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dc.contributor.author
Cian, Raúl Esteban  
dc.contributor.author
Alaiz, Manuel  
dc.contributor.author
Vioque, Javier  
dc.contributor.author
Drago, Silvina Rosa  
dc.date.available
2017-07-28T21:46:27Z  
dc.date.issued
2012-10  
dc.identifier.citation
Cian, Raúl Esteban; Alaiz, Manuel; Vioque, Javier; Drago, Silvina Rosa; Enzyme proteolysis enhanced extraction of ACE inhibitory and antioxidant compounds (peptides and polyphenols) from Porphyra columbina residual cake; Springer; Journal Of Applied Phycology; 25; 4; 10-2012; 1197-1206  
dc.identifier.issn
0921-8971  
dc.identifier.uri
http://hdl.handle.net/11336/21619  
dc.description.abstract
The traditional method to obtain phycocolloids from seaweeds implies successive extraction steps with cold and hot water. The residual cake derived from phycocolloids obtaining process of red seaweed Porphyra columbina is a waste containing 27 % protein and 10.7-mg gallic acid equivalents (100 g)−1. Seaweeds contain functional proteins, and the enzymatic hydrolysis of these proteins has been shown to release bioactive peptides. The aims of this study were to extract bioactive peptides and polyphenols after enzymatic hydrolysis of the residual cake and to evaluate their ACE inhibitory and antioxidant capacities (TEAC, DPPH, and copper-chelating activity). Residual cake hydrolysate has low molecular weight peptides containing Asp, Glu, Ala, and Leu. Residual cake hydrolysate had higher protein solubility than residual cake. ACE inhibition (≈45 %) and radical scavenging activity (TEAC and DPPH inhibition) were attributed mainly to low molecular weight peptides (500 Da) and polyphenols compounds released during proteolysis. The 50 % inhibition protein concentration value (IC50) corresponded to residual cake hydrolysate was 1.01 ± 0.02 and 0.91 ± 0.01 g L−1, for ABTS and DPPH, respectively. Also, residual cake hydrolysate had high copper-chelating activity (≈97.5 %). Hydrolysis could be used as a means to obtain ACE inhibitory and antioxidant compounds (peptides and polyphenols) from algae protein waste and add value to the phycocolloids extraction process.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Springer  
dc.rights
info:eu-repo/semantics/restrictedAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
Red Seaweeds  
dc.subject
Rhodophyta  
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Residual Cake  
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Hydrolysates  
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Ace Inhibitory Activity  
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Antioxidant Capacity  
dc.subject.classification
Ingeniería Química  
dc.subject.classification
Ingeniería Química  
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INGENIERÍAS Y TECNOLOGÍAS  
dc.title
Enzyme proteolysis enhanced extraction of ACE inhibitory and antioxidant compounds (peptides and polyphenols) from Porphyra columbina residual cake  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2016-07-06T15:47:09Z  
dc.identifier.eissn
1573-5176  
dc.journal.volume
25  
dc.journal.number
4  
dc.journal.pagination
1197-1206  
dc.journal.pais
Alemania  
dc.journal.ciudad
Berlin  
dc.description.fil
Fil: Cian, Raúl Esteban. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina  
dc.description.fil
Fil: Alaiz, Manuel. Consejo Superior de Investigaciones Cientificas; España  
dc.description.fil
Fil: Vioque, Javier. Consejo Superior de Investigaciones Cientificas; España  
dc.description.fil
Fil: Drago, Silvina Rosa. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina  
dc.journal.title
Journal Of Applied Phycology  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s10811-012-9913-2  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs10811-012-9913-2