2006
DOI: 10.1111/j.1365-2621.2005.tb07140.x
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Abstract: ABSTRA ABSTRA ABSTRA ABSTRA ABSTRACT CT CT CT CT: S : S : S : S : Studies w tudies w tudies w tudies w tudies wer er er er ere conducted to ev e conducted to ev e conducted to ev e conducted to ev e conducted to evaluate the effect of sucr aluate the effect of sucr aluate the effect of sucr aluate the effect of sucr aluate the effect of sucrose (0% to 60% w/w) on the heat denatur ose (0% to 60% w/w) on the heat denatur ose (0% to 60% w/w) on the heat denatur ose (0% to 60% w/w) on the heat denatur ose (0% to 6… Show more

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Cited by 22 publications
(15 citation statements)
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“…As reported by Babij et al (1991), about 200 lysine residues exist in a molecule of myosin heavy chain, and about 120 glucose and 60 maltose molecules were considered to be conjugated with a myosin heavy chain such decreases in solubility and suggested that the cause depended on heat denaturation of the myofibrillar proteins. Protein is known to be stabilized in the presence of glucose (Boye et al, 1996;Chen and Chang, 1998;Christ et al, 2005). As shown in Figures 1A and 1B, the progress of the Maillard reaction were similar among the myofibrillar protein-glucose systems, indicating that the loss of protein solubility with a decrease in glucose concentration in protein-glucose mixture ( Figures 2D and 2E) seems to be caused by a shortage of glucose as a thermal protectant.…”
Section: Resultsmentioning
confidence: 70%
“…As reported by Babij et al (1991), about 200 lysine residues exist in a molecule of myosin heavy chain, and about 120 glucose and 60 maltose molecules were considered to be conjugated with a myosin heavy chain such decreases in solubility and suggested that the cause depended on heat denaturation of the myofibrillar proteins. Protein is known to be stabilized in the presence of glucose (Boye et al, 1996;Chen and Chang, 1998;Christ et al, 2005). As shown in Figures 1A and 1B, the progress of the Maillard reaction were similar among the myofibrillar protein-glucose systems, indicating that the loss of protein solubility with a decrease in glucose concentration in protein-glucose mixture ( Figures 2D and 2E) seems to be caused by a shortage of glucose as a thermal protectant.…”
Section: Resultsmentioning
confidence: 70%
“…Monosaccharides and disaccharides have a positive effect on various food proteins. Glucose, sucrose, and lactose increased the Td and denaturation enthalpy of the food proteins such as bovine serum albumin (BSA) (Boye, Alli, and Ismail 1996a), β-lactoglobulin (Boye, Ismail, and Alli 1996b), and egg proteins (ovalubumin and ovotransferrin) (Christ, Takeuchi, and Cunha 2005). Figure 9.1 shows the effect of sucrose on the thermal denaturation of BSA measured by ultrasensitive DSC.…”
Section: Stabilization Of Proteins In the Presence Of Saccharidesmentioning
confidence: 97%
“…The improved thermal stability of proteins in the presence of saccharides leads to an increase in the gel transition temperature (Figure 9.4) and a delay in the gel-forming process. The gelation temperature of BSA (Baier and McClements 2001), whey protein (Dierckx and Huyghebaert 2002), and hen egg albumin (Christ, Takeuchi, and Cunha 2005) sols increased in the presence of lowmolecular-weight saccharides, such as sucrose and sorbitol. Saccharides often inhibit the heat-induced gel formation of proteins and alter the gel properties.…”
Section: Effects Of Saccharides On the Gel Formation Of Proteinsmentioning
confidence: 98%
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“…In other words, the properties of ovalbumin can be improvement by heating in dry state 2. According to Divair et al,3 the gel mechanical properties and network density of the ovalbumin showed a strong dependence on heat treatment temperature (70, 80, and 90°C). The equilibrium stress of egg‐white and ovalbumin gels using the statistical theory of rubber elasticity suggested that 3.9 covalent disulfide crosslinks per ovalbumin molecule were formed on gelling 4.…”
Section: Introductionmentioning
confidence: 99%