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Maillard reaction affecting immunobinding activity and digestibility of tropomyosin in Alectryonella plicatula food matrix

Chenchen Yua, Xinrong Hea, Nairu Jia, Shuai Kanga, Dongxiao Lia, Huilin Zhanga, Yang Yanga, Dong Laib, Qingmei Liua, Guangming Liua ()
College of Ocean Food and Biological Engineering, Xiamen Key Laboratory of Marine Functional Food, Fujian Provincial Engineering Technology Research Center of Marine Functional Food, Jimei University, Xiamen 361021, China
The Second Affi liated Hospital of Xiamen Medical College, Xiamen 361021, China

Peer review under responsibility of Tsinghua University Press.

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• Maillard reaction with xylose significantly decreased the immunobinding activity of Alectryonella plicatula food matrix.

• Maillard reaction reduced the α-helix and digestion stability of Alectryonella plicatula food matrix.

• Ten amino acids were modified in 7 epitopes of Alectryonella plicatula food matrix tropomyosin.

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Abstract

In recent years, the allergy rate of oysters has surged, and daily food processing methods make it hard to reduce heat resistance and digestive allergy such as tropomyosin (TM). In this study, the Maillard reaction with xylose significantly reduced the IgE binding capacity of Alectryonella plicatula food matrix (AFM), that reduced by (77.81 ± 2.68)%. The study found the Maillard reaction changes the structure of the AFM, in which the content of α-helix decreased by (24.64 ± 1.46)%. Structural transformation further explains why the Maillard reaction alters the immunobinding activity of AFM. In addition, the Maillard reaction reduces the digestive stability of the AFM and makes TM in the A. plicatula food matrix Maillard reaction products (AFM-MRPs) more easily digested. Based on the above research, 10 amino acids on the 7 IgE epitopes of TM were modified. This result indicates that the Maillard reaction reduces the immunobinding activity of the AFM by changing the structure and modifying the amino acids on the epitope.

Keywords

Alectryonella plicatulaFood matrixImmunobinding activityMaillard reactionTropomyosin

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Food Science and Human Wellness
Volume 13 Issue 5,
September 2024
Pages 2959-2969
DOI: 10.26599/FSHW.2022.9250239
Cite this article:
Yu C, He X, Ji N, et al. Maillard reaction affecting immunobinding activity and digestibility of tropomyosin in Alectryonella plicatula food matrix. Food Science and Human Wellness, 2024, 13(5): 2959-2969. https://doi.org/10.26599/FSHW.2022.9250239
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Specific IgE levels and symptoms of the shellfish-sensitive patients.

No.Age (years)SexIgE of A. plicatula food matirx (OD450 nm)aSymptoms
Note:aThe OD450 nm of serum from patients over 2 times than that of the nonallergic individual was defined as A. plicatula sensitive sera. bA person was nonallergic individual and was non-allergic symptom. M, male; F, female.
119M0.25Anaphylactic rhinitis
217M0.25Atopic dermatitis
326F0.22Cough
418M0.22Nausea and vomiting
519M0.20Atopic dermatitis
617F0.20Cough
736M0.20Urticaria
822F0.19Lungs infected
918F0.19Nausea and vomiting
1021M0.18Cough
1154M0.18Anaphylactic rhinitis
1238M0.18Cough
1321F0.18Nausea and vomiting
1417F0.17Atopic dermatitis
1549F0.17Atopic dermatitis
1617F0.17Cough
1731M0.15Cough
1822F0.15Urticaria
1927M0.15Atopic dermatitis
2018F0.13Nausea and vomiting
21b22F0.06-
22b18M0.07-

Identification of Maillard reaction modification sites from A. plicatula TM.

Modified amino acids on IgE epitopesPeptide sequenceMVobs (M + H)Modification
K12, K15, N17, R21AMKMEKENAQDRAEQL2215.06Dimethyl (K); C5H10O5 (N, R)
R90EQEIQSLNR2292.05Methyl (R)
R101QLLEEDMERSEERLQT1775.84Methyl (R)
R140NNASEERTDVLEKQLTEAKLIAEEA1386.68Dimethyl (R)
R167EAARKLAITEVDLER1720.86Dimethyl (R)
K189LEAAEAKVYELEEQLS730.38Dimethyl (K)
K205IKTLQVQNDQASQ2986.65Dimethyl (K)

Alignment of Maillard reaction modified sites of the purified TMs from other species.

Species and Maillard reaction conditionsModified amino acidsReference
Note: Bold indicates the amino acid that has been modified on the epitope.
A. plicatula-Xylose K12, K15, N17, R21, R90, R101, R140, K160, K161, R167, K189, K205
C. nobilis-Xylose K12, R15, K28, K76, R125, R127, K128, R133, R140, K146, K189Bai et al.[17]
E. modetus-MaltoseK5, K12, K15, K30, K38, K48, K66, K74, K76, K112, K128, K149, K161, K189, K205, K213, K222, K226, K231, K233, K248, K251, K264, K266, K268Zhang et al.[24]
E. modetus-MaltotrioseK15, K38, K48, K66, K74, K76, K112, K128, K149, K161, K168, K189, K205, K213, K222, K226, K231, K233, K248, K251, K264, K266, K268Zhang et al.[24]
E. modetus-GlucoseK5, K6, K7, K12, K15, K30, K38, K48, K66, K74, K76, K112, K128, K149, K161, K168, K189, K205, K213, K222, K226, K231, K233, K248, K251, K264, K266, K268Zhang et al.[24]
L. vannamei-Galactose-115 ℃ R21, R35, K38, K48, R49, K66, K74, K76, R90, R91, R101, R105, K112, R125, R127, K128, R140, K149, R152, R160, K161, R167, K168, R178, R182, K189, K205, K213, R217, K222, K226, K231, R238, R255, K264, K266, K268Liu et al.[8]
L. vannamei-Galactose-121 ℃ R21, K30, K48, R49, K66, K74, K76, R90, R91, R101, R105, K112, R140, K149, R152, R160, K161, R178, R182, K205, K213, R217, K222, K226, K231, R238, K264, K266, K268Liu et al.[8]
K12, K15, R21, K30, R35, R44, K49, K70, K74, K76, R90, R91, R101, R105, K112, R125, R127, K128, R133, R140,
S. paramamosain-Galactose K149, R152, R160, K161, R167, K168, R178, R182, K189, R198, K205, K213, R217, K222, K226, K231, K233, R238, R244, K248, K251, R255, K264Han et al.[25]
S. paramamosain-Arabinose K49, R90, R91, R101, K112, R125, R133, R140, R160, K161, K168, R255Han et al.[21]