Reduced IgE/IgG binding capacities of bovine α-Lactalbumin by glycation after dynamic high-pressure microfluidization pretreatment evaluated by high resolution mass spectrometry

被引：35
作者：
Li, Jin-lin [1 ,4 ]
Liu, Jun [1 ,2 ]
Ye, Yun-hua [1 ,2 ]
Yang, Ping [1 ]
Tu, Zong-cai [1 ,2 ,3 ]
机构：
[1] Jiangxi Normal Univ, Natl Res & Dev Ctr Freshwater Fish Proc, Nanchang 330022, Jiangxi, Peoples R China
[2] Engn Res Ctr Freshwater Fish High Value Utilizat, Nanchang 330022, Jiangxi, Peoples R China
[3] Nanchang Univ, State Key Lab Food Sci & Technol, Nanchang 330047, Jiangxi, Peoples R China
[4] Nanchang Inst Food & Drug Control, Nanchang 330038, Jiangxi, Peoples R China
来源：
FOOD CHEMISTRY | 2019年 / 299卷
关键词：
Bovine alpha-Lactalbumin; IgE/IgG binding capacities; Dynamic high-pressure microfluidization; Glycation; High resolution mass spectrometry; BETA-LACTOGLOBULIN; PROTEIN GLYCATION; IGE-BINDING; ULTRASOUND PRETREATMENT; MILK ALLERGY; ALLERGENICITY; REDUCTION; PRODUCTS; PEPTIDE;
D O I：
10.1016/j.foodchem.2019.125166
中图分类号：
O69 [应用化学];
学科分类号：
081704 ;
摘要：
Dynamic high-pressure microfluidization (DHPM) pretreatment and glycation with lactose were employed to modify alpha-Lactalbumin (alpha-LA) with respect to the IgE/IgG binding capacities. No significant difference on incorporation ratio value of glycated alpha-LA was observed with and without DHPM pretreatment. However, IgE/IgG binding capacities of alpha-LA were decreased after glycation and DHPM pretreatment promoted the reduction. The lowest IgE/IgG binding capacities of glycated alpha-LA were obtained by DHPM pretreatment at 110 MPa. Native alpha-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 alpha-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 alpha-LA. The study revealed that glycation combined with DHPM was a promising way to decrease the allergenicity of proteins.
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页数：8
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