Effect of polymerization with transglutaminase on in vitro digestion and antigenicity of β-lactoglobulin

Villas-Boas, Mariana Battaglin; Fernandes, Michele Augusto; Zollner, Ricardo de Lima; Netto, Flávia Maria

doi:10.1016/j.idairyj.2012.02.007

Cited by 34 publications

(24 citation statements)

References 44 publications

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“…Furthermore, subsequent digestion by α-chymotrypsin and trypsin led to an increase of DH in both C and Tg-C digests, reaching similar DH values (57.3 ± 2.81 and 59.2 ± 2.48%, respectively). Unlike β-lactoglobulin, β-casein, and phaseolin, for which it was reported that cross-linking by Tg resulted in products resistant to both pepsin and pancreatic enzymes [11,14,24] polymerization of cucurbitin by Tg had no influence on its digestion process. 2), Tg-C (5); cucurbitin digested by pepsin C1 (3), pepsin, α-chymotrypsin and trypsin C2 (4); enzymatically cross-linked cucurbitin digested by pepsin Tg-C1 (6), pepsin, α-chymotrypsin and trypsin Tg-C2 (7) by pepsin, two bands were still visible, but with reduced intensity (lanes 3 and 6).…”

Section: Resultsmentioning

confidence: 99%

“…the gelation and texture properties of food proteins such as soya, wheat, pea and whey proteins, casein, myosin, gluten, etc. [9][10][11][12].…”

Section: Introductionmentioning

confidence: 99%

“…allergenicity) [14] and nutritive properties such as digestibility. The Tg-mediated isopeptide bond (G-L) is highly resistant to mechanical stress and proteolytic degradation [15], thus the effect of cross-linking by Tg on the digestion by human gastrointestinal proteases has been studied in a variety of protein substrates, and it has been reported that, generally, cross-linking decreases protein digestibility [9][10][11].…”

Section: Introductionmentioning

confidence: 99%

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Biologically Active Digests from Pumpkin Oil Cake Protein: Effect of Cross‐linking by Transglutaminase

Popović

Stolić

Čakarević

et al. 2017

J Americ Oil Chem Soc

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The objective of this study was to show that biologically active hydrolysates can be obtained by simulated human gastrointestinal digestion (HGD) of transglutaminase cross‐linked pumpkin oil cake protein (Tg‐C) which was previously reported as a potential functional food additive. A two‐stage in vitro digestion model system (by pepsin and α chymotrypsin and trypsin, simultaneously) was used to simulate the process of HGD on native and Tg‐C major storage pumpkin oil seed/cake protein, cucurbitin (C). The biologically active potential of the digests was evaluated, measuring the angiotensin‐converting‐I enzyme (ACE) inhibitory and anti‐oxidant capacity. The ACE inhibitory activity was determined in both final digests, with IC50 = 0.30 ± 0.04 mg/ml for C and IC50 = 0.28 ± 0.01 for Tg‐C. The anti‐oxidant potency of the examined proteins was enhanced by the digestion process. The 2,2‐diphenyl‐1‐picrylhydrazyl and 2,2′‐azino‐bis(3‐ethylbenzothiazoline‐6‐sulphonic acid) radical cation activities and reducing power testing showed that all the hydrolysates act as a radical quencher and reducing agents. Overall, the results showed that the cross‐linking by Tg did not influence the digestion process, as well as having no effect on the biological activity of the hydrolysates. These also indicate that Tg‐C, if used as functional food additive, after food consumption can be digested and become a source of peptides exerting positive effects on human health.

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Section: Resultsmentioning

confidence: 99%

“…the gelation and texture properties of food proteins such as soya, wheat, pea and whey proteins, casein, myosin, gluten, etc. [9][10][11][12].…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Biologically Active Digests from Pumpkin Oil Cake Protein: Effect of Cross‐linking by Transglutaminase

Popović

Stolić

Čakarević

et al. 2017

J Americ Oil Chem Soc

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“…Particularly, MTGase used in food stuff may modify the immunogenicity of food proteins, such as soy proteins (Babiker et al, 1998), peanut proteins (Clare, Gharst & Sanders, 2007) and fermented milk beverages (Wróblewska et al, 2013). However, the resistant ability of food proteins to the gastrointestinal enzymes is an important factor to take into account which is related to immunological assays (Villas-Boas et al, 2012). In some cases the MTGase-catalyzed reaction can affect the stability of proteins with respect to their bioaccessibility (Rui et al, 2016), digestibility and allergenicity (Stanic et al, 2010; Tang et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

In vitro gastrointestinal digestion study of a novel bio-tofu with special emphasis on the impact of microbial transglutaminase

Xing

Rui

Jiang

et al. 2016

PeerJ

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We have developed a novel bio-tofu, made from mixed soy and cow milk (MSCM), using Lactobacillus helveticus MB2-1 and Lactobacillus plantarum B1-6 incorporated with microbial transglutaminase (MTGase) as coagulant. MTGase was added to improve the textural properties and suit for cooking. However, the effect of MTGase on the digestion of mixed-protein fermented by lactic acid bacteria was unclear. This study aimed at evaluating the effect of MTGase on protein digestion of bio-tofu under simulated gastrointestinal digestion condition. The results showed that addition of MTGase could affect the particle size distribution, degree of hydrolysis, the content of soluble proteins and free amino acids. Based on the electrophoresis data, MTGase addition enhanced protein polymerization. During gastric and intestinal digestion process, proteins from bio-tofu were degraded into low molecular mass peptides. Our results suggested that incorporation of MTGase could lead to enzymatic modification of proteins of bio-tofu which may help in controlling energy intake and decrease the chance of food allergy.

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“…glucosamine and oligochitosan) into proteins (Jiang & Zhao, 2011). Glucosamine or oligochitosan glycation and cross-linking of whey proteins by TGase have been found resulting in lower in vitro antigenicity (Gaspar & de Góes-Favoni, 2015;Villas-Boas, Fernandes, Zollner, & Netto, 2012;Zhang, Liu, Xu, & Zhao, 2016).…”

Section: Introductionmentioning

confidence: 99%

Two horseradish peroxidase-based modifications result in two milk protein products with ordered secondary structure and enhanced in vitro antigenicity

Zhang

Wang

Liu

et al. 2016

CyTA - Journal of Food

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(2016) Two horseradish peroxidase-based modifications result in two milk protein products with ordered secondary structure and enhanced invitro antigenicity, CyTA -Journal of Food, 14:4, 572-577, DOI: 10.1080/19476337.2016 To link to this article: https://doi.org/10. 1080/19476337.2016 In this study, two horseradish peroxidase (HRP)-based modifications were used to treat whey protein isolate (WPI) and skim milk powder (SKMP) at protein concentration of 50 g/L, pH 7.0, and 37°C, via dityrosine formation in protein molecules. When HRP, glucose oxidase, and glucose were used to treat WPI and SKMP, suitable usages of HRP, glucose oxidase, and glucose, and reaction time were selected from single factor trials based on relative dityrosine contents of the modified products. After that, the selected HRP plus the calculated H 2 O 2 were used to treat WPI and SKMP. Electrophoretic analysis demonstrated that the modified products contained some crosslinked proteins with greater molecular weights. Other analyses showed that the modified products had more ordered secondary structure, and higher in vitro α-lactalbumin and β-lactoglobulin antigenicity than the respective substrates. HRP-glucose oxidase-glucose system was more potent than HRP-H 2 O 2 system to enhance in vitro antigenicity of WPI and SKMP.Dos modificaciones de peroxidasa de rábano picante resultan en dos productos proteínicos con estructura secundaria ordenada y una antigenicidad in vitro mejorada RESUMEN En este estudio se utilizaron dos modificaciones de peroxidasa de rábano picante (HRP) para tratar aislado proteínico de lactosuero (WPI) y leche desnatada en polvo (SKMP) con una concentración proteínica de 50 g/L, pH 7,0 y 37°C, mediante formación de ditirosina en moléculas proteínicas. En referencia a HRP, se utilizaron glucosa oxidasa y glucosa para tratar WPI y SKMP, se seleccionaron la utilización adecuada de HRP, glucosa oxidasa y glucosa, además del tiempo de reacción de las pruebas de factor único basadas en los contenidos relativos de ditirosina de los productos modificados. Después, la HRP seleccionada y el H 2 O 2 calculado se utilizaron para tratar WPI y SKMP. El análisis electroforético demostró que los productos modificados contenían algunas proteínas reticuladas con un mayor peso molecular. Otros análisis mostraron que los productos modificados tenían más estructuras secundarias ordenadas, además de una mayor antigenicidad in vitro de lactoalbúmina α y lactoglobulina β que los substratos respectivos. El sistema HRPglucosa oxidasa-glucosa fue más potente que el sistema HRP-H 2 O 2 para mejorar la antigenicidad in vitro de WPI y SKMP. ARTICLE HISTORY

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Effect of polymerization with transglutaminase on in vitro digestion and antigenicity of β-lactoglobulin

Cited by 34 publications

References 44 publications

Biologically Active Digests from Pumpkin Oil Cake Protein: Effect of Cross‐linking by Transglutaminase

Biologically Active Digests from Pumpkin Oil Cake Protein: Effect of Cross‐linking by Transglutaminase

In vitro gastrointestinal digestion study of a novel bio-tofu with special emphasis on the impact of microbial transglutaminase

Two horseradish peroxidase-based modifications result in two milk protein products with ordered secondary structure and enhanced in vitro antigenicity

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