ACE-inhibitory activities of peptide fractions (<3 kDa) and identification of peptide sequence by MALDI-ToF-MS in model cheeses incorporating different Lactobacillus species

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dc.authoridHayaloglu, Ali Adnan/0000-0002-4274-2729
dc.authoridSahingil, Didem/0000-0002-7354-0679
dc.authorwosidŞahingil, Didem/ABG-8429-2020
dc.authorwosidHayaloglu, Ali Adnan/ABF-7063-2020
dc.contributor.authorSahingil, D.
dc.contributor.authorGokce, Y.
dc.contributor.authorCelikbicak, O.
dc.contributor.authorHayaloglu, A. A.
dc.date.accessioned2024-08-04T20:51:55Z
dc.date.available2024-08-04T20:51:55Z
dc.date.issued2022
dc.departmentİnönü Üniversitesien_US
dc.description.abstractIn this study, the effects of five adjunct lactobacilli on the formation of angiotensin-converting enzyme inhibitory (ACE-i) peptides in model cheeses were investigated. A total of seven peptide fractions (less than 3 kDa) were obtained by means of a fraction collector coupled with a HPLC system. ACE-i activity and peptide sequence analysis of the seven fractions were determined by RP-HPLC and then MALDI-ToF-MS techniques, respectively. Peptides produced from alpha s1- and kappa-caseins had higher amounts compared to those produced by other caseins. There were considerable differences between the fractions in terms of peptide sequences and ACE-i activities. In general, the peptide fraction containing Lactobacillus delbrueckii ssp. bulgaricus exhibited a higher level of ACE-i activity (79.56%) than the other samples. The next highest ACE-i activity was determined in the cheese containing L. plantarum and significant differences were observed between the ACE-i activities of the fractions. The highest ACE-i activity was identified in fractions including f1 (51.39%) for L. casei, f6 (33.49%) for L. helveticus, f4 (46.62%) for L. helveticus DPC4571 and f1 (47.96%) for cheese containing non-adjunct culture. In conclusion, use of lactobacilli as an adjunct in model cheese increased the peptide types and amounts and also ACE-i activity.en_US
dc.description.sponsorshipScientific and Technological Research Council of Turkey (TUBITAK, Ankara, Turkey) [213O 131]en_US
dc.description.sponsorshipThis work was supported by The Scientific and Technological Research Council of Turkey (TUBITAK, Ankara, Turkey) with project no. 213O 131.en_US
dc.identifier.doi10.1016/j.jfca.2022.104579
dc.identifier.issn0889-1575
dc.identifier.issn1096-0481
dc.identifier.scopus2-s2.0-85129516346en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.urihttps://doi.org/10.1016/j.jfca.2022.104579
dc.identifier.urihttps://hdl.handle.net/11616/100633
dc.identifier.volume110en_US
dc.identifier.wosWOS:000794973900014en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherAcademic Press Inc Elsevier Scienceen_US
dc.relation.ispartofJournal of Food Composition and Analysisen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectPeptide fractionsen_US
dc.subjectCheeseen_US
dc.subjectProteolysisen_US
dc.subjectHPLC-coupled fraction collectoren_US
dc.subjectAdjunct lactobacillien_US
dc.subjectCheese ripeningen_US
dc.titleACE-inhibitory activities of peptide fractions (<3 kDa) and identification of peptide sequence by MALDI-ToF-MS in model cheeses incorporating different Lactobacillus speciesen_US
dc.typeArticleen_US

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