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- W2912072271 abstract "Non-lamellar lipid aqueous phases, such as reverse cubic or hexagonal phases, can be used to entrap smaller biomolecules. The curvature of these lipid phases and hence the size of the aqueous cavities depends on the composition, water content and temperature. The challenge is to encapsulate proteins, such as large enzymes due to the limited size of these cavities. Here, we will present a lipid system, based on mixtures of acylglycerides and acyldiglycerides, which are able to form highly swollen sponge phases (L3), with aqueous pores up to 13 nm of diameter. The structure and composition of the particles were revealed by using small angle neutron scattering (SANS), light scattering, cryo-TEM, size exclusion chromatography and Raman spectroscopy. The Raman spectroscopy results for the sponge phases are compared with data for lamellar and reverse bicontinuous cubic phase in the same lipid system and show large similarities in lipid chain confirmation and head group interactions as all three structures are formed by lipid bilayers, albeit of different curvature. The L3 structure is preserved even in excess aqueous solution, where they form sponge-like nanoparticles (L3 NPs). We investigate encapsulation of two key types of enzymes of different sizes, used in food processing, namely Aspartic protease (34 KDa) and Beta-galactosidase (460 KDa). They are today delivered into the process as solutions with a considerable amount of preservatives and still with limited shelf-life and limited control of the enzyme activity. The SANS results reveal differences in the L3 NPs with and without enzyme that can be interpreted as inclusion of the protein in the liquid crystalline phase. These findings are verified by size exclusion chromatography and the enzymatic activity of the encapsulated enzyme, which surpasses the enzymes stability in solution." @default.
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- W2912072271 date "2019-02-01" @default.
- W2912072271 modified "2023-09-26" @default.
- W2912072271 title "Lipid Sponge-Phase Nanoparticles as Enzyme Carriers - Structure and Intermolecular Interaction Controlling the Enzyme Inclusion" @default.
- W2912072271 doi "https://doi.org/10.1016/j.bpj.2018.11.1004" @default.
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