Thermal Denaturation of Human Lactoferrin and Its Effect on the Ability To Bind Iron

Mata, Luis; Sánchez, Lourdes; Headon, Denis R.; Calvo, Miguel

doi:10.1021/jf980266d

Cited by 68 publications

(53 citation statements)

References 28 publications

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“…Thermal stability data of LF from different species have been reported (Bezwoda & Mansoor, 1989;Conesa et al, 2008;Mata, Sanchez, Headon, & Calvo, 1998;Nam, Shimazaki, Kumura, Lee, & Yu, 1999;Paulsson et al, 1993). In the present study, one thermal transition peak was evident for both cLF and bLF in the temperature range between 35 and 90 C. This depends on the detection limits of the analytical equipment used.…”

Section: Effect Of Ph On Thermal Denaturation Temperature Of Lactoferrinsupporting

confidence: 48%

A comparison of effects of pH on the thermal stability and conformation of caprine and bovine lactoferrin

Sreedhara

Flengsrud

Prakash

et al. 2010

International Dairy Journal

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Section: Effect Of Ph On Thermal Denaturation Temperature Of Lactoferrinsupporting

confidence: 48%

A comparison of effects of pH on the thermal stability and conformation of caprine and bovine lactoferrin

Sreedhara

Flengsrud

Prakash

et al. 2010

International Dairy Journal

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“…In some cases, specific ion-protein binding (20) produces an increase of the denaturing ∆H due to the presence of the ion. This phenomenon would explain the ∆H increase in some calcium-containing isolates (samples 2 and 3).…”

Section: Resultsmentioning

confidence: 99%

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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“…There are reports on using the Kissinger method to determine the activation energy for denaturation of lactoglobulin, [25][26][27][28][29][30] whey proteins, [31] and lactoferrin. [32] The method evaluates the activation energy from the shift in the DSC peak temperature, T p , with the heating rate, b i , as follows:…”

Section: Kinetic Computationsmentioning

confidence: 99%

Thermal Denaturation of Collagen Analyzed by Isoconversional Method

Vyazovkin¹,

Vincent²,

Sbirrazzuoli³

2007

Macromolecular Bioscience

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An isoconversional method is proposed to be used for evaluating activation energy of protein denaturation. Applied to DSC data on collagen denaturation, the method yields an activation energy that decreases throughout the process. The Lumry-Eyring model gives an explanation for this decrease and affords estimates for the enthalpy of the reversible step and the activation energy of the irreversible step of denaturation. The reversible unfolding is detectable by multi-frequency temperature-modulated DSC.

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Thermal Denaturation of Human Lactoferrin and Its Effect on the Ability To Bind Iron

Cited by 68 publications

References 28 publications

A comparison of effects of pH on the thermal stability and conformation of caprine and bovine lactoferrin

A comparison of effects of pH on the thermal stability and conformation of caprine and bovine lactoferrin

Characterization of soybean protein isolates The effect of calcium presence

Thermal Denaturation of Collagen Analyzed by Isoconversional Method

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