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Application of Nanotechnology in the Safe Delivery of Bioactive Compounds
Published in V Ravishankar Rai, Jamuna A. Bai, Nanotechnology Applications in the Food Industry, 2018
Behrouz Ghorani, Sara Naji-Tabasi, Aram Bostan, Bahareh Emadzadeh
Milk proteins are natural vehicles for bioactives. They are widely used in the food industry for their nutritional and functional properties. Casein, the major milk protein, is inexpensive, readily available, nontoxic, and highly stable. As a natural food product, this GRAS protein is biocompatible and biodegradable. Studies based on ingestion by patients allergic to milk found that 62% of the patients reacted to β-lactoglobulin (β-lg), 60% to casein, and 53% to α-lactalbumin. The allergic response of β-lg, which was the highest, was due to its relative resistance to acid digestion. Caseins, in particular, have evolved to be easily digestible (Elzoghby, Abo El-Fotoh, and Elgindy 2011).
Ultrafiltration
Published in Michael J. Matteson, Clyde Orr, Filtration, 2017
Ultrafiltration is now regarded as a standard processing technology of the dairy industry [45–47]. Since its acceptance around 1970, two main industrial-scale applications have been recovery and concentration of cheese whey proteins (mainly α-lactalbumin and β-lactoglobulin) and concentration of milk in the production of soft cheeses (Brie, Camambert, feta, cottage cheese).
Interactions of α -Lactalbumin and Cytochrome c with Langmuir Monolayers of Glycerophospholipids
Published in Journal of Dispersion Science and Technology, 2011
Wilhelm R. Glomm, Sondre Volden, Marit-Helen Glomm Ese, Øyvind Halskau
Bovine α-lactalbumin (α-La) is a 14.2 kDa globular calcium-binding milk protein which is a component of the lactose synthase complex. α-La binds to galactosyltransferase, promoting glucose binding and facilitating the synthesis of lactose in lactating mammary glands.[18] Previous in vitro studies have shown that α-La adopts a molten globular-like conformation when it interacts with membranes.[1-5] Cytochrome c (Cyt c) shuttles electrons between the two membrane-associated protein complexes cytochrome c reductase and cytochrome c oxidase on the inside of the inner mitochondrial membrane, and is a part of the mitochondrial production of ATP. It has been established using fluorescence measurements of monolayers[19] and solid-state 31P NMR[20] that Cyt c binds specifically to anionic phospholipids. Moreover, Cyt c has been demonstrated to form stable molten globules both at electrodes set up to mimic the in vivo redox reaction,[21] in association with anionic membranes, and in bulk solution.[12,22-25] Thus, the two proteins are both globular and mostly helical, amphitropic proteins of similar size and share the trait of being able to partially unfold as they interact with membranes and surfaces. Their charge properties are different, however, with α-La being an acidic while Cyt c being a basic protein. Herein, we address whether proteins and their trapped folding states can intercalate into already formed phospholipid monolayers, as well as the importance of global protein charge for interaction.