Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction. (15th June 2015)

• Record Type: Journal Article
• Authors: Perusko, Marija; Al-Hanish, Ayah; Cirkovic Velickovic, Tanja; Stanic-Vucinic, Dragana
• Is Part Of: Food chemistry. Volume 177(2015)
• Page Start: 248
• Page End: 257
• Publication Date: 2015-06-15
• Subjects: HIUS high intensity ultrasound -- WP whey proteins -- MR Maillard reaction -- MRPs Maillard reaction products -- BLG β-lactoglobulin; Whey proteins -- Ultrasound -- Maillard reaction -- Macromolecular crowding -- Protein oxidation; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2015.01.042
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Macromolecular crowding enhances ultrasound-promoted Maillard reaction. Only minor change in whey protein structure occurs by enhanced glycation. Enhanced Maillard reaction results in increased whey protein oxidation. Glycated proteins have improved antioxidative capacity and thermal stability. Abstract: High intensity ultrasound (HIUS) can promote Maillard reaction (MR). Macromolecular crowding conditions accelerate reactions and stabilise protein structure. The aim of this study was to investigate if combined application of ultrasound and macromolecular crowding can improve efficiency of MR. The presence of crowding agent (polyethylene glycol) significantly increased ultrasound-induced whey protein (WP) glycation by arabinose. An increase in glycation efficiency results only in slight change of WP structure. Macromolecular crowding intensifies oxidative modifications of WP, as well as formation of amyloid-like structures by enhancement of MR. Solubility at different pH, thermal stability and antioxidative capacity of glycated WP were increased, especially in the presence of crowding agent, compared to sonicated nonglycated proteins. The application of HIUS under crowding conditions can be a new approach for enhancement of reactions in general, enabling short processing time and mild conditions, while preserving protein structure and minimising protein aggregation.