Polymerization of soybean 11S globulin due to reactions with peroxidizing linoleic acid.

Shimada, Kaoru; Matsushita, Setsuro

doi:10.1271/bbb1961.42.781

Cited by 5 publications

(1 citation statement)

References 2 publications

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“…This result suggested that most of the disulfide-linked acidic polypeptides of aggregates in protein particles were cleaved into monomers after treatment by TB + 2-ME. The basic polypeptides have a larger amount of hydrophobic amino acid than the acidic ones , . The disulfide bonds between basic polypeptides may be buried in the hydrophobic regions and hard for 2-ME to attack in the absence of urea and SDS.…”

Section: Resultsmentioning

confidence: 99%

Structural Characterization of Heat-Induced Protein Particles in Soy Milk

Ren

Tang

Zhang

et al. 2009

J. Agric. Food Chem.

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This study analyzed the aggregation mode of polypeptides in protein particles of soy milk by using ultracentrifugation, gel filtration, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The results show that the protein particles in soy milk were mainly formed by various complex protein aggregates. These protein aggregates were mainly composed of the basic and acidic polypeptides of glycinin (11S), which interact with each other via disulfide bonds, and a very small amount of the disulfide-linked alpha' and alpha subunits of beta-conglycinin (7S). Moreover, the protein aggregates and a part of monomeric subunits of 7S and 11S form protein particles through non-covalent interactions, especially hydrophobic interactions and hydrogen bonds. It is suggested that the polymerized basic polypeptides should be located inside the protein particles, whereas the acidic polypeptides of 11S, alpha' and alpha subunits are located outside them.

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Section: Resultsmentioning

confidence: 99%

Structural Characterization of Heat-Induced Protein Particles in Soy Milk

Ren

Tang

Zhang

et al. 2009

J. Agric. Food Chem.

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Ernährungsphysiologische Untersuchungen an acetylierten Vicia‐faba‐Proteinfraktionen

Uhlig¹,

Proll²,

Noack³

et al. 1980

Nahrung

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The nutritional-physiological value of an easily soluble and of a difficulty soluble fraction of protein from Vicia faba (showing a degree of acetylation of 0%, 43% and 94%, respectively) was characterized by determining the amino-acid content, the enzymatic amino-acid availability and the nitrogen balance in the rat. The results from both the amino-acid analysis and the animal experiments on the biological value evidenced that the nutritional-physiological value of the easily soluble fraction of protein from Vicia faba is significantly lower, which is in particular attributable to its lower content of sulphur-containing amino acids. Acetylation did not reduce the nutritional-physiological value of the easily soluble fraction of protein from Vicia faba, and impaired that of the difficulty soluble fraction but slightly. From the viewpoint of nutritional physiology, there are no objections against the use of these protein fractions as food additives.

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Metals and lipid oxidation. Contemporary issues

Schaich

1992

Lipids

180

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Lipid oxidation is now recognized to be a critically important reaction in physiological and toxicological processes as well as in food products. This provides compelling reasons to understand what causes lipid oxidation in order to be able to prevent or control the reactions. Redox-active metals are major factors catalyzing lipid oxidation in biological systems. Classical mechanisms of direct electron transfer to double bonds by higher valence metals and of reduction of hydroperoxides by lower valence metals do not always account for patterns of metal catalysis of lipid oxidation in multiphasic or compartmentalized biological systems. To explain why oxidation kinetics, mechanisms, and products in molecular environments which are both chemically and physically complex often do not follow classical patterns predicted by model system studies, increased consideration must be given to five contemporary issues regarding metal catalysis of lipid oxidation: hypervalent non-heme iron or iron-oxygen complexes, heme catalysis mechanism(s), compartmentalization of reactions and lipid phase reactions of metals, effects of metals on product mixes, and factors affecting the mode of metal catalytic action.

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Polymerization of soybean 11S globulin due to reactions with peroxidizing linoleic acid.

Cited by 5 publications

References 2 publications

Structural Characterization of Heat-Induced Protein Particles in Soy Milk

Structural Characterization of Heat-Induced Protein Particles in Soy Milk

Ernährungsphysiologische Untersuchungen an acetylierten Vicia‐faba‐Proteinfraktionen

Metals and lipid oxidation. Contemporary issues

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