Pre‐deamidation of soy protein isolate exerts impacts on transglutaminase‐induced glucosamine glycation and cross‐linking as well as properties of the products

Yao, Xintong; Zhao, Xin‐Huai

doi:10.1002/jsfa.7361

Cited by 11 publications

(10 citation statements)

References 40 publications

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“…In the absence of primary amine, the water would become an acyl receptor, and the glutamine residue removes the amino, which is hydrolyzed into acidic carboxyl groups; this reaction could alter the isoelectric point and solubility of protein (Folk, ). Deamidated proteins contain decreased amount of glutamine residues, which will offer less opportunity for protein cross‐linking induced by MTGase, inevitably, the cross‐linking reaction would be maintained in a less reaction extent (Yao & Zhao, ), and the properties of the cross‐linked product might be influenced by deamidation. Therefore, the mechanism to control the reaction condition should be explored to modify the direction of reaction.…”

Section: Introductionmentioning

confidence: 99%

Modification of the reaction system of Ara h 2 catalyzed by MTGase: Products and reaction conditions analysis

Zhao

Ren

et al. 2017

J Food Process Preserv

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Peanut (Arachis hypogaea) is listed among the eight major food allergens, in which Ara h 2 is the major allergen. The microbial transglutaminase (MTGase)‐catalyzed cross‐linking reaction reduces the allergenicity of Ara h 2. However, deamidation might occur and influence the cross‐linking reaction. In this work, native and reduced Ara h 2 were catalyzed by MTGase. In addition to intermolecular cross‐linking, intramolecular cross‐linking and deamidation were proven to occur simultaneously. Moreover, intramolecular cross‐linking sites were identified using mass spectrometry and the PLINK software. The reactions moved toward different directions because of different reduction conditions and different protein concentrations. Practical applications Cross‐linking is a common processing method used to improve the textural and functional properties of protein. Deamidation reaction might occur during processing and influence the cross‐linking reaction. The two types of reactions have a competitive relation, because both of them occur on glutamine residue. In Ara h 2 and MTGase system, protein concentration and reduction content influence the direction of reaction. The results can be applied to modify the reaction system of Ara h 2 catalyzed by MTGase. In addition, the relationship between structure and properties changes on Ara h 2 was discussed based on analysis of cross‐linking sites.

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Section: Introductionmentioning

confidence: 99%

Modification of the reaction system of Ara h 2 catalyzed by MTGase: Products and reaction conditions analysis

Zhao

Ren

et al. 2017

J Food Process Preserv

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“…After the glycosylation reaction, the peak intensity at around 208 nm decreased (Figure 7b), indicating that the reaction caused a structural change of WPI‐D. The peak intensity at 217 nm after the glycosylation reaction decreased, indicating that the content of the β‐sheet structure was lowered during the reaction (Yao & Zhao, 2016). Lysine residues were mostly present in the β‐sheet structure of proteins, and glycosylation reaction was most likely to occur according to the report lysines 47, 70 and 91 (Fogliano et al., 1998).…”

Section: Resultsmentioning

confidence: 99%

Effect of reaction temperature on the protein structure and the ability to encapsulate β‐carotene of WPI‐dextran conjugates

Chu

Kang

Zhao

et al. 2020

Journal of Food Science

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In this paper, we studied the effect of glycosylation reaction on the molecular structure and functional properties of whey protein isolate (WPI), and studied the effect of reaction temperature (50 to 90 °C) on the molecular structure and functional properties of WPI–dextran conjugates (WPI‐D). The results of the extent of glycation (EG) and sodium dodecyl sulfate–polyacrylamide gel electrophoresis confirmed the formation of WPI‐D. Circular dichroism (CD), Fourier transform infrared spectrum, and fluorescence spectroscopy indicated that the molecular structure of WPI was changed after glycosylation—the β‐sheet content was decreased and the tryptophan content was increased. The emulsifying properties and the ability to encapsulate β‐carotene of WPI‐D were improved compared with WPI (P < 0.05). When the reaction temperature was 70 and 80 °C, the EG and the ability to encapsulate β‐carotene of WPI‐D were better (P < 0.05), which was related to protein unfolding. However, due to the polymerization between the WPI molecules, the emulsion activity index of WPI‐D and the ability to encapsulate β‐carotene were lowered at 90 °C (P < 0.05). Therefore, the glycosylation reaction can change the molecular structure and functional properties of WPI; the emulsifying properties and the ability to encapsulate β‐carotene of WPI‐D can be changed by controlling the reaction temperature of glycosylation. Practical Application The glycosylation reaction can change the molecular structure and functional properties of Whey protein isolate; the emulsifying properties and the ability to encapsulate β‐carotene of WPI‐dextran conjugates can be changed by controlling the reaction temperature of glycosylation.

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“…(TGase, protein-glutamine: amine -glutamyltransferase, EC 2.3.2.13) is an enzyme that catalyzes post-translation modification of proteins and glycation reaction between protein and amino-containing saccharides. 1,2 The cross-linking effect introduced by TGase may improve the function properties of proteins without altering their nutritional quality. TGase was first extracted from animals in 1973, and subsequent studies showed that this enzyme is widespread in plants and microorganisms.…”

Section: Transglutaminasementioning

confidence: 99%

“…Transglutaminase (TGase, protein‐glutamine: amine γ ‐glutamyltransferase, EC 2.3.2.13) is an enzyme that catalyzes post‐translation modification of proteins and glycation reaction between protein and amino‐containing saccharides . The cross‐linking effect introduced by TGase may improve the function properties of proteins without altering their nutritional quality.…”

Section: Introductionmentioning

confidence: 99%

Expression of Zea mays transglutaminase in Pichia pastoris under different promoters and its impact on properties of acidified milk protein concentrate gel

Zhang

Jin

et al. 2019

J Sci Food Agric

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BACKGROUND Transglutaminase (TGase) catalyzes post‐translational modification of proteins by γ‐glutamyl‐ϵ‐lysine chain links, covalent conjugation of polyamines, and deamidation. Zea mays TGase (TGZ) is a plant TGase with potential application prospects in the food industry. In this study, two promoter types, PFLD1 and PTEF1, were compared to improve the expression of TGZ, and the cross‐linking effect of recombinant TGZ on the properties of acid‐induced milk protein concentrate (MPC) gel was assessed. RESULTS A higher expression of TGZ was obtained under the induction of PFLD1 with a production of 635 U L−1. After purification using chromatography, TGZ activity was 0.4 U mg−1. The results indicated that TGZ treatment has effectively improved the textural properties of MPC gel at strength level and water‐holding capacity. Optimal texture of MPC gel was achieved after TGZ treatment using 2 U g−1 TGZ for 2 h at 35 °C and pH 7. CONCLUSION Comparative analysis of the promoters has greatly contributed to the production of TGZ in the industrial field. Furthermore, the modification of MPC gel texture by TGZ indicated that this recombinant enzyme has a practical value in dairy product, especially in yoghurt industry. © 2019 Society of Chemical Industry

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Pre‐deamidation of soy protein isolate exerts impacts on transglutaminase‐induced glucosamine glycation and cross‐linking as well as properties of the products

Cited by 11 publications

References 40 publications

Modification of the reaction system of Ara h 2 catalyzed by MTGase: Products and reaction conditions analysis

Modification of the reaction system of Ara h 2 catalyzed by MTGase: Products and reaction conditions analysis

Effect of reaction temperature on the protein structure and the ability to encapsulate β‐carotene of WPI‐dextran conjugates

Expression of Zea mays transglutaminase in Pichia pastoris under different promoters and its impact on properties of acidified milk protein concentrate gel

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