Measurement of unfrozen and free water in soy proteins by differential scanning calorimetry

Muffett, Dorothy J.; Snyder, Harry E.

doi:10.1021/jf60232a069

Cited by 29 publications

(20 citation statements)

References 2 publications

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“…Differential thermal analysis (DTA) and differential scanning calorimetry (DSC) are two recently-developed techniques available to the food industry for multi-purpose uses. DTA was used by Duckworth [9], Parducci and Duckworth [10] and Bushuk and Mehrotra [11,12], while Ross [5], Karmas and Chen [13], Muffet and Snyder [14], Kumagai et al [15], Roos [6,16,17], Lovric et al [18], Heinevetter et al [19], Roos and Karel [20] and Wang and Kolbe [21] applied DSC to determine the free and bound water contents of different food products and biological materials.…”

Section: Introductionmentioning

confidence: 99%

Determination of freezable water content of beef semimembranous muscle DSC study

Aktaş

Tülek

Gökalp

1997

Journal of Thermal Analysis

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The freezable water contents of samples obtained from previously chilled semimembranous muscle of middle-aged beef carcasses after a 24 h cooling period a room at in 5+1~ were determined by differential scanning calorimetry (DSC) at -5, -10, -15, -20, -30, --40, -50 and -65~ This was accomplished by freezing the samples at the above-mentioned temperatures, followed by thawing to 35~ and measuring the melting peaks of freezable water. The areas of these peaks were determined by using the peak integration method programs through a computer linked to the DSC, and they were then used to determine the latent heat of melting (AHm) in kJ kg -~ at each freezing temperature. The resultant latent heat of melting per sample was divided by the latent heat for pure water to determine the amount of freezable water present in these samples. This amount of freezable water was divided by the total water content of the meat sample to determine the percentage of freezable water in the sample. The percentage of freezable water was subtracted from 100 to determine the percentage of bound water present in the sample.

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Section: Introductionmentioning

confidence: 99%

Determination of freezable water content of beef semimembranous muscle DSC study

Aktaş

Tülek

Gökalp

1997

Journal of Thermal Analysis

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“…Schnepf (2) reviewed the types of bonding between water and protein molecules, and how their interaction relates to these functional properties. Numerous methods for assessing protein hydration include dielectric studies (3), nuclear magnetic resonance (4)(5)(6)(7)(8) and calorimetry (9)(10)(11)(12)(13).…”

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confidence: 99%

Thermal densturation of glycinin as a function of hydration

Sessa

1993

J Americ Oil Chem Soc

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Hydration effects on the thermal stability of glycinin (soybean 11S protein) were examined by differential scanning calorimetry (DSC). In a model system with pure glycinin, the denaturation temperature (Td) decreased with increasing moisture. Between 22 and 44% moisture, two endotherms were observed, where the lower‐temperature endotherm became progressively reduced in magnitude with a concomitant increase in a higher‐temperature transition. At 45.5% moisture, only a single endotherm was observed. The regression curves over the entire moisture range from 2 to 66% were derived as asymptote functions, where M equals the percentage total moisture. Equations were developed from the curves, and the relationship between Td and moisture were: Td=92.4+196.5e−0.068M and, for the low‐temperature endotherm, 82.4+144.3e−0.068M. By interaction of 11S protein with either ethanol, a neutral detergent (Triton X‐100) or 40% sucrose, both one‐ and two‐endotherm curves were generated. Such calorimetric behavior is indicative of nonequilibrium denaturation and supports the notion that structure reorganization during DSC is water content‐dependent. Our findings suggest that either glycinin’s acidic/basic subunits or a change in secondary protein structure may give rise to two endotherms.

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“…In fact, an endothermic peak around 0°C, which would correspond to the melting of crystallizable (unbound) water, was not observed. Thus, it was concluded that the water molecules situated in the feathermeal were bound to the protein macromolecules 15…”

Section: Resultsmentioning

confidence: 99%

Biodegradable plastics from animal protein coproducts: Feathermeal

Sharma

Hodges

Luzinov

2008

J of Applied Polymer Sci

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This work describes the properties of plastics made from partially denatured proteins produced by the animal coproduct (rendering) industry and these plastics' fabrication. Specifically, plastic samples from partially denatured feathermeal protein were successfully produced by a compression-molding process. The modulus (stiffness) of the material obtained was found to be comparable with that of commercial synthetic materials, such as polystyrene, but was found to have lower toughness characteristics, which is a common phenomenon among plastics produced from animal and plant proteins. A reversible stress-strain property was observed over the yield region. Plastic-forming conditions for undenatured animal proteins, such as albumen and whey proteins, were also formulated for fabricating plastics out of these proteins' blends with feathermeal proteins. The resultant plastic samples that were developed of biomacromolecular blends, such as feathermeal/whey and feathermeal/ albumen, demonstrated improved mechanical properties, specifically tensile strength, when compared with neat plastics from feathermeal proteins. The values for the stiffness of the feathermeal/whey blends deviated from simple mixing rule and showed a synergistic effect.

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Measurement of unfrozen and free water in soy proteins by differential scanning calorimetry

Cited by 29 publications

References 2 publications

Determination of freezable water content of beef semimembranous muscle DSC study

Determination of freezable water content of beef semimembranous muscle DSC study

Thermal densturation of glycinin as a function of hydration

Biodegradable plastics from animal protein coproducts: Feathermeal

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