The Influence of Processing Parameters on Food Protein Functionality I. Differential Scanning Calorimetry as an Indicator of Protein Denaturation

Arntfield, Susan D.; Murray, E.D.

doi:10.1016/s0315-5463(81)72929-8

Cited by 273 publications

(171 citation statements)

References 10 publications

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“…The ΔH D represented the extent of the ordered structure of a protein. [22] Thus, the data suggested that the extent of the ordered structure of Yak solution was gradually increased with the molecular weight. It was suggested that the endothermic peak of the gelatin in the DSC profile was mainly caused by the protein denaturation or the disruption of hydrogen bonds between protein and water.…”

Section: Uv-vis Absorption Spectra Of Gelatinmentioning

confidence: 96%

Molecular structural properties of extracted gelatin from Yak skin as analysed based on molecular weight

Wei

et al. 2017

International Journal of Food Properties

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This paper dealt with the physicochemical, functional and antioxidative properties of Yak skin gelatins with various molecular weights. The gelatin was extracted by alkaline process, and different molecular weight gelatin was achieved by ultrafiltration with different molecular weight cut membrane. The SDS-PAGE showed the molecular weight of the yak skin gelatin. The UV-Vis absorption turned out that the high molecular weight (HMW) of yak skin gelatin had a higher maximum absorption peaks. The FT-IR indicated the change of gelatin structures with the change of the molecular weight. No matter the HMW or the low molecular weight (LMW), the Yak skin gelatin had a high denaturation temperature (T d ), and it was higher than most of the other mammals and marine biological gelatin. The HMW gelatin had higher imino acids contents and lower oxidation resistance, foamability and emulsibility compared to the LMW gelatin. These findings showed that a certain molecular weight range of Yak skin gelatin has great potential for application as an alternative to commercial gelatin due to its good antioxidative, foamability emulsibility and thermotolerance.ARTICLE HISTORY

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Section: Uv-vis Absorption Spectra Of Gelatinmentioning

confidence: 96%

Molecular structural properties of extracted gelatin from Yak skin as analysed based on molecular weight

Wei

et al. 2017

International Journal of Food Properties

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“…Changes associated with absorption or evolution of heat in the sample cause a differential heat flow, which is recorded graphically as a thermogram. DSC has been employed to study effects of heatinduced phase transitions of starch and protein systems [3,4]. Heat changes associated with such transitions are measured and related to functionality.…”

Section: Introductionmentioning

confidence: 99%

Thermal properties of cowpea flour: A study by differential scanning calorimetry

Henshaw¹,

McWatters

Akingbala

et al. 2003

Nahrung

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The thermal properties of 12 varieties of cowpea flour were studied by differential scanning calorimetry (DSC). Flour samples were prepared to a paste of 60% moisture content and sealed in standard DSC pans. Samples were scanned at a heating rate of 5 degrees C/min over a scan range of 40- 130 degrees C. Samples exhibited single major endotherms, which occurred over varied temperatures. The transition enthalpy (deltaH) ranged between 1.4 J/g and 4.7 J/g. Transition onset (T(o)) and transition peak (T(p)) temperatures ranged between 75-78 degrees C and 78-82 degrees C,respectively. All the DSC parameters measured varied significantly among the varieties. The transition enthalpy (deltaH) was the most discriminating parameter and accounted for 80% of the total variance. The major chemical components of cowpea flour, starch amylose and protein are significant predictors of deltaH. Protein denaturation appears to be a significant modification which occurs during processing of cowpea seeds to flour. The transition enthalpy deltaH could become an important functional index of cowpea flour when related to some quality parameters in products that contain the flour.

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“…The SPF samples showed a endothermic peak (∆H = 4.92 ± 0.5 J/ g protein) around 89.3± 0.7 o C, which is in line with other values reported for pea protein denaturation temperature Shand et al 2007;Kozhevnikov et al 2001). The CPI sample did not show a distinguished endothermic peak, which is reported by more authors for other commercial pea protein isolates (Arntfield and Murray 1981;Shand et al 2007;. The absence of endothermic peak in the CPI indicates that the sample is already denatured during previous processing, whereas the SPF sample is still in their native state.…”

Section: Functional Properties 3421 Protein Transition Statesupporting

confidence: 58%

“…Overall, this protein fractionation method uses chemicals (acids and bases) and high drying temperatures to allow complete disentanglement of the original structures and extract the individual components. However, pH and the heat treatment are linked to a loss in (native) protein functionality (Arntfield and Murray 1981;Taherian et al 2011;Wang and Corredig 2011;Denmat et al 1999), and negative impact on the environment Schutyser and van der Goot 2011).…”

Section: Introductionmentioning

confidence: 99%

Functionality-driven fractionation the need for mild food processing

Geerts¹

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The Influence of Processing Parameters on Food Protein Functionality I. Differential Scanning Calorimetry as an Indicator of Protein Denaturation

Cited by 273 publications

References 10 publications

Molecular structural properties of extracted gelatin from Yak skin as analysed based on molecular weight

Molecular structural properties of extracted gelatin from Yak skin as analysed based on molecular weight

Thermal properties of cowpea flour: A study by differential scanning calorimetry

Functionality-driven fractionation the need for mild food processing

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