•  
  •  
 

Abstract

The method of indirect competitive ELISA, scanning electron microscopy (SEM) and dynamic light scattering (DLS) were used to study the ultrasound-assisted glycation with lactose (UAG) on changes in allergenicity and structure of β-lactoglobulin (β-Lg) during digestion in vitro. The results showed that the allergenicity and the degree of hydrolysis of UAG modified β-Lg had a reduced during gastrointestinal digestion. Glycation limited β-Lg to form a smaller particle structure during gastric digestion, then aggregated during intestinal digestion. The fluorescence intensity first increased and then decreased, and the maximum emission wavelength appeared red shift. These results indicated that UAG modification could effectively reduce the allergenicity of protein during digestion. The decrease of allergenici-ty was closely related to structural changes of UAG modification.

Publication Date

4-28-2021

First Page

6

Last Page

11

DOI

10.13652/j.issn.1003-5788.2021.04.002

References

[1] CARRARD A, RIZZUTI D, SOKOLLIK C. Update on food allergy[J]. Journal of Allergy & Clinical Immunology, 2016, 70(12): 1 511-1 520.
[2] DISEASES N. Food Allergy-an overview[J]. Environmental Health Perspectives, 2012, 111(2): 223-225.
[3] HULSHOF L, SCHOEMAKER A A, PETRUS N C M, et al. Re: Oral desensitization as a useful treatment in 2-year-old children with cow's milk allergy[J]. Clinical & Experimental Allergy, 2011, 41(12): 1 815-1 818.
[4] IKEUCHI T, AOKI T, YOSHIDA T, et al. Functional improvements to beta-lactoglobulin by preparing an edible conjugate with cationic saccharide using microbial transglutaminase (MTGase)[J]. Bioscience, Biotechnology, and Biochemistry, 2008, 72(5): 1 227-1 234.
[5] JONATHAN O, SULLIVAN A C, BRIAN MURRAY B, et al. The effect of ultrasound treatment on the structural, physical and emulsifying properties of animal and vegetable proteins[J]. Food Hydrocolloids, 2016, 53: 141-154.
[6] MILKOVSKA-STAMENOVA S, HOFFMANN R. Influence of storage and heating on protein glycation levels of processed lactose-free and regular bovine milk products[J]. Food Chemistry, 2017, 221(15): 489-495.
[7] 贾本盼, 袁晓金, 范智义, 等. 面包皮中水溶性晚期糖基化终产物对人肾小管上皮细胞的氧化损伤[J]. 食品科学, 2018, 39(1): 136-141.
[8] MA Shuang, WANG Cui-na, GUO Ming-ruo. Changes in structure and antioxidant activity of beta-lactoglobulin by ultrasound and enzymatic treatment[J]. Ultrasonics Sonochemistry, 2018, 43: 227-236.
[9] ZHANG Nan-hai, TU Zong-cai, WANG Hui, et al. Liquid chromatography high-Resolution mass spectrometry identifies the glycation sites of bovine serum albumin induced by d-ribose with ultrasonic treatment[J]. Journal of Agricultural and Food Chemistry, 2018, 66(3): 563-570.
[10] 毛积华, 王辉, 涂宗财, 等. 己糖修饰的糖基化卵清蛋白产物及其致敏性分析[J]. 食品与机械, 2020, 36(6): 11-15.
[11] SONG Chun-li, ZHAO Xin-huai. Structure and property modification of an oligochitosan-glycosylated and crosslinked soybean protein generated by microbial transglutaminase[J]. Food Chemistry, 2014, 163(15): 114-119.
[12] LIU Guang-xian, TU Zong-cai, YANG Wen-hua, et al. Investigation into allergenicity reduction and glycation sites of glycated beta-lactoglobulin with ultrasound pretreatment by high-resolution mass spectrometry[J]. Food Chemistry, 2018, 252(11): 99-107.
[13] MINEKUS M, ALMINGER M, ALVITO P, et al. A standardised static in vitro digestion method suitable for food: An international consensus[J]. Food Function, 2014, 5(6): 1 113-1 124.
[14] XIANG B Y, NGADI M O, OCHOA-MARTINEZ L A, et al. Pulsed electric field-induced structural modification of whey protein isolate[J]. Food and Bioprocess Technology, 2011, 4(8): 1 341-1 348.
[15] PINTO M S, LONIL J, HENRY G, et al. Heating and glycation of β-lactoglobulin and β-casein: Aggregation and in vitro digestion[J]. Food Research International, 2014, 55: 70-76.
[16] KIM S B, KI K S, KHAN M A, et al. Peptic and tryptic hydrolysis of native and heated whey protein to reduce its antigenicity[J]. Journal of Dairy Science, 2007, 90(9): 4 043-4 050.
[17] LI Bo-wen, MO Ling, YANG Yu-hui, et al. Processing milk causes the formation of protein oxidation products which impair spatial learning and memory in rats[J]. RSC Advances, 2019, 9(39): 22 161-22 175.
[18] 张敏, 涂宗财, 王辉, 等. 糖基化鳕鱼小清蛋白消化过程中的致敏性[J]. 食品与机械, 2020, 36(6): 16-22.
[19] PERUSKO M, VAN ROEST M, STANIC-VUCINIC D, et al. Glycation of the major milk allergen beta-lactoglobulin changes its allergenicity by alterations in cellular uptake and degradation[J]. Molecular Nutrition & Food Research, 2018, 62(17): e1800341.
[20] ZHAO Di, LI Lin, LE T T, et al. Digestibility of glycated milk proteins and the peptidomics of their in vitro digests[J]. Journal of the Science of Food & Agriculture, 2019, 99(6): 3 069-3 077.
[21] CORZO-MARTNEZ M, SORIA A C, BELLOQUE J, et al. Effect of glycation on the gastrointestinal digestibility and immunoreactivity of bovine β-lactoglobulin[J]. International Dairy Journal, 2010, 20(11): 742-752.
[22] YEBOAH F K, ALLI I, YAYLAYAN V, et al. Effect of limited solid-state glycation on the conformation of lysozyme by ESI-MSMS peptide mapping and molecular modeling[J]. Bioconjugate Chemistry, 2004, 15(1): 27-34.
[23] YAN Yun-feng, SEEMAN D, ZHENG Bing-qian, et al. pH-dependent aggregation and disaggregation of native β-Lactoglobulin in low salt[J]. Langmuir the Acs Journal of Surfaces & Colloids, 2013, 29(14): 4 584-4 593.
[24] PERAM M R, LOVEDAY S M, YE A, et al. In vitro gastric digestion of heat-induced aggregates of β-lactoglobulin[J]. Journal of Dairy Science, 2013, 96(1): 63-74.
[25] MICHELE D S P, BOUHALLAB S D, DE CARVALHO A F, et al. Glucose slows down the heat-induced aggregation of β-lactoglobulin at neutral pH[J]. Journal of Agricultural and Food Chemistry, 2012, 60(1): 214-219.
[26] LIU Gang, ZHONG Qi-xin. Glycation of whey protein to provide steric hindrance against thermal aggregation[J]. Journal of Agricultural and Food Chemistry, 2012, 60(38): 9 754-9 762.
[27] PALLARS I, VENDRELL J, AVILS F X, et al. Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin[J]. Journal of Molecular Biology, 2004, 342(1): 321-331.
[28] REN Guo-yan, SUN He, GUO Jin-ying, et al. Molecular mechanism of the interaction between resveratrol and trypsin via spectroscopy and molecular docking[J]. Food Function, 2019, 10(6): 3 291-3 302.
[29] FEYZI S, VARIDI M, ZARE F, et al. Effect of drying methods on the structure, thermo and functional properties of fenugreek (trigonella foenum graecum) protein isolate[J]. Journal of the Science of Food & Agriculture, 2017, 98(5): 1 880-1 888.
[30] JING Jian, QU Xin, TU Zhi, et al. Spectroscopic investigations of the interaction of the antihypertension drug valsartan with human serum albumin[J]. Molecular Medicine Reports, 2014, 9(6): 2 191-2 196.

Share

COinS
 
 

To view the content in your browser, please download Adobe Reader or, alternately,
you may Download the file to your hard drive.

NOTE: The latest versions of Adobe Reader do not support viewing PDF files within Firefox on Mac OS and if you are using a modern (Intel) Mac, there is no official plugin for viewing PDF files within the browser window.