Impacts of glycation and transglutaminase-catalyzed glycosylation with glucosamine on the conformational structure and allergenicity of bovine β-lactoglobulin

Yuan, Fangzhou; Ahmed, Ifty; Lv, Liangtao; Li, Zhaojie; Lin, Hong; Lin, Hang; Zhao, Jinxin; Tian, Shenglan; Ma, Jian

doi:10.1039/c8fo00909k

Cited by 41 publications

(32 citation statements)

References 59 publications

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“…The content of free amino groups in SPI‐E decreased significantly ( P < 0.05) compared to SPI. It is mainly due to the crosslinking of SPI, which reduces the content of free amino groups 22 . The content of free amino groups in the SPI‐G sample was significantly reduced compared to the SPI+G mixture ( P < 0.05), because the protein incorporated the amino group in glucosamine into the protein molecule under the action of transglutaminase.…”

Section: Resultsmentioning

confidence: 99%

Effects of transglutaminase glycosylated soy protein isolate on its structure and interfacial properties

Zhang

Cui

et al. 2021

J Sci Food Agric

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BACKGROUNDS The structural and interfacial properties of soybean protein isolate (SPI) after glycosylation by the transglutaminase method were studied. It is hoped that preliminary explorations will find a new food ingredient and broader application of SPI in the food industry. RESULTS The contents of free amino proves that transglutaminase can insert glucosamine into SPI through its transamination, and realize the enzymatic glycosylated SPI. The results of structure properties showed that a decrease in the content of the α‐helical structure indicates that the rigid structure of the protein is opened and the flexibility is increased. The blue shift of the maximum fluorescence intensity of soy protein isolate‐glucosamine with transglutaminase (SPI‐G) indicates the formation of a new substance; scanning electron microscopy shows that the SPI‐G powder can be seen at a magnification of 2000×, and the protein structure becomes soft. The results of interfacial properties found that enzymatic protein glycosylation exposes the internal hydrophobic groups of SPI, resulting in increased surface hydrophobicity, increased emulsification and emulsification stability, and reduced surface tension. CONCLUSION It shows that SPI‐G effectively improves the interfacial properties of SPI, providing a theoretical basis for the application of enzymatic glycosylation of SPI in the food industry. © 2021 Society of Chemical Industry

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Section: Resultsmentioning

confidence: 99%

Effects of transglutaminase glycosylated soy protein isolate on its structure and interfacial properties

Zhang

Cui

et al. 2021

J Sci Food Agric

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“…This mild modification has been used to enhance the sugar-conjugation efficiency and improve the functional properties of proteins. 4 Non-enzymatic glycation of proteins sets the stage for the formation of advanced glycation end-products and the development of chronic complications of diabetes 5 Transferrin (Tf) is a critical iron transport protein in the body. 6,7 In recent years, with the continuous deepening of research technologies, such as proteomics and glycometabonomics, and the rapid development of related detection technologies, such as high-performance liquid chromatography/electrospray ionization-mass spectrometry (HPLC/ESI-MS), studies have shown that non-enzymatic glycated modification of Tf is closely related to the occurrence and development of diabetes.…”

Section: Introductionmentioning

confidence: 99%

Non-Enzymatic Glycation of Transferrin and Diabetes Mellitus

Ma¹,

Cai²,

Wang³

et al. 2021

DMSO

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Diabetes is a metabolic disease characterized by high blood sugar. Its complications may damage multiple organs, such as eyes, kidneys, heart, blood vessels, and nerves, severely threatening human health. Transferrin (Tf) is a major iron transport protein in the body. Recent studies have shown that the degree of non-enzymatic glycated modification of Tf is increased in diabetic patients, and glycated Tf is closely related to the occurrence and development of diabetes and diabetic complications. However, the molecular mechanisms underlying this glycated modification in diabetes and diabetic complications are still unclear. It is speculated that the mechanism may be that glycated modification reduces the binding ability of Tf and its receptor TfR, followed by excessive iron accumulation in the body. Iron overload in the body may further lead to the death of pancreatic beta cells and insulin resistance by increasing oxidative stress, inducing iron death, interfering with the insulin signaling pathway, and causing autophagy deficiency. In addition, non-enzymatic glycation affects the binding of Tf with chromium and reduces the ability of Tf to transport chromium into tissues, resulting in a decrease in the levels of chromium in tissues and ultimately affecting the sensitivity of tissues to insulin. In diabetic patients, the concentrations of glycated Tf in serum were significantly correlated with those of fructosamine.Tf has a shorter half-life, and not affected by anemia or hypoalbuminemia and less negative charge under physiological conditions, while glycated modification could not change the isoelectric point of Tf, which easily passes through the negatively charged basement membrane of the glomerulus. Therefore, compared to glucosamine, HbA1C, etc., glycated Tf may be a future biomarker for evaluating short-term glycemic control and early renal damage in diabetic patients.

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“…For now, there are no restrictions on MTG addition in the food industry. Some researchers produced aggregated proteins with a significantly reduced allergenicity by adding the MTG at 30 U/g [ 24 ] and 50 U/g [ 42 ]. According to these studies, we set the rAra h 1 concentrations as 0.2, 0.4, 0.5, 0.7 and 1.0 mg/mL, which correspond with MTG addition of 30, 37.5, 50, 60, 75, 150 U/g.…”

Section: Resultsmentioning

confidence: 99%

Crosslinked Recombinant-Ara h 1 Catalyzed by Microbial Transglutaminase: Preparation, Structural Characterization and Allergic Assessment

Tian

Liu

Xue

et al. 2020

Foods

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As the one of the major allergens in peanut, the allergenicity of Ara h 1 is influenced by its intrinsic structure, which can be modified by different processing. However, molecular information in this modification has not been clarified to date. Here, we detected the influence of microbial transglutaminase (MTG) catalyzed cross-linking on the recombinant peanut protein Ara h 1 (rAra h 1). Electrophoresis and spectroscopic methods were used to analysis the structural changes. The immunoreactivity alterations were characterized by enzyme linked immunosorbent assay (ELISA), immunoblotting and degranulation test. Structural features of cross-linked rAra h 1 varied at different reaction stages. Hydrogen bonds and disulfide bonds were the main molecular forces in polymers induced by heating and reducing. In MTG-catalyzed cross-linking, ε-(γ-glutamyl) lysine isopeptide bonds were formed, thus inducing a relatively stable structure in polymers. MTG catalyzed cross-linking could modestly but significantly reduce the immunoreactivity of rAra h 1. Decreased content of conserved secondary structures led to a loss of protection of linear epitopes. Besides, the reduced surface hydrophobic index and increased steric hindrance of rAra h 1 made it more difficult to bind with antibodies, thus hindering the subsequent allergic reaction.

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Impacts of glycation and transglutaminase-catalyzed glycosylation with glucosamine on the conformational structure and allergenicity of bovine β-lactoglobulin

Cited by 41 publications

References 59 publications

Effects of transglutaminase glycosylated soy protein isolate on its structure and interfacial properties

Effects of transglutaminase glycosylated soy protein isolate on its structure and interfacial properties

Non-Enzymatic Glycation of Transferrin and Diabetes Mellitus

Crosslinked Recombinant-Ara h 1 Catalyzed by Microbial Transglutaminase: Preparation, Structural Characterization and Allergic Assessment

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