Effect of Maillard Reaction on Tropomyosin Immunoreactivity in Mactra veneriformis

被引：1

作者：

Kang S. ^{[1
]}

He X. ^{[1
]}

Li D. ^{[1
]}

Ji N. ^{[1
]}

Yu C. ^{[1
]}

Chen G. ^{[2
]}

Cao M. ^{[1
,3
]}

Liu G. ^{[1
,3
]}

机构：

[1] Xiamen Key Laboratory of Marine Functional Food, College of Marine Food and Biological Engineering, Jimei University, Xiamen

[2] Women and Children’s Hospital Affiliated to Xiamen University, Xiamen

[3] Fujian Provincial Engineering Technology Research Center of Marine Functional Food, Xiamen

来源：

Shipin Kexue/Food Science | 2023年 / 44卷 / 16期

关键词：

digestive properties; dry-heating Maillard reaction; immunoreactivity; Mactra veneriformis; structural properties; tropomyosin;

D O I：

10.7506/spkx1002-6630-20220908-077

中图分类号：

学科分类号：

摘要：

In this study, xylose and arabinose were subjected separately to Maillard reaction with a crude extract of Mactra veneriformis under dry-heating conditions. The immunoreactivity and digestion properties of the Maillard reaction products (MRPs) were analyzed, finding that the Maillard reaction could reduce the immunoreactivity of allergens derived from Mactra veneriformis, increase the continuous digestion rate of the crude extract in simulated gastrointestinal fluid, and reduce the particle diameter of the digestion products. After that, TM in the MRPs was separated and purified, and its structural characteristics and immunoreactivity were analyzed. The results showed that the α-helix content of TM decreased and the β-sheet, β-turn, and random coil contents increased after the Maillard reaction, the surface hydrophobicity increased, and the spatial structure changed, which eventually led to a reduction in the immunoreactivity of TM. This study provides a theoretical basis for the development of hypoallergenic clam products. © 2023 Chinese Chamber of Commerce. All rights reserved.

引用

页码：16 / 24

页数：8

共 26 条

[1] LIN J, ALCOCER M., Overview of the commonly used methods for food allergens, Methods in Molecular Biology, 1592, pp. 1-9, (2017)
[2] IWEALA O I, CHOUDHARY S K, COMMINS S P., Food allergy, Current Gastroenterology Reports, 20, 5, (2018)
[3] MICHELET M, BALBINO B, GUILLEMINAULT L, Et al., IgE in the pathophysiology and therapy of food allergy, European Journal of Immunology, 51, 3, pp. 531-543, (2021)
[4] GRABENHENRICH L B, DOLLE S, MONERET-VAUTRIN A, Et al., Anaphylaxis in children and adolescents: the European anaphylaxis registry, Journal of Allergy and Clinical Immunology, 137, 4, pp. 1128-1137, (2016)
[5] ZHOU J, WANG Y, QIAN Y, Et al., Quantification of shellfish major allergen tropomyosin by SPR biosensor with gold patterned biochips, Food Control, 107, (2020)
[6] pp. 27-28
[7] LIN H X, LI Z X, LIN H, Et al., Effect of pH shifts on IgE-binding capacity and conformational structure of tropomyosin from short-neck clam (Ruditapes philippinarum), Food Chemistry, 188, pp. 248-255, (2015)
[8] KOPPELMAN S J, LARDIZABAL A L, NIEMANN L, Et al., Development of a sandwich enzyme-linked immunosorbent assay for detection and quantification of clam residues in food products, BioMed Research International, 2021, (2021)
[9] JING H, KITTS D D., Chemical and biochemical properties of casein-sugar Maillard reaction products, Food and Chemical Toxicology, 40, 7, pp. 1007-1015, (2002)
[10] BRANDS C, VAN BOEKEL M., Kinetic modelling of reactions in heated disaccharide-casein systems, Food Chemistry, 83, 1, pp. 13-26, (2003)

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