Proteolytic regulation of the extent of dietary proteins with skin grape proanthocyanidin and anthocyanidin's interactions
Autor: | Sami Fattouch, Rim Ben Abdallah, Ana Belén Bautista-Ortín, Tesnime Ghazouani, Encarna Gómez-Plaza, Wafa Talbi, María Dolores Jiménez-Martínez |
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Rok vydání: | 2018 |
Předmět: |
0106 biological sciences
Protease medicine.diagnostic_test biology Chemistry Proteolysis medicine.medical_treatment 04 agricultural and veterinary sciences 040401 food science 01 natural sciences Industrial and Manufacturing Engineering chemistry.chemical_compound 0404 agricultural biotechnology Blood serum Pepsin Proanthocyanidin 010608 biotechnology Casein medicine biology.protein Food science Bovine serum albumin Food Science Anthocyanidin |
Zdroj: | International Journal of Food Science & Technology. 54:1633-1641 |
ISSN: | 1365-2621 0950-5423 |
Popis: | During technological processing, proanthocyanidins and anthocyanidins could be partly lost due to the complexation phenomena, affecting food and beverage nutritional properties, organoleptic properties and health‐promoting potentials. A common issue is encountered when processing food and beverage which is binding of phenolics to dietary proteins. The present investigation aims at evaluating the proteolysis contribution, using pure protease (Pepsin, 3000 units g⁻¹), to protein–anthocyanidin and protein–proanthocyanidin interactions. Bovine serum albumin (BSA), ovalbumin (OVA) and casein (CAS) dietary protein models were used. High‐performance liquid chromatography coupled to diode array detector (HPLC‐DAD) and size exclusion chromatography analyses proved that pepsin treatment significantly (P > 0.05) decreased the ratio of flavonoids’ interaction with tested proteins . The proteolysis reduced anthocyanidin interactions with CAS, OVA and BSA by 64.88%, 57.37% and 42.87% respectively. Similarly, proanthocyanidins interaction with CAS, OVA and BSA were reduced by 34.23%, 13.74% and 2.39% respectively. This study provides the basis to develop innovative technologies to limit protein–flavonoid complexation during food and beverage processing. |
Databáze: | OpenAIRE |
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