Determination of Sh‐ and Ss‐groups in Some Food Proteins Using Ellman's Reagent

Beveridge, T.; Toma, S.J.; Nakai, S.

doi:10.1111/j.1365-2621.1974.tb00984.x

Cited by 749 publications

(341 citation statements)

References 5 publications

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“…Since the output of the refractometer linearly increases with sample concentration, Eq. (1) 6 ) during the heat denaturation of ovalbumin. The surface hydrophobicity of heat-denatured ovalbumin was determined by using the method described previously.7) Ten microliters of ethanolic solutions of cisparinaric acid, 3.6 x 10 -3 M, were added to 2 ml of the protein solution.…”

Section: Methodsmentioning

confidence: 99%

Determination of Molecular Weight of Soluble Ovalbumin Aggregates during Heat Denaturation Using Low Angle Laser Light Scattering Technique

Kato

NAGASE

Matsudomi

et al. 1983

Agricultural and Biological Chemistry

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Section: Methodsmentioning

confidence: 99%

Determination of Molecular Weight of Soluble Ovalbumin Aggregates during Heat Denaturation Using Low Angle Laser Light Scattering Technique

Kato

NAGASE

Matsudomi

et al. 1983

Agricultural and Biological Chemistry

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“…Determination of SS groups and SH content was carried out according to the methods of Beveridge (1974) and Luo et al (2016) with some modifications. The principle of this method is that the interaction between DTNB and SH results in the formation of thioethyl nitrobenzene anions whose molar absorption coefficient is 13 600 at 412 nm.…”

Section: Methodsmentioning

confidence: 99%

Effects of the addition of gluten with different disulfide bonds and sulfhydryl concentrations on Chinese white noodle quality

Li¹,

Lu²,

Liu³

et al. 2018

Czech J. Food Sci.

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Li C., Lu Q., Liu Z., Yan H. (2018): Effects of the addition of gluten with different disulfide bonds and sulfhydryl concentrations on Chinese white noodle quality. Czech J. Food Sci., 36: 246-254.The disulfide bonds and sulfhydryl in gluten were evaluated to investigate the effects of structural characteristics on the quality of white noodles. The free sulfhydryl concentration increased significantly, but disulphide bonds decreased initially, and then became stable with increasing sodium sulfite concentration. With a decrease in disulfide bond concentration from 56.78 μmol/g to 20.01 μmol/g in gluten added to noodles, microstructural graphs verified that the cross-section and surface of noodles became rougher and looser with more holes generated; optimal cooking time decreased from 4.4 min to 3.3 min for fresh noodles and from 10.11 min to 9.19 min for dried samples; water absorption and cooking loss increased from 159% to 203% and from 5.26% to 9.06%, respectively. A decreasing trend and marked differences were observed for hardness, springiness, chewiness as well as resilience of fresh and cooked noodles, but the cohesiveness of fresh noodles exhibited no significant changes (P < 0.05).

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“…Determination of sulfhydryl groups Sulfhydryl groups were determined according to Ellman's DTNB method (Beveridge et al, 1974). Seventy-five mg of sample was suspended in 1 ml of Tris-Gly(10.4 g Tris, 6.9 g glycine and 1.2 g EDTA per l, pH 8.0, denoted as Tris-Gly), 4.7 g of GuHCl was added, and the volume made up to 10 ml.…”

Section: Methodsmentioning

confidence: 99%

Effects of Microbial Transglutaminase for Gelation of Soy Protein Isolate during Cold Storage

Soeda

2003

FSTR

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On gelation of soy protein isolate during cold storage, strength, deformation, elasticity E 0 and Newtonian viscosity N of the gels greatly increased with addition of one unit/g protein of microbial transglutaminase when kept for 3 days at 5˚C, while retardation time decreased. With addition of 3 units/g protein, the gels were too hard, but became brittle after being kept for 3 days at 5˚C. The viscoelasticity of gel treated during cold storage was superior to that of gel heated after having been kept in cold storage. It was assumed that the texture of the gel treated for one day at 5˚C was nearly equivalent to that of the gel treated at 40˚C for 60 min, on enzyme reactivity of transglutaminase. e e e e-(␥-glutamyl)lysine bonds in the gels were not formed in the case of the gel without transglutaminase, but increased linearly in the gel with transglutaminase. Contents of the sulfhydryl group of the gel were found to decrease during cold storage, and the degree of decrease was smaller in the gel with transglutaminase than in the gel without transglutaminase. This indicated less contribution of disulfide bonds in the gel treated with transglutaminase during cold storage.Keywords: soy protein, gel formation, cold storage, microbial transglutaminase, e-(␥-glutamyl)lysine bonds, sulfhydryl groups Transglutaminase (glutaminyl-peptide: amine ␥-glutamyltransferase, E.C. 2.3.2.13; TGase) catalyzes an acyl transfer reaction between a ␥-carboxyamide of peptide or protein-bound glutamine and a primary amine.When TGase acts on protein molecules, e-(␥-glutamyl)lysine (abbreviated e-(␥-Glu)Lys) bonds are formed. Many studies have been carried out to use this unique enzyme reaction, crosslinking between protein molecules, to change rheological properties of food proteins (Whitaker, 1977;Ikura et al., 1980;Motoki & Nio, 1983). TGase, derived from a microorganism, has been found and mass produced (Ando et al., 1989). Enzymological properties and various basic effects on physical properties of food proteins have been reported Nonaka et al., 1992;Nonaka et al., 1994;Nonaka et al., 1996).The principal mechanism of gelation of soy protein isolate (abbreviated SPI) is due to the formation of disulfide bonds, reported by Wolf and Smith (1961), Circle et al. (1964), Aoki and Sakurai (1969), Saio et al. (1971) on heat-induced gel, and by Watanabe et al. (1963), andHashizume et al. (1974) on freezeinduced gel. On the other hand, as described in previous reports (Soeda, 1994a;1994b;1995a;Soeda & Baba, 1999), the gel (abbreviated Cold-gel) was obtained by keeping it in cold storage. The Cold-gel showed physical properties characterized by flexibility and springiness, which were excellent compared with the viscoelasticity of heat-induced or freeze-induced gel. We also reported that characteristics of gels required for application of SPI gel in food processing were flexibility and springiness related to masticability and swallowing in the mouth, and that Cold-gel provided an improved texture in processed foods (Soeda, 1995b). These superior t...

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Determination of Sh‐ and Ss‐groups in Some Food Proteins Using Ellman's Reagent

Cited by 749 publications

References 5 publications

Determination of Molecular Weight of Soluble Ovalbumin Aggregates during Heat Denaturation Using Low Angle Laser Light Scattering Technique

Determination of Molecular Weight of Soluble Ovalbumin Aggregates during Heat Denaturation Using Low Angle Laser Light Scattering Technique

Effects of the addition of gluten with different disulfide bonds and sulfhydryl concentrations on Chinese white noodle quality

Effects of Microbial Transglutaminase for Gelation of Soy Protein Isolate during Cold Storage

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