Beta-lactoglobulin removal from whey protein concentrates

Lucena, María Eugenia; Álvarez, Silvia; Menéndez, Carlos; Riera, Francisco A.; Álvarez, Roberto

doi:10.1016/j.seppur.2006.05.006

Cited by 38 publications

(2 citation statements)

References 18 publications

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“…Similar chromatographic profiles for β-lactoglobulin were observed previously (Lucena, Alvarez, Menendez, Riera, & Alvarez, 2006).…”

Section: Chromatographicprofilesofβ-lactoglobulinsupporting

confidence: 87%

Ultrasound‐induced changes in structural and physicochemical properties of β‐lactoglobulin

Zhao

et al. 2018

Food Science & Nutrition

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Effect of ultrasound treatment on the physicochemical properties and structure of β‐lactoglobulin were investigated. β‐Lactoglobulin was treated with ultrasound at different amplitudes, temperatures, and durations. The surface hydrophobicity and free sulfhydryl group of β‐lactoglobulin were significantly increased after ultrasound treatment (p < .05). The maximal surface hydrophobicity and free sulfhydryl group were 5,812.08 and 5.97 μmol/g, respectively. Ultrasound treatment changed the physicochemical properties of β‐lactoglobulin including particle size (from 1.21 ± 0.05 nm to 1.66 ± 0.03 nm), absolute zeta potential (from 15.47 ± 1.60 mV to 27.63 ± 3.30 mV), and solubility (from 84.66% to 95.17%). Ultrasound treatment increased α‐helix and β‐sheet structures of β‐lactoglobulin. Intrinsic fluorescence intensity of ultrasound‐treated β‐lactoglobulin was increased with shift of λmax from 334 to 329 nm. UV absorption of β‐lactoglobulin was decreased with shift of λmax from 288 to 285 nm after ultrasound treatment. There were no significant changes in high‐performance liquid chromatography and protein electrophoretic patterns. These findings indicated that ultrasound treatment had high potential in modifying the physiochemical and structural properties of β‐lactoglobulin for industrial applications.

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“…Similar chromatographic profiles for β-lactoglobulin were observed previously (Lucena, Alvarez, Menendez, Riera, & Alvarez, 2006).…”

Section: Chromatographicprofilesofβ-lactoglobulinsupporting

confidence: 87%

Ultrasound‐induced changes in structural and physicochemical properties of β‐lactoglobulin

Zhao

et al. 2018

Food Science & Nutrition

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“…Under these conditions, α-la forms precipitates, most likely caused by a combination of hydrophobic and electrostatic interactions [26]. The formed precipitates enable a size-based separation either by microfiltration [10,27] or centrifugation [18,28,29].…”

Section: Introductionmentioning

confidence: 99%

Molecular Analytical Assessment of Thermally Precipitated α-Lactalbumin after Resolubilization

Haller

Maier

Kulozik

2021

Foods

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Selective thermal precipitation followed by a mechanical separation step is a well described method for fractionation of the main whey proteins, α-lactalbumin (α-la) and β-lactoglobulin (β-lg). By choosing appropriate environmental conditions the thermal precipitation of either α-la or β-lg can be induced. Whereas β-lg irreversibly aggregates, the precipitated α-la can be resolubilized by a subsequent adjustment of the solution’s pH and the ionic composition. This study reports on the analytical characterization of resolubilized α-la compared to its native counterpart as a reference in order to assess whether the resolubilized α-la can be considered close to ‘native’. Turbidity and quantification by RP-HPLC of the resolubilized α-la solutions were used as a measure of solubility in aqueous environment. RP-HPLC was also applied to determine the elution time as a measure for protein’s hydrophobicity. DSC measurement was performed to determine the denaturation peak temperature of resolubilized α-la. FTIR spectroscopy provided insights in the secondary structure. The refolding of α-la achieved best results using pH 8.0 and a 3-fold stoichiometric amount of Ca2+ per α-la molecule. The results showed that the mechanism of aggregation induced by gentle thermal treatment under acidic conditions with subsequent mechanical separation is reversible to a certain extent, however, the exact native conformation was not restored.

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High Power Ultrasound Processing in Milk and Dairy Products

Zisu¹,

Chandrapala²

2015

Emerging Dairy Processing Technologies

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Beta-lactoglobulin removal from whey protein concentrates

Cited by 38 publications

References 18 publications

Ultrasound‐induced changes in structural and physicochemical properties of β‐lactoglobulin

Ultrasound‐induced changes in structural and physicochemical properties of β‐lactoglobulin

Molecular Analytical Assessment of Thermally Precipitated α-Lactalbumin after Resolubilization

High Power Ultrasound Processing in Milk and Dairy Products

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