Please use this identifier to cite or link to this item: http://hdl.handle.net/10316/10481
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dc.contributor.authorMacedo, I. Queiroz-
dc.contributor.authorFaro, Carlos J.-
dc.contributor.authorPires, Euclides M.-
dc.date.accessioned2009-07-06T09:23:21Z-
dc.date.available2009-07-06T09:23:21Z-
dc.date.issued1996-01-18-
dc.identifier.citationJournal of Agricultural and Food Chemistry. 44:1 (1996) 42-47en_US
dc.identifier.issn0021-8561-
dc.identifier.urihttp://hdl.handle.net/10316/10481-
dc.description.abstractThe action of cardosin on bovine αs- and β-casein at 30 °C in 50 mM citrate buffer (pH 6.2) was studied. Peptides were isolated by reversed-phase HPLC on C18 columns and identified from their amino acid composition and N-terminal amino acid sequence. The relative susceptibility of peptide bonds cleaved was Phe23-Phe24 > Trp164-Tyr165 > Tyr166-Val167 > Tyr165-Tyr166 > Phe153-Tyr154 > Phe145-Tyr146 ≈ Leu149-Phe150 ≈ Leu156-Asp157 ≈ Ala163-Trp164 for αs1-casein and Leu192-Tyr193 > Leu191-Leu192 ≈ Leu165-Ser166 > Phe190-Leu191 ≥ Ala189-Phe190 ≈ Leu127-Thr128 for β-casein. In αs2-casein, cardosin cleaved the bonds Phe88-Tyr89 and Tyr95-Leu96. The enzyme shows a clear preference for bonds between hydrophobic, bulky amino acids, cleaving four consecutive peptide bonds in extremely bulky, hydrophobic regions of both αs1-CN (Ala163-Val167) and β-CN (Ala189-Tyr193), which was less attacked by chymosin in various experimental conditions. The active site cleft of cardosin accommodates sequences as bulky as Trp-Tyr-Tyr in different subsites (S1 to S‘2, S2 to S‘1, and probably S3 to S1). Several bitter peptides were identified in the digests.en_US
dc.language.isoengen_US
dc.publisherAmerican Chemical Societyen_US
dc.rightsopenAccesseng
dc.subjectαs-Caseinen_US
dc.subjectβ-caseinen_US
dc.subjectCardosinen_US
dc.subjectVegetal renneten_US
dc.subjectSpecificityen_US
dc.subjectProteolysisen_US
dc.subjectBitter peptidesen_US
dc.titleCaseinolytic Specificity of Cardosin, an Aspartic Protease from the Cardoon Cynara cardunculus L.: Action on Bovine αs- and β-Casein and Comparison with Chymosinen_US
dc.typearticleen_US
dc.identifier.doi10.1021/jf9406929-
item.fulltextCom Texto completo-
item.grantfulltextopen-
item.languageiso639-1en-
crisitem.author.deptFaculty of Sciences and Technology-
crisitem.author.deptFaculty of Sciences and Technology-
crisitem.author.parentdeptUniversity of Coimbra-
crisitem.author.parentdeptUniversity of Coimbra-
crisitem.author.researchunitCNC - Center for Neuroscience and Cell Biology-
crisitem.author.researchunitCNC - Center for Neuroscience and Cell Biology-
crisitem.author.orcid0000-0002-0480-8379-
crisitem.author.orcid0000-0002-5853-0165-
Appears in Collections:FCTUC Ciências da Vida - Artigos em Revistas Internacionais
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