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Proteolytic regulation of the extent of dietary proteins with skin grape proanthocyanidin and anthocyanidin's interactions
Author(s) -
Ben Abdallah Rim,
BautistaOrtin Ana Belén,
Ghazouani Tesnime,
Talbi Wafa,
JiménezMartinez Maria D.,
GómezPlaza Encarna,
Fattouch Sami
Publication year - 2019
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.14038
Subject(s) - proanthocyanidin , anthocyanidins , chemistry , anthocyanidin , food science , proteolysis , flavonoid , pepsin , anthocyanin , bovine serum albumin , casein , soy protein , biochemistry , chromatography , polyphenol , enzyme , antioxidant
Summary 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.