2021
DOI: 10.21926/rpm.2102027
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Use of α-Lactalbumin [α-La] from Whey as a Vehicle for Bioactive Compounds in Food Technology and Pharmaceutics: A Review

Abstract: Whey protein is a byproduct of cheese, casein, and Greek yogurt produced in Europe, North America, and Australasia. It is a substantial source of functional proteins and peptides for the worldwide food industry. α-Lactalbumin (α-La) is a globular protein that can be isolated from WPI (whey protein isolates) using techniques such as chromatography/gel filtration, membrane separation, etc. α-La is used in the elaboration of functional foods and is a very good source of peptides with anticancer, antimicrobial, an… Show more

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Cited by 2 publications
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“…In DLS, because of the aggregation of proteins in an aqueous solution, the protein molecules seek lower thermodynamic energy, which can happen with the interactions among the sulfidic groups (Kolakowski et al, 2001;Madalena et al, 2016). When drying the colloidal dispersion for use in TEM, it is possible that the protein has undergone changes in confor-mation and sought a more favorable state with molecular interactions of hydrophilic potions that were previously interacting with the solvent, so it was compacted, exposing the hydrophobic regions, suggesting a crystallization process, which is reaffirmed by the TEM images (Figure 3) showing a nonglobular structure, more commonly viewed when this molecule is not pure, as reviewed by Cuevas-Gómez et al (2021) and shown by Nigen et al (2009), who combined α-la with lysozyme and obtained spherical nano proteins, observing the influence of the medium's electrostatic force on the behavior of the bottom-up nanostructuring, and Arroyo-Maya et al ( 2012) using ketone as solvent.…”
Section: Characterization Of α-La Nanostructured Aggregates Via Trans...mentioning
confidence: 77%
“…In DLS, because of the aggregation of proteins in an aqueous solution, the protein molecules seek lower thermodynamic energy, which can happen with the interactions among the sulfidic groups (Kolakowski et al, 2001;Madalena et al, 2016). When drying the colloidal dispersion for use in TEM, it is possible that the protein has undergone changes in confor-mation and sought a more favorable state with molecular interactions of hydrophilic potions that were previously interacting with the solvent, so it was compacted, exposing the hydrophobic regions, suggesting a crystallization process, which is reaffirmed by the TEM images (Figure 3) showing a nonglobular structure, more commonly viewed when this molecule is not pure, as reviewed by Cuevas-Gómez et al (2021) and shown by Nigen et al (2009), who combined α-la with lysozyme and obtained spherical nano proteins, observing the influence of the medium's electrostatic force on the behavior of the bottom-up nanostructuring, and Arroyo-Maya et al ( 2012) using ketone as solvent.…”
Section: Characterization Of α-La Nanostructured Aggregates Via Trans...mentioning
confidence: 77%