Preparation of Biocompatible Liquid Marbles Stabilized by Food-Grade Stearate Microparticle for Aerobic Bacteria Cultivation.

Liquid marble (LM), a non-stick drop coated with micro- or nano-scale particles, has great potential in a wide range of applications. LMs have an advantageous feature in which gas or vapor can freely transport through their particle shell; therefore, it makes them an ideal candidate to be utilized as microbioreactor containing aerobic microorganisms. In this study, safer and more biocompatible LMs were successfully prepared using a food-grade calcium stearate microparticle as a stabilizer.

Heparin-dependent aggregation of hen egg white lysozyme reveals two distinct mechanisms of amyloid fibrillation.

Heparin, a biopolymer possessing high negative charge density, is known to accelerate amyloid fibrillation by various proteins. Using hen egg white lysozyme, we studied the effects of heparin on protein aggregation at low pH, raised temperature, and applied ultrasonic irradiation, conditions under which amyloid fibrillation was promoted. Heparin exhibited complex bimodal concentration-dependent effects, either accelerating or inhibiting fibrillation at pH 2.

Higher order structure of Mucor miehei lipase and micelle size in cetyltrimethylammonium bromide reverse micellar system.

The higher order structure of Mucor miehei lipase and micelle size in a cationic cetyltrimethylammonium bromide (CTAB) reverse micellar system was investigated. Circular dichroic (CD) measurement revealed that the lipase far-UV CD spectra changed markedly, going from buffer solution to the reverse micellar solution, and were very similar for any organic solvent used. The ellipticity of the solubilized lipase in the far-UV region markedly decreased with increasing water content (W(0): molar ratio of water to CTAB), indicating that the secondary structure of lipase changed with the water content.

Liquid-liquid extraction of alpha-lactalbumin using reverse micellar organic solvent.

The liquid-liquid extraction of alpha-lactalbumin based on reverse micellar organic solvents was investigated. Forward extraction of the protein in the reverse micellar organic phase from aqueous feed solutions was strongly dependent on the initial pH of the feed solution and the complete forward extraction of 0.03 mM alpha-lactalbumin was successfully achieved at pH 6.

Higher order structure of proteins solubilized in AOT reverse micelles.

The higher order structure of proteins solubilized in an bis(2-ethylhexyl) sulfosuccinate sodium (AOT) reverse micellar system was investigated. From circular dichroic (CD) measurement, CD spectra of cytochrome c, which is solubilized at the interface of reverse micelles, markedly changed on going from buffer solution to the reverse micellar solution, and the ellipticity values in the far- and near-UV regions decreased with decreasing the water content (W0: molar ratio of water to AOT), indicating that the secondary and tertiary structures of cytochrome c changed with the water content. The ellipticity of ribonuclease A, which is solubilized in the center of micellar water pool, in the near-UV region was dependent on W0 and became minimum when W0 of ca.