Effects of high hydrostatic pressure on the structure of bovine α-lactalbumin

Rodiles‐López, José Octavio; Arroyo‐Maya, Izlia J.; Jaramillo-Flores, M.E.; Gutiérrez-López, Gustavo F.; Hernández‐Arana, Andrés; Barbosa‐Cánovas, Gustavo V.; Niranjan, Keshavan; Hernández‐Sánchez, Humberto

doi:10.3168/jds.2009-2786

Cited by 36 publications

(36 citation statements)

References 41 publications

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“…The results suggest that the molten globule state of α-LA consists of a mixture of variously unfolded conformers from the mostly folded to the nearly totally unfolded that differ in stability and partial molar volume [ 112 ]. A similar conclusion was obtained in another work: High pressure produces a variety of molten globules with differences in their surface hydrophobicity and secondary and tertiary structures [ 113 ]. At pH values of 3 and 5, the increase in pressure results in a decrease in α-helix content concomitant with an increase in β-strand content.…”

Section: Unfolding Of α-Lactalbumin Caused By Heat and Various Densupporting

confidence: 87%

“…No changes in the molecular size of α-LA due to pressure-induced aggregation were detected. The pressure-treated α-LA samples showed an elevated thermal stability [ 113 ]. The second derivative Fourier transform infrared (FTIR) spectroscopy method was used to study heat-induced (20 to 80 °C) and pressure-assisted cold-induced (20 to −15 °C) changes in the secondary structure of bovine α-LA in the holo- and apo-state [ 114 ].…”

Section: Unfolding Of α-Lactalbumin Caused By Heat and Various Denmentioning

confidence: 99%

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α-Lactalbumin, Amazing Calcium-Binding Protein

Permyakov

2020

Biomolecules

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α-Lactalbumin (α-LA) is a small (Mr 14,200), acidic (pI 4–5), Ca2+-binding protein. α-LA is a regulatory component of lactose synthase enzyme system functioning in the lactating mammary gland. The protein possesses a single strong Ca2+-binding site, which can also bind Mg2+, Mn2+, Na+, K+, and some other metal cations. It contains several distinct Zn2+-binding sites. Physical properties of α-LA strongly depend on the occupation of its metal binding sites by metal ions. In the absence of bound metal ions, α-LA is in the molten globule-like state. The binding of metal ions, and especially of Ca2+, increases stability of α-LA against the action of heat, various denaturing agents and proteases, while the binding of Zn2+ to the Ca2+-loaded protein decreases its stability and causes its aggregation. At pH 2, the protein is in the classical molten globule state. α-LA can associate with membranes at neutral or slightly acidic pH at physiological temperatures. Depending on external conditions, α-LA can form amyloid fibrils, amorphous aggregates, nanoparticles, and nanotubes. Some of these aggregated states of α-LA can be used in practical applications such as drug delivery to tissues and organs. α-LA and some of its fragments possess bactericidal and antiviral activities. Complexes of partially unfolded α-LA with oleic acid are cytotoxic to various tumor and bacterial cells. α-LA in the cytotoxic complexes plays a role of a delivery carrier of cytotoxic fatty acid molecules into tumor and bacterial cells across the cell membrane. Perhaps in the future the complexes of α-LA with oleic acid will be used for development of new anti-cancer drugs.

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Section: Unfolding Of α-Lactalbumin Caused By Heat and Various Densupporting

confidence: 87%

Section: Unfolding Of α-Lactalbumin Caused By Heat and Various Denmentioning

confidence: 99%

α-Lactalbumin, Amazing Calcium-Binding Protein

Permyakov

2020

Biomolecules

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“…These findings are supported by various studies at the molecular level [31,32]. Proteins are a complex organization of subunits with primary, secondary, tertiary and quaternary structures.…”

Section: Discussionsupporting

confidence: 66%

Mechanical Characterization of Human Trabecular and Formed Granulate Bone Cylinders Processed by High Hydrostatic Pressure

et al. 2021

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One main disadvantage of commercially available allogenic bone substitute materials is the altered mechanical behavior due to applied material processing, including sterilization methods like thermal processing or gamma irradiation. The use of high hydrostatic pressure (HHP) might be a gentle alternative to avoid mechanical alteration. Therefore, we compressed ground trabecular human bone to granules and, afterwards, treated them with 250 and 300 MPa for 20 and 30 min respectively. We characterized the formed bone granule cylinders (BGC) with respect to their biomechanical properties by evaluating stiffness and stress at 15% strain. Furthermore, the stiffness and yield strength of HHP-treated and native human trabecular bone cylinders (TBC) as control were evaluated. The mechanical properties of native vs. HHP-treated TBCs as well as HHP-treated vs. untreated BGCs did not differ, independent of the applied HHP magnitude and duration. Our study suggests HHP treatment as a suitable alternative to current processing techniques for allogenic bone substitutes since no negative effects on mechanical properties occurred.

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“…The formation of inter-and intra-molecular interactions of the sulphydryl group is suggested to be the main cause for the pressure-induced irreversible denaturation of b-lactoglobulin [15]. Compared to b-lactoglobulin, a-lactalbumin is stable to pressures up to about 400-500 MPa in milk at 20°C [12,18].…”

Section: Introductionmentioning

confidence: 99%

Effect of high-pressure treatment on denaturation of bovine β-lactoglobulin and α-lactalbumin

Mazri

Sánchez

Ramos

et al. 2012

Eur Food Res Technol

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The effect of high-pressure treatment on denaturation of b-lactoglobulin and a-lactalbumin in skimmed milk, whey, and phosphate buffer was studied over a pressure range of 450-700 MPa at 20°C. The degree of protein denaturation was measured by the loss of reactivity with their specific antibodies using radial immunodiffusion. The denaturation of b-lactoglobulin increased with the increase of pressure and holding time. Denaturation rate constants of b-lactoglobulin were higher when the protein was treated in skimmed milk than in whey, and in both media higher than in buffer, indicating that the stability of the protein depends on the treatment media. a-Lactalbumin is much more baroresistant than b-lactoglobulin as a low level of denaturation was obtained at all treatments assayed. Denaturation of b-lactoglobulin in the three media was found to follow a reaction order of n = 1.5. A linear relationship was obtained between the logarithm of the rate constants and pressure over the pressure range studied. Activation volumes obtained for the protein treated in milk, whey, and buffer were -17.7 ± 0.5, -24.8 ± 0.4, and -18.9 ± 0.8 mL/mol, respectively, which indicate that under pressure, reactions of volume decrease of b-lactoglobulin are favoured. Kinetic parameters obtained in this work allow calculating the pressure-induced denaturation of b-lactoglobulin on the basis of pressure and holding times applied.

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Effects of high hydrostatic pressure on the structure of bovine α-lactalbumin

Cited by 36 publications

References 41 publications

α-Lactalbumin, Amazing Calcium-Binding Protein

α-Lactalbumin, Amazing Calcium-Binding Protein

Mechanical Characterization of Human Trabecular and Formed Granulate Bone Cylinders Processed by High Hydrostatic Pressure

Effect of high-pressure treatment on denaturation of bovine β-lactoglobulin and α-lactalbumin

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