Antioxidant properties of bovine liver protein hydrolysates and their practical application in biphasic systems

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Özet

BACKGROUND: The influence of protein hydrolysate produced from bovine liver protein hydrolysate (LPH) by enzymatic hydrolysis, using Alcalase/Protamex (1:1), on lipid dispersions was investigated. LPH production was optimized to maximize the antioxidant activity (at 45, 50, and 55 °C for 12, 18, and 24 h). Different concentrations of LPHs (1, 3, and 5 mg/g) were added to emulsions and to liposomes. Lipid oxidation level and particle size of the lipid dispersions were monitored for 14 days of storage at 25 °C. RESULTS: Radical scavenging activity and reducing power were the highest at 45 °C after 24 h of hydrolysis. Electrophoresis pattern showed that the antioxidant activity was arising from the peptides with molecular weight around 10 kDa. Lipid oxidation occurred more rapidly in samples without LPH during storage. In emulsions, lower thiobarbituric acid-reactive substance and conjugated diene values were measured with increasing concentrations of LPH at day 14. Accordingly, particle size of the samples containing 5 mg/g of LPH was smaller than those of other groups. Phase separation was observed only in lecithin emulsion without LPH at day 14. The use of LPH in liposome limited the lipid oxidation and maintained the size of the particles independently from the concentration. CONCLUSION: This study highlights the potential applications of animal by-products as natural antioxidants in complex food systems. The results demonstrate that LPH, particularly when hydrolyzed at optimized conditions, can effectively inhibit lipid oxidation. The findings suggest that biphasic systems incorporating LPH have promising prospects for enhancing the stability and quality of food products. © 2023 The Authors. Journal of The Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry. © 2023 The Authors. Journal of The Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.

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RDL Kalıcı Bağlantı (PID)
https://rdlopen.rawdatalibrary.net/r/ebyu/11853Resmi atıflarda kullanılan kalıcı adres
DOI
https://doi.org/10.1002/jsfa.13190Yayıncı resmi DOI adresi
Tam Kayıt
AlanDeğerDil
dc.contributor.authorArslan, Betul
dc.contributor.authorXiong, Youling L
dc.contributor.authorSoyer, Ayla
dc.date.accessioned2026-10-18T20:26:50.861267892Z
dc.date.available2026-10-18T20:26:50.861267892Z
dc.date.issued2024
dc.description.abstractBACKGROUND: The influence of protein hydrolysate produced from bovine liver protein hydrolysate (LPH) by enzymatic hydrolysis, using Alcalase/Protamex (1:1), on lipid dispersions was investigated. LPH production was optimized to maximize the antioxidant activity (at 45, 50, and 55 °C for 12, 18, and 24 h). Different concentrations of LPHs (1, 3, and 5 mg/g) were added to emulsions and to liposomes. Lipid oxidation level and particle size of the lipid dispersions were monitored for 14 days of storage at 25 °C. RESULTS: Radical scavenging activity and reducing power were the highest at 45 °C after 24 h of hydrolysis. Electrophoresis pattern showed that the antioxidant activity was arising from the peptides with molecular weight around 10 kDa. Lipid oxidation occurred more rapidly in samples without LPH during storage. In emulsions, lower thiobarbituric acid-reactive substance and conjugated diene values were measured with increasing concentrations of LPH at day 14. Accordingly, particle size of the samples containing 5 mg/g of LPH was smaller than those of other groups. Phase separation was observed only in lecithin emulsion without LPH at day 14. The use of LPH in liposome limited the lipid oxidation and maintained the size of the particles independently from the concentration. CONCLUSION: This study highlights the potential applications of animal by-products as natural antioxidants in complex food systems. The results demonstrate that LPH, particularly when hydrolyzed at optimized conditions, can effectively inhibit lipid oxidation. The findings suggest that biphasic systems incorporating LPH have promising prospects for enhancing the stability and quality of food products. © 2023 The Authors. Journal of The Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry. © 2023 The Authors. Journal of The Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.
dc.description.sponsorshipThis research was funded by Ankara University Scientific Research Projects Office (Grant #21H0443001) and additional support was provided by the Scientific and Technological Research Council of Turkey (TÜBİTAK) 2214/A Doctoral Dissertation Abroad Research Grant Program (Grant #1059B141900415). Author Arslan acknowledges the exchange study at the University of Kentucky, where a portion of the research was conducted.
dc.identifier.doi10.1002/jsfa.13190
dc.identifier.eissn1097-0010
dc.identifier.endpage2989
dc.identifier.issn0022-5142
dc.identifier.issue5
dc.identifier.pmid38087783
dc.identifier.scopus2-s2.0-85180501650
dc.identifier.startpage2980
dc.identifier.urihttps://rdlopen.rawdatalibrary.net/r/ebyu/11853
dc.identifier.volume104
dc.identifier.wosWOS:001129033300001
dc.language.isoen
dc.publisherJohn Wiley and Sons Ltd
dc.relation.ispartofJournal of the Science of Food and Agriculture
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectantioxidant activity
dc.subjectemulsion
dc.subjectlipid oxidation
dc.subjectliposome
dc.subjectliver protein hydrolysate
dc.subjectoptimization
dc.subjectAnimals
dc.subjectAntioxidants
dc.subjectCattle
dc.subjectHydrolysis
dc.subjectLipids
dc.subjectLiver
dc.subjectOxidation-Reduction
dc.subjectProtein Hydrolysates
dc.subjectSubtilisins
dc.subjectantioxidant
dc.subjectlipid
dc.subjectprotein hydrolysate
dc.subjectsubtilisin
dc.subjectanimal
dc.subjectbovine
dc.subjectchemistry
dc.subjectmetabolism
dc.subjectoxidation reduction reaction
dc.titleAntioxidant properties of bovine liver protein hydrolysates and their practical application in biphasic systems
dc.typeArticle
dspace.entity.typePublication
rdl.citation.scopus4
rdl.citation.wos3
rdl.departmentDepartment of Food Engineering, Faculty of Engineering, Erzincan Binali Yıldırım University, Erzincan, Turkey.
rdl.oa.statusgold
rdl.source.indexSCOPUS
rdl.source.indexWOS
rdl.source.indexPUBMED
rdl.wos.indexScience Citation Index Expanded (SCI-EXPANDED)