1989
DOI: 10.1111/j.1365-2621.1989.tb04661.x
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Preparation and Functional Properties of Enzymatically Deamidated Soy Proteins

Abstract: Heat‐denatured soy protein was hydrolyzed by Alcalase to 2.0% or 4.0% degree of hydrolysis (DH), heated again at 100°C and deamidated with B. circulans peptidoglutaminase. The extent of deamidation was 6.0% and 8.2% for 2.0 DH hydrolysates and 12.8% and 16.0% for 4.0 DH hydrolysates heated for 15 and 30 min, respectively. Deamidation increased protein solubility and substantially enhanced emulsifying activity under mildly acidic (pH 4–6) as well as alkaline conditions. Deamidation improved emulsion stability a… Show more

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Cited by 56 publications
(41 citation statements)
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“…Protein solubility profiles were determined by using the method of Hamada and Marshall (12). (iii) Foaming properties.…”
Section: Soymentioning
confidence: 99%
“…Protein solubility profiles were determined by using the method of Hamada and Marshall (12). (iii) Foaming properties.…”
Section: Soymentioning
confidence: 99%
“…Enzymatic modification is usually performed through limited proteolysis (Puski 1975, Feeney and Whitaker 1977, Hamada and Marshall 1989, Bernardi et al 1991. Adler-Nissen and Olsen (1979) reported improved emulsifying capacity, solubility, and foaming capacity of soy protein after a1calase and neutrase treatment.…”
Section: Enzymatic Methodsmentioning
confidence: 99%
“…For soy proteins to have the desired functional properties, several methods of protein modification have been used, including physical. chemical, and enzymatic methods (Puski 1975, Feeney and Whitaker 1977, Kinsella 1979, Sung et aL 1983, Hamada 1989.…”
Section: Modification Of Soy Proteinsmentioning
confidence: 99%
“…Deamidation has been shown to affect protein functionality. Functional properties, such as solubility, emulsifying and foaming properties, of gluten have been reported to improve upon low levels of deamidation brought about by mild acid hydrolysis (Hamada & Marshall, 1989;Matsudomi et al, 1982Matsudomi et al, , 1985. Deamidation also was reported to increase exposed hydrophobicity of gluten induced by a conformational change and, subsequently, to increase surface activity (Matsudomi et al, 1982).…”
Section: Deamidationmentioning
confidence: 99%