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Soybean globulin

Semenova, M.G., Bolotina, V.S., Grinberg, V.Ya., Tolstoguzov, V.B. (1990). Thermodynamic incompatibility of the 11S fraction of soybean globulin and pectinate in aqueous medium. Food Hydrocolloids, 3, 447 156. [Pg.112]

Because of the dependence of sulfhydryl and disulfide reactions on heat treatment. It would be expected that their Involvement In protein gelation would depend greatly on gel formation conditions. For example, Catslmpoolas and Meyer (7) have suggested that disulfides play only a minor role In the progel to gel transformation In soybean globulins. In more Irreversible soy protein gelation processes, disulfide bridging may be Involved In... [Pg.133]

MC Garcfa, M Torre, F Laborda, ML Marina. Rapid separation of soybean globulins by reversed-phase high-performance liquid chromatography. J Chromatogr A 758 75-83, 1997. [Pg.166]

To study the effect of the Maillard reaction on nutritive value of protein, Patton, et a l. (57) heated purified casein and soybean globulin in 57. glucose solution for 24 hrs at 96.5°C, and found significant losses of lysine, arginine, tryptophan, and histidine (52). [Pg.10]

Yoshida et al (25) Isolated 2-amino-91/-pyrIdo[2,3- ]Indole (AcxC) and 2-amino-3-me thy l-9 -pyrido[ 2,3-b ] indole (MeActC) from pyrolysate of soybean globulin. [Pg.525]

Kumagai, H., Shizawa, Y., Sakurai, H., Kumagai, H. 1998. Influence of phytate removal and structural modification on the calcium-binding properties of soybean globulins. Biosci... [Pg.312]

Ovalbumin (pH 6.6) Soybean globulins Ovalbumin thermotropic aggregates Casein... [Pg.351]

Figure 9. Disc-gel electrophoretic patterns of 11S soybean globulin stored in a frozen or concentrated state, (a), original solution (b), after 2 days storage in a frozen state at —5°C (c), after the addition of 0.01 M mercaptoethanol (ME) to solution (b) (d), after 2 days of storage in a concentrated state (unfrozen) and (e), after the addition of 0.01M mercaptoethanol to solution (d) (lO). Figure 9. Disc-gel electrophoretic patterns of 11S soybean globulin stored in a frozen or concentrated state, (a), original solution (b), after 2 days storage in a frozen state at —5°C (c), after the addition of 0.01 M mercaptoethanol (ME) to solution (b) (d), after 2 days of storage in a concentrated state (unfrozen) and (e), after the addition of 0.01M mercaptoethanol to solution (d) (lO).
Nash AM and Wolf WJ. Solubility and ultracentrifugal studies on soybean globulins. Cereal Chem. 1967 44 183-192. [Pg.630]

Of special interest is the pH, the third factor influencing plastein formation. The optima for most proteases for plastein formation generally lie in a narrow range of pH 4-7 (Table I) measured with soybean globulin hydrolysates. Pepsin, for example, is an acid protease, and one of its characteristics is high degradative activity at low pH. Even at pH 1 it is active and able to degrade proteins. As Yamashita et al. (37) have demonstrated, no appreciable amount of plastein is formed at pH 1-2... [Pg.162]

Properties of Plasteins. Plasteins are generally characterized by their low solubility in water. If during the resynthesis reaction a part of the product becomes insoluble, this serves as a driving force. Aso et al. (56, 57) investigated some physicochemical properties of a water-insoluble fraction of a plastein produced from a soybean globulin hydrolysate. This fraction interacted with l-anilino-8-naphthalene sulfonate (ANS) to give a new and larger ANS emission spectrum at 450 nm (Table II). [Pg.167]

Normalized relative to the activity to soybean globulin. Source Vaintraub et al., Ref. 46. Reprinted by permission. [Pg.100]

Protein pyrolysates Albumin Soybean globulin Calf thymus Egg white Serum albumin Casein collagen ... [Pg.1232]

Yoshida, D, T. Matsumoto, R. Yoshimura, and T. Matsuzaki Mutagenicity of amino-a-carbolines in pyrolysis products of soybean globulin Biochem. Biophys. Res. Comm. 83 (1978) 915-920. [Pg.1434]

Lovati, M.R. C. Manzoni A. Corsini A. Granata R. Frattini R. Fum alli C.R. Sirtori. Low density lipoprotein receptor activity is modulated by soybean globulins in cell culture. J. Nutr. 1992,122, 1971-1978. [Pg.267]

Yamauchi, R M. Sato W. Sato Y. Kamata K. Shibasaki. Isolation and purification of new types of P-conglycinin in soybean globulins. Agric. Biol Chem. 1981, 45, 2893. [Pg.273]

Koshiyama, I. Chemical and physical properties of a 7s protein in soybean globulins. Cereal Chem. 1968a, 45, 394-404. [Pg.727]

Roberts, R.C. D.R. Briggs. Isolation and characterization of the 7s component of soybean globulins. Cereal Chem. 1965, 42, 71-85. [Pg.729]

POL Polyakov, V.I., Grinberg, V.Ya., and Tolstoguzov, V.B., Application of phase-volume-ratio method for determining the phase diagram of water-casein-soybean globulins system, Polym. Bull, 2, 757,1980. [Pg.706]

Fig. 16.2. Soybean globulin as an emulsifier. (According to Aoki et al., 1980). The capacity of an o/w-emulsion after addition of 11S globulin (-0-) and 7 S globulin (- -) is plotted versus pH... Fig. 16.2. Soybean globulin as an emulsifier. (According to Aoki et al., 1980). The capacity of an o/w-emulsion after addition of 11S globulin (-0-) and 7 S globulin (- -) is plotted versus pH...
Polyakov, V. L, Grinberg, V. Ya, Tolstoguzov, V. B. (1980). Application of Phase-Volume Ratio Method for Determining the Phase Diagram of Water-Casein-Soybean Globulins System. Polymer Bulletin, 2,160-161. [Pg.243]


See other pages where Soybean globulin is mentioned: [Pg.153]    [Pg.167]    [Pg.526]    [Pg.526]    [Pg.43]    [Pg.224]    [Pg.25]    [Pg.369]    [Pg.369]    [Pg.39]    [Pg.57]    [Pg.163]    [Pg.166]    [Pg.167]    [Pg.168]    [Pg.177]    [Pg.180]    [Pg.100]    [Pg.845]    [Pg.1375]    [Pg.73]    [Pg.283]   
See also in sourсe #XX -- [ Pg.226 ]




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