Peanut allergen reduction and functional property improvement by means of enzymatic hydrolysis and transglutaminase crosslinking. (1st January 2020)

• Record Type: Journal Article
• Authors: Meng, Shi; Tan, Yuqing; Chang, Sam; Li, Jiaxu; Maleki, Soheila; Puppala, Naveen
• Is Part Of: Food chemistry. Volume 302(2019)
• Publication Date: 2020-01-01
• Subjects: Peanut allergen -- Enzymatic processing -- IgE-binding properties -- Papain -- Ficin -- Bromelain -- Transglutaminase (TGase) -- Functional properties; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2019.125186
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: The kinetics analysis of peanut protein hydrolyzed by eight enzymes were conducted. Enzyme processing reduced IgE-binding and functional properties of peanut protein. TGase treatment maintained IgE-binding properties of peanut protein hydrolysates. TGase treatment increased the functional properties of peanut protein hydrolysates. Abstract: Enzymatic processing could reduce the allergenicity of peanut proteins while may lose the functional properties. Transglutaminase (TGase) is an enzyme for improving the functional properties of proteins/hydrolysates. No studies have been conducted on peanut hydrolysates that are crosslinked with TGase. In this study, allergenicity and functional properties of peanut protein hydrolysate cross-linked by TGase were tested. Papain, ficin and bromelain were selected out of eight food-grade enzymes for the kinetic analysis of peanut protein hydrolysis that lead to high reduction rate (K) of the IgE-binding property. Peanuts hydrolyzed by the three selected enzymes (200 AzU/g) were used for IgE binding, TGase-crosslinking and functional property characterization. After hydrolysis, the IgE-binding properties of the peanut soluble extracts were decreased (by 85%–95%); and functional properties were also decreased as compared to intact peanut protein extracts. The TGase crosslinked hydrolysates had similar IgE-binding properties to the un-crosslinked hydrolysates, but with higher functional properties.