Conformational Changes and Functional Properties of Acid-modified Soy Protein

Matsudomi, Naotoshi; Sasaki, Tetsuyuki; Kato, Akio; Kobayashi, Kunihiko

doi:10.1080/00021369.1985.10866906

Cited by 48 publications

(76 citation statements)

References 6 publications

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“…This effect of deamidation has already been verified with some proteins. 5,6,[19][20][21] In agreement with those findings, each deamidated gliadin was more soluble in water, a salt solution, and buffered solution at neutral and alkaline pH than the undeamidated type (Fig. 2).…”

Section: Discussionsupporting

confidence: 76%

“…15) Deamidation could be used to reduce wheat allergenicity, because some tandem sequencing sites involving glutamine residues in wheat gliadin and glutenin have been reported to constitute the primary structure of IgE-binding epitopes. [16][17][18] There are several methods that can be used to deamidate proteins, including the use of acids, [19][20][21][22][23][24] enzymes, 1,[25][26][27] and cation exchangers. [2][3][4][5][6]28) Among them, an acid treatment is the most commonly used, y To whom correspondence should be addressed.…”

Section: Improvement Of Digestibility Reduction In Allergenicity Anmentioning

confidence: 99%

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Improvement of Digestibility, Reduction in Allergenicity, and Induction of Oral Tolerance of Wheat Gliadin by Deamidation

Kumagai

Suda

Sakurai

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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Section: Discussionsupporting

confidence: 76%

Section: Improvement Of Digestibility Reduction In Allergenicity Anmentioning

confidence: 99%

Improvement of Digestibility, Reduction in Allergenicity, and Induction of Oral Tolerance of Wheat Gliadin by Deamidation

Kumagai

Suda

Sakurai

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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“…Indeed, surface hydrophobicity is an important factor in determining emulsifying properties. It was previously reported that hydrophobicity exposed by a protein would allow a better molecular anchorage to be established in the oil-water interface, giving more stable emulsions (Nakai et al, 1986;Matsudomi et al, 1985). However, DGPSM contained more hydrophobic amino acid residues than DPM (Table 1).…”

Section: Emulsifying Capacity (Ec)mentioning

confidence: 94%

Nutritional and functional characteristics of gingerbread plum (<i>Neocarya macrophylla</i>): an underutilized oilseed

Amza¹,

Amadou²,

Kamara³

et al. 2011

Grasas y Aceites

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The In-vitro protein digestibility, protein nutritional quality and functional characteristics (protein solubility, water/oil binding capacity, emulsifying capacity and foaming capacity) of gingerbread plum and peanut seed flour were studied. Among the nutritional parameters, the proportion of essential amino acids to total amino acids (E/T), amino acid scores (AAS) and protein efficiency ratio (PER) were studied. Defatted gingerbread plum seed meal (DGPSM) showed a high nutritional quality with PER and AAS values of 2.35 and 65.53 respectively. The solubility profile of DGPSM was similar to that of defatted peanut meal (DPM), with minimum solubility observed at pH 4 and maximum solubility at pH 10 and higher. Water and oil holding capacities were 3.01 and 3.12; 2.96 and 3.11 g/g for DGPSM and DPM respectively. DGPSM showed good foaming capacity (145 mL /100 mL) and stability (110 mL /100 mL) even after 60 min at room temperature. The emulsifying capacity of DGPSM was 29%. Bulk densities were 0.30 and 0.28 g/mL for DGPSM and DPM respectively. Finally, DGPSM was easily hydrolyzed by trypsin in vitro. These results show that DGPSM has functional properties that may find applications in the food industry.

La digestibilidad de proteínas in vitro, la calidad nutricional de proteínas y las características funcionales (solubilidad de proteínas, capacidad de enlace agua/aceite, capacidad emulsionante y capacidad espumante) de harina de semillas de ciruela de pan de jengibre y de cacahuete fueron estudiadas. Entre los parámetros nutricionales, la relación aminoácidos esenciales/aminoácidos totales (E/T), el perfil de aminoácidos (AAS) y el coeficiente de eficacia proteica (PER) fueron estudiadas. Harina de semillas de ciruela de pan de jengibre (DGPSM) mostraron una alta calidad nutricional con unos valores de PER y de AAS de 2.35 y 65.53 respectivamente. El perfil de solubilidad de DGPSM fue similar al de la harina desengrasada de cacahuete (DPM), con una mínima solubilidad observada a pH 4 y un máximo de solubilidad a pH 10 y superior. Las capacidad de retención de agua y de aceite fueron 3.01 y 3.12; 2.96 y 3.11 g/g para DGPSM y DPM respectivamente. DGPSM mostró una buena capacidad espumante (145 mL /100 mL) and estabilidad (110 mL /100 mL) incluso después de 60 min a temperatura ambiente. La capacidad emulsionante de DGPSM fue del 29%. Las densidades fueron 0.30 y 0.28 g/ml para DGPSM y DPM respectivamente. Por último, DGPSM fue fácilmente hidrolizado por tripsina in vitro. Estos resultados mostraron que DGPSM tienen propiedades funcionales que pueden encontrar aplicación en la industria alimentaria

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“…5 -7) Since it was demonstrated in this experiment that p-aspartylurea was not digested in the rat body and excreted in urine in relatively high concentration, the existence of p-aspartylurea residues in ozoriated casein may be responsible for its low digestibility to some extent. Hydrolysis of p-aspartylurea residues of ozonated casein by a mild deamidation reaction 12 ) and feeding experiments of rats with the preparation will be presented in a subsequent paper.…”

Section: Resultsmentioning

confidence: 99%

α-Aspartylurea and 4-Methylproline in Urine of Rats Fed Ozonated Casein

Kasai¹,

Kiriyama²

1990

Agricultural and Biological Chemistry

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It has been proved in our laboratory that rats fed ozonated casein that did not contain aromatic amino acid residues besides a very small amount of phenylalanine residues had no significant unfavorable change compared with those fed casein and that ozonated casein supplemented with amino acids lost by ozonolysis has nearly the same biological value as that of casein. But some unusual ninhydrin-positive substances existed in urine of rats fed ozonatd casein. Two of them, p-aspartylurea (major component) and 4-methyl-proline (minor), were identified. It was confirmed that p-aspartylurea was formed during ozonolysis of casein in aq. solution that contained urea to solubilize casein and, therefore, present originally in ozonated casein ingested by rats. The origin of 4-methylproline is still obscure.

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Conformational Changes and Functional Properties of Acid-modified Soy Protein

Cited by 48 publications

References 6 publications

Improvement of Digestibility, Reduction in Allergenicity, and Induction of Oral Tolerance of Wheat Gliadin by Deamidation

Improvement of Digestibility, Reduction in Allergenicity, and Induction of Oral Tolerance of Wheat Gliadin by Deamidation

Nutritional and functional characteristics of gingerbread plum (<i>Neocarya macrophylla</i>): an underutilized oilseed

α-Aspartylurea and 4-Methylproline in Urine of Rats Fed Ozonated Casein

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