Proteolytic regulation of the extent of dietary proteins with skin grape proanthocyanidin and anthocyanidin's interactions. (29th November 2018)

• Record Type: Journal Article
• Authors: Ben Abdallah, Rim; Bautista‐Ortin, Ana Belén; Ghazouani, Tesnime; Talbi, Wafa; Jiménez‐Martinez, Maria D.; Gómez‐Plaza, Encarna; Fattouch, Sami
• Is Part Of: International journal of food science & technology. Volume 54:Number 5(2019)
• Page Start: 1633
• Page End: 1641
• Publication Date: 2018-11-29
• Subjects: Anthocyanidin -- dietary proteins -- phloroglucionolysis -- proanthocyanidin -- proteolysis -- size exclusion chromatography; Food industry and trade -- Periodicals; 664
• DOI: 10.1111/ijfs.14038
• Languages: English
• ISSNs: 0950-5423

Abstract

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. Abstract : Pepsin contributes to the regulation of protein‐flavonoid interactions. A limited formation of protein‐flavonoid aggregations is resulted from pepsin proteolysis effect.