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- Alander, J, et al.
(author)
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Model microemulsions containing vegetable oils Part 1: Nonionic surfactant systems
- 1989
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In: Journal of the American Oil Chemists Society. - 0003-021X .- 1558-9331. ; 66, s. 1656-1660
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Journal article (peer-reviewed)abstract
- Nonionic microemulsions containing triglucerides and fatty acid esters as lipophilic components have been studied. The phase inversion temperature (PIT) of the systems was determined by a conductometric method. Partial phase diagrams were constructed in the phase inversion temperature range. Water solubilization capacity of the nonionic surfactant systems studied was dependent on surfactant and oil types in analogy to ordinary hydrocarbon systems. The PIT:s increased with increased molecular weight for both esters and triglycerides.
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- Alander, J, et al.
(author)
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Model microemulsions containing vegetable oils Part 2: Ionic surfactant systems
- 1989
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In: Journal of the American Oil Chemists Society. - 0003-021X .- 1558-9331. ; 66, s. 1661-1665
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Journal article (peer-reviewed)abstract
- The phase behavior and the structure of ionic microemulsions, stabilized by sodium oleate and different alcohol cosurfactants, containing fatty acid esters or triglycerides as lipophilic components, have been investigated. Microemulsions containing triglycerides display a smaller stability region than microemulsions containing hydrocarbons or fatty acid esters. From structural investigations, using the NMR FT pulsed gradient spin echo method for measuring self-diffusion coefficients, differences in the microstructure are revealed as well. Adding an ester (or a hydrocarbon) to a microemulsion containing sodium oleate/pentanol will at certain compositions lead to a gradual transition from a bicontinuous to an oilcontinuous system, while this behavior cannot be detected when adding a triglyceride. Instead, a phase-separation occurs, and it is suggested that the larger molecular size of the triglyceride is responsible for the diffirence.
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- Bergenståhl, BA, et al.
(author)
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Lipids and colloidal stability
- 1997
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In: Current Opinion in Colloid & Interface Science. - 1359-0294 .- 1879-0399. ; 2, s. 590-595
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Journal article (peer-reviewed)abstract
- Polar lipids have an important role as emulsifiers and stability controlling agents in the food industry. The principal effects of the emulsifiers have been found to depend on the situation in which they are applied. They may act as stabilising additives, creating repulsive interactions between droplets. They may act as emulsifying agents, or they may destabilise emulsions by reducing protein adsorption at the oil/water interface. They may also destabilise emulsions by increasing wettability of fat crystals. Furthermore, they may form micellar or liposomal aggregates in the dispersion, influencing interactions and aggregation.
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- Busenlehner, Laura S., et al.
(author)
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Location of substrate binding sites within the integral membrane protein microsomal glutathione transferase-1
- 2007
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In: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 46:10, s. 2812-2822
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Journal article (peer-reviewed)abstract
- Microsomal glutathione transferase-1 (MGST1) is a trimeric, membrane-bound enzyme with both glutathione (GSH) transferase and hydroperoxidase activities. As a member of the MAPEG superfamily, MGST1 aids in the detoxication of numerous xenobiotic substrates and in cellular protection from oxidative stress through the GSH-dependent reduction of phospholipid hydroperoxides. However, little is known about the location of the different substrate binding sites, including whether the transferase and peroxidase activities overlap structurally. Although molecular density attributed to GSH has been observed in the 3.2 A resolution electron crystallographic structure of MGST1, the electrophilic and phospholipid hydroperoxide substrate binding sites remain elusive. Amide H-D exchange kinetics and H-D ligand footprinting experiments indicate that GSH and hydrophobic substrates bind within similar, but distinct, regions of MGST1. Site-directed mutagenesis, guided by the H-D exchange results, demonstrates that specific residues within the GSH footprint effect transferase activity toward 1-chloro-2,4-dinitrobenzene. In addition, cytosolic residues surrounding the chemical stress sensor C49 but not modeled in the crystal structure appear to play an important role in the formation of the binding site for hydrophobic substrates. Although the fatty acid/phospholipid binding site structurally overlaps that for GSH, it does not appear to be localized to the same region as other hydrophobic substrates. Finally, H-D exchange mass spectrometry reveals a specific conformational transition that may mediate substrate binding and/or product release. Such structural changes in MGST1 are essential for activation of the enzyme and are important for its biological function.
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- Staab, CA, et al.
(author)
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The Janus face of alcohol dehydrogenase 3
- 2009
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In: Chemico-biological interactions. - : Elsevier BV. - 1872-7786 .- 0009-2797. ; 178:1-3, s. 29-35
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Journal article (peer-reviewed)
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