Abstract: A solar powered vapor compression refrigeration system is made practicable with thermal storage and novel control techniques. In one embodiment, the refrigeration system includes a photovoltaic panel, a variable speed compressor, an insulated enclosure, and a thermal reservoir. The photovoltaic (PV) panel converts sunlight into DC (direct current) electrical power. The DC electrical power drives a compressor that circulates refrigerant through a vapor compression refrigeration loop to extract heat from the insulated enclosure. The thermal reservoir is situated inside the insulated enclosure and includes a phase change material. As heat is extracted from the insulated enclosure, the phase change material is frozen, and thereafter is able to act as a heat sink to maintain the temperature of the insulated enclosure in the absence of sunlight. The conversion of solar power into stored thermal energy is optimized by a compressor control method that effectively maximizes the compressor's usage of available energy.

Abstract: A solar powered vapor compression refrigeration system is made practicable with thermal storage and novel control techniques. In one embodiment, the refrigeration system includes a photovoltaic panel, a variable speed compressor, an insulated enclosure, and a thermal reservoir. The photovoltaic (PV) panel converts sunlight into DC (direct current) electrical power. The DC electrical power drives a compressor that circulates refrigerant through a vapor compression refrigeration loop to extract heat from the insulated enclosure. The thermal reservoir is situated inside the insulated enclosure and includes a phase change material. As heat is extracted from the insulated enclosure, the phase change material is frozen, and thereafter is able to act as a heat sink to maintain the temperature of the insulated enclosure in the absence of sunlight. The conversion of solar power into stored thermal energy is optimized by a compressor control method that effectively maximizes the compressor's usage of available energy.

Abstract: Microcapsules prepared by encapsulating an aqueous solution of a protein, drug or other bioactive substance inside a semi-permeable membrane by are disclosed. The microcapsules are formed by interfacial coacervation under conditions where the shear forces are limited to 0-100 dynes/cm2 at the interface. By placing the microcapsules in a high osmotic dewatering solution, the protein solution is gradually made saturated and then supersaturated, and the controlled nucleation and crystallization of the protein is achieved. The crystal-filled microcapsules prepared by this method can be conveniently harvested and stored while keeping the encapsulated crystals in essentially pristine condition due to the rugged, protective membrane. Because the membrane components themselves are x-ray transparent, large crystal-containing microcapsules can be individually selected, mounted in x-ray capillary tubes and subjected to high energy x-ray diffraction studies to determine the 3-D structure of the protein molecules.

Abstract: Microcapsules prepared by encapsulating an aqueous solution of a protein, drug or other bioactive substance inside a semi-permeable membrane by are disclosed. The microcapsules are formed by interfacial coacervation under conditions where the shear forces are limited to 0-100 dynes/cm2 at the interface. By placing the microcapsules in a high osmotic dewatering solution, the protein solution is gradually made saturated and then supersaturated, and the controlled nucleation and crystallization of the protein is achieved. The crystal-filled microcapsules prepared by this method can be conveniently harvested and stored while keeping the encapsulated crystals in essentially pristine condition due to the rugged, protective membrane. Because the membrane components themselves are x-ray transparent, large crystal-containing microcapsules can be individually selected, mounted in x-ray capillary tubes and subjected to high energy x-ray diffraction studies to determine the 3-D structure of the protein molecules.