Reduced IgE/IgG Binding Capacities of Bovine α-Lactalbumin by Glycation after Dynamic High-Pressure Microfluidization Pretreatment Evaluated by High Resolution Mass Spectrometry

Publication date: Available online 9 July 2019Source: Food ChemistryAuthor(s): Jin-lin Li, Jun Liu, Yun-hua Ye, Ping Yang, Zong-cai TuAbstractDynamic high-pressure microfluidization (DHPM) pretreatment and glycation with lactose were employed to modify α-Lactalbumin (α-LA) with respect to the IgE/IgG binding capacities. No significant difference on incorporation ratio value of glycated α-LA was observed with and without DHPM pretreatment. However, IgE/IgG binding capacities of α-LA were decreased after glycation and DHPM pretreatment promoted the reduction. The lowest IgE/IgG binding capacities of glycated α-LA were obtained by DHPM pretreatment at 110 MPa. Native α-LA was mainly glycated at K62, K94, K98, whereas glycation sites and degree of substitution per peptide (DSP) were added after DHPM treatment. Therefore, the reduced IgE/IgG binding capacities of α-LA was attributed to the characteristics of glycated sites, including the amount, location, and DSP values. Interestingly, K98 played the most important role in decreasing IgE/IgG binding capacities of α-LA. The study revealed that glycation combined with DHPM was a promising way to decrease the allergenicity of proteins.
Source: Food Chemistry - Category: Food Science Source Type: research