1992
DOI: 10.1016/0308-8146(92)90221-m
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Comparative performance of chemically and enzymatically modified whey proteins

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Cited by 24 publications
(32 citation statements)
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“…The wild-type BLGA, R40C, and F82C rBLGs were capable of forming gels when heated; however, the minimum protein and gelation temperature in addition to the strength of the resulting gels varied significantly. The strength of the gels was measured by the microscale penetrometry which permitted the use of small sample volumes, an important factor given the limited supply of rBLG (Lee and Batt, 1993). Wildtype BLGA when heated at 90 "C for 15 min formed gels with strengths of 14-19 g over a concentration range of 9.4-10% (Figure 2).…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…The wild-type BLGA, R40C, and F82C rBLGs were capable of forming gels when heated; however, the minimum protein and gelation temperature in addition to the strength of the resulting gels varied significantly. The strength of the gels was measured by the microscale penetrometry which permitted the use of small sample volumes, an important factor given the limited supply of rBLG (Lee and Batt, 1993). Wildtype BLGA when heated at 90 "C for 15 min formed gels with strengths of 14-19 g over a concentration range of 9.4-10% (Figure 2).…”
Section: Resultsmentioning
confidence: 99%
“…Gel strength was measured on 20-pL samples using a microscale penetrometer as described (Lee and Batt, 1993). The weight necessary to penetrate the sample to a depth of 33 % of the original height was recorded.…”
Section: Methodsmentioning
confidence: 99%
“…There have been several studies on the digestibility of deamidated proteins, [22][23][24] but there is no information available on that of deamidated gliadin. Little difference in the in vitro peptic digestibility of gliadin (Fig.…”
Section: Discussionmentioning
confidence: 99%
“…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%
“…Deamidation can improve the solubility and other functional properties of food proteins by increasing the number of negative charges in the protein (Lakkis & Villota, 1992) and then increase the quality and acceptability of a food protein product by improving stability and mouth-feel (Webb, Naeem, & Schmidt, 2002). Therefore, considerable researches have focused on catalyzing the deamidation of proteins (such as rice protein, wheat gluten and zein) by acids, bases and enzymes with different reaction mechanisms (Berti et al, 2007;Paraman, Hettiarachchy, & Schaefer, 2007;Yong, Yamaguchi, Gu, Mori, & Matsumura, 2004).…”
Section: Introductionmentioning
confidence: 99%