Water filtration using nonwoven cartridge filter system

A cartridge based fibrous filtration system has been designed and investigated. For the fibrous medium, needle-punch nonwoven structure has been selected and different nonwoven samples are analysed for the water purification. A series of different needle-punched nonwovens made of polypropylene have been produced by changing mass per unit area, needling density and fibre linear density. A chemical oxygen demand test has been employed to obtain the filtration efficiency (FE). The FE obtained for these samples ranges from 8.84% to 78.04% in purifying the reference water (mud water). It has been found that the FE increases with increase in mass per unit area and needling density (p < 0.01). Also, the filter media made of finer fibres displays higher FE than coarser fibre (p < 0.01). On examining the filter performance in multiple filtration cycles, it is found that the FE increases initially and finally reaches to a saturation value. A good correlation (r2 > 0.95) has been found for the FE of each cycle with the air permeability, thickness and weight density of the loaded filter. The FE of the bare nonwoven (maximum FE) further improves (95%) by incorporating activated particles

Water filtration using nonwoven cartridge filter system

72-79A cartridge based fibrous filtration system has been designed and investigated. For the fibrous medium, needle-punch nonwoven structure has been selected and different nonwoven samples are analysed for the water purification. A series of different needle-punched nonwovens made of polypropylene have been produced by changing mass per unit area, needling density and fibre linear density. A chemical oxygen demand test has been employed to obtain the filtration efficiency (FE). The FE obtained for these samples ranges from 8.84% to 78.04% in purifying the reference water (mud water). It has been found that the FE increases with increase in mass per unit area and needling density (p r2 > 0.95) has been found for the FE of each cycle with the air permeability, thickness and weight density of the loaded filter. The FE of the bare nonwoven (maximum FE) further improves (95%) by incorporating activated particles

Hyperexpression and purification of biologically active human luteinizing hormone and human chorionic gonadotropin using the methylotropic yeast, Pichia pastoris

The glycoprotein hormones, luteinizing hormone (LH), human chorionic gonadotropin (hCG), thyroid stimulating hormone (TSH), and follicle stimulating hormone (FSH), play important roles in overall physiology and reproduction. These hormones are heterodimeric molecules consisting of an identical a subunit non-covalently associated with the hormone-specific β subunit. The inherent structural intricacies possessed by these hormones make them very interesting model systems for structure-function relationship studies of complex dimeric glycoproteins. The structural studies, as well as, the therapeutic applications require large quantities of biologically active hormones free of any contaminants. In this study, we report hyperexpression and purification of biologically active recombinant hLH and hCG expressed using Pichia pastoris expression system. A combination of hydrophobic interaction chromatography and ion exchange chromatography has been used to purify these recombinant hormones to homogeneity. Using a number of biochemical and immunological criteria, the recombinant hormones have been shown to be similar to the natural hormones and were equally biologically active. The preliminary data also suggested that P. pastoris cells express a low molecular weight isoform of hCG that appeared to be less glycosylated. This isoform exhibited lesser affinity for the receptor as compared to hCG, but was found to be fully biologically active

Hyperexpression and purification of biologically active human luteinizing hormone and human chorionic gonadotropin using the methylotropic yeast, Pichia pastoris

The glycoprotein hormones, luteinizing hormone (LH), human chorionic gonadotropin (hCG), thyroid stimulating hormone (TSH), and follicle stimulating hormone (FSH), play important roles in overall physiology and reproduction. These hormones are heterodimeric molecules consisting of an identical \alpha subunit non-covalently associated with the hormone-specific \beta subunit. The inherent structural intricacies possessed by these hormones make them very interesting model systems for structure–function relationship studies of complex dimeric glycoproteins. The structural studies, as well as, the therapeutic applications require large quantities of biologically active hormones free of any contaminants. In this study, we report hyperexpression and purification of biologically active recombinant hLH and hCG expressed using Pichia pastoris expression system. A combination of hydrophobic interaction chromatography and ion exchange chromatography has been used to purify these recombinant hormones to homogeneity. Using a number of biochemical and immunological criteria, the recombinant hormones have been shown to be similar to the natural hormones and were equally biologically active. The preliminary data also suggested that P. pastoris cells express a low molecular weight isoform of hCG that appeared to be less glycosylated. This isoform exhibited lesser affinity for the receptor as compared to hCG, but was found to be fully biologically active