounding physical appearance, the search for new bioactive compounds to prevent or attenuate skin ageing and enhance self-image is a priority of current research. In this context, being rich in valuable compounds, such as proteins, phenolics, lipids and vitamins, this study is focused on the potential activity of rapeseed press cake hydrolysates to be used as raw materials for skincare applications.; METHODS: In this study, the protein-rich press residue from the rapeseed oil industry was converted enzymatically into short-chain biologically active peptides using four protease products with varying substrate specificity - Alcalase 2.4L FG, Protex 6L, Protamex and Corolase 7089. The antioxidant, anti-wrinkle and anti-inflammatory activities of the obtained hydrolysates were evaluated invitro while their biocompatibility with human skin fibroblasts was tested.; RESULTS: All hydrolysates were biocompatible with skin fibroblasts after 24h of exposure, while the non-hydrolysed extract induced cell toxicity. Alcalase 2,4L FG and Protex 6L-obtained hydrolysates were the most promising extracts showing improved bioactivities suitable for skin anti-ageing formulations, namely antioxidant activity, inhibiting approximately 80% cellular reactive oxidative species, anti-inflammatory and anti-wrinkle properties, inhibiting around 36% of myeloperoxidase activity and over 83% of elastase activity.; CONCLUSION: The enzymatic technology applied to the rapeseed oil industry costream results in the release of bioactive compounds suitable for skincare applications.
dc.format.extent10 p.
dc.language.isoeng
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es/
dc.subjectÀrees temàtiques de la UPC::Enginyeria química
dc.subject.lcshRapeseed industry
dc.subject.lcshSkin--Care and hygiene
dc.subject.otherbioactive peptides
dc.subject.othercell culture
dc.subject.otherchemical analysis
dc.subject.otherenzymatic hydrolysis
dc.subject.otherskin care
dc.subject.otherspectroscopy
dc.subject.otherhuman neutrophil elastase
dc.subject.otherbrassica-napus l.
dc.subject.otherfunctional-properties
dc.subject.otherantioxidant activity
dc.subject.otheroxidative stress
dc.subject.otherpotential applications
dc.subject.othercanola-meal
dc.subject.otherin-vitro
dc.subject.otherprotein
dc.subject.otherpeptides
dc.titleBiocompounds from rapeseed oil industry co-stream as active ingredients for skin care applications
dc.typeArticle
dc.subject.lemacColza
dc.subject.lemacPell -- Cura i higiene
dc.contributor.groupUniversitat Politècnica de Catalunya. GBMI - Grup de Biotecnologia Molecular i Industrial
dc.identifier.doi10.1111/ics.12222
dc.description.peerreviewedPeer Reviewed
dc.relation.publisherversionhttp://onlinelibrary.wiley.com/doi/10.1111/ics.12222/abstract;jsessionid=DEA268F55EE9650A01F4DFB0BBE11366.f04t04
dc.rights.accessOpen Access
local.identifier.drac16978934
dc.description.versionPostprint (published version)
local.citation.authorRivera, D.; Rommi, K.; Macedo, M.M.; Lantto, R.; Tzanov, T.
local.citation.publicationNameINTERNATIONAL JOURNAL OF COSMETIC SCIENCE
local.citation.volume37
local.citation.number5
local.citation.startingPage496
local.citation.endingPage505


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