Studies of Thermal Denaturation of Oat Globulin by Differential Scanning Calorimetry

Ma, Ching‐Yung; Harwalkar, V. R.

doi:10.1111/j.1365-2621.1988.tb07749.x

Cited by 70 publications

(57 citation statements)

References 22 publications

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“…Increases in T d during heating may be due to re-arrangement of the pre-heated protein molecules to assume a compact, ordered conformation with higher thermal stability than the unassociated native protein. Similar changes in DSC characteristics have been observed in oat globulin pre-heated at 100 and 110°C (Ma & Harwalkar, 1988). For oat globulin, a progressive decrease in DT 1/2 value was also observed, indicating highly cooperative denaturation of the pre-heated protein.…”

Section: Effect Of Heatingsupporting

confidence: 73%

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Thermal properties of globulin from rice (Oryza sativa) seeds

Ellepola

2006

Food Research International

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Section: Effect Of Heatingsupporting

confidence: 73%

“…hydrogen bonds, hydrophobic bonds, ionic interactions, and covalent disulfite bonds Ma & Harwalkar, 1988). Heat treatments may also trigger protein aggregation.…”

Section: Introductionmentioning

confidence: 99%

Thermal properties of globulin from rice (Oryza sativa) seeds

Ellepola

2006

Food Research International

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“…This result suggests that soybean proteins in the presence of high calcium content may aggregate to form compact structures with higher cooperativity; a similar behavior was detected in preheated vegetable proteins (21).…”

Section: Resultsmentioning

confidence: 60%

Characterization of soybean protein isolates The effect of calcium presence

Scilingo

Añón

2004

J Americ Oil Chem Soc

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Results of a study of the effect of calcium addition on polypeptide composition, hydrophobicity, sulfhydryl content, thermal stability, enthalpy of denaturation, and water solubility of soybean protein isolates suggest that the addition of small amounts of calcium (1.23-5.0 mg/g protein) induced the formation of α,α′ soluble aggregates, whereas large amounts (5.0-9.73 mg/g protein) induced the selective insolubilization of the glycinin fraction. The addition of this ion also produced thermal stabilization of the soybean proteins, mainly the glycinin fraction, and increased the enthalpy of denaturation. A decrease in the surface hydrophobicity of proteins with increasing calcium content was also observed. The results obtained suggested the existence of specific calcium-soy protein interactions, especially with the glycinin fraction.New food ingredients with good-quality protein and low cost currently are being sought. Many of those being investigated include soy protein because soybean seeds contain a high amount of protein with good nutritional quality. Furthermore, glycinin (11S) and β-conglycinin (7S) globulins, the major components of soy protein isolates, possess appropriate functional properties for food applications. The structure and conformation of these proteins as well as substances present during the isolation procedure influence these properties.Macromolecules are affected by salts. These effects will depend not only on salt concentration (ionic strength) but also on their nature (lyotropic effect). According to Hofmeister's series, which arranges ions according to the lyotropic effect they may have, the calcium ion is located at the end of this series, corresponding to those ions that promote protein saltingin, leading to destabilization of the native structure (1).Calcium is an essential mineral, either by itself or when replacing sodium. It participates in the etiology or control of two widespread diseases: osteoporosis and arterial hypertension (2). Moreover, calcium intakes are often far below the recommended levels. Accordingly, its incorporation into nondairy foods is an appropriate method for achieving adequate intake.Although the interactions between soy proteins and calcium have been studied (3-7), no consensus has been reached. Although some researchers support the existence of specific interactions (4,7), others disagree (5).The aims of this study were to obtain soy protein isolates enriched by calcium addition and to study the influence of this ion on some protein structural parameters and on the water solubility of the isolates. MATERIALS AND METHODS Preparation of isolates.Protein isolates were prepared from hexane-defatted soy flour (Bunge-Ceval, Brazil) containing 50% protein (NSI 78-80). The flour was extracted with water adjusted to pH 8.0 with 2 N NaOH (flour/water ratio of 1:10 wt/vol) at room temperature for 2 h. The pH was periodically readjusted to 8.0. This suspension was filtered through gauze, and the filtered material was centrifuged at 10,000 × g at 4°C for 30 min. The sup...

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“…However, this contribution can also come from amorphous amylose-lipid complexes that dissociate at temperature lower than 100°C and can be present in native cereal materials 27,35 . Enthalpy values reported in Table 4 are within those reported for protein denaturation in rice and oat products (including protein fractions and flours), which vary from 6 to 26 J/g 30,33,36 . The values characterizing the third transition in Figure 2, are shown in Table 5.…”

Section: Pasting and Thermal Behavior In Excess Of Watermentioning

confidence: 74%

“…6 gives χ AB =0. 36. This theoretical value of the polymer-diluent interaction factor is also shown in Table 7.…”

Section: Methodsmentioning

confidence: 89%

Thermal Characterization and Phase Behavior of a Ready-to-Eat Breakfast Cereal Formulation and its Starchy Components

et al. 2009

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Gelatinization in excess of water and melting transition for different moisture contents of a ready-to-eat cereal formulation (RTE blend) and its major components, (i.e., oat flour, rice flour, and an oat-rice flour blend) were studied by differential scanning calorimetry (DSC) and rapid visco-analyzer (RVA). The highest swelling power was exhibited by the rice flour and the lowest by the RTE blend. Two endothermic peaks under excess of water were exhibited by all materials, at 53-75°C and 80-102°C, and they were associated to gelatinization and cereal protein denaturation, respectively. A third peak appearing in all materials except in rice flour, at higher temperatures (102-116°C), was attributed to the melting of the amylose-lipid complexes. The effect of water in the melting of the flours and blends was well described by the Flory-Huggins equation and its parameters agreed well with those reported in the literature for starchy products. A theoretical value of the polymer-diluent (starchwater) interaction factor for starch of 0.36 was calculated from a combined model of Hildebrand empirical approach to solubility and the Flory-Huggins theory, and reasonably compared with the interaction parameter (χ) obtained for the materials considered in this work. State diagrams for the oat-rice flour blend and for the RTE blend going through an extrusion process were finally obtained.

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Studies of Thermal Denaturation of Oat Globulin by Differential Scanning Calorimetry

Cited by 70 publications

References 22 publications

Thermal properties of globulin from rice (Oryza sativa) seeds

Thermal properties of globulin from rice (Oryza sativa) seeds

Characterization of soybean protein isolates The effect of calcium presence

Thermal Characterization and Phase Behavior of a Ready-to-Eat Breakfast Cereal Formulation and its Starchy Components

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