No abstract

Production of extracellular alkaline protease by a locally isolated fungal species, Rhizopus oryzae, under solid state fermentation was optimized. The maximum enzyme activity under the optimum conditions of temperature (32°C), relative humidity (90%±95%), spore count ($2´10 5 /g wheat bran), moisture content of solid substrate (140%) adjusted suitably with salt solution (M-9) of pH 5.5 was 341 unit/g wheat bran.

No abstract

A locally isolated ®lamentous fungus belonging to the group phycomycetes namely Rhizopus oryzae was identi®ed to secrete alkaline protease. The production of this enzyme through solid state fermentation process has been attempted. From fermented biomass extraction of the enzyme was found to depend on the different parameters like nature of solvent, time of soaking, temperature etc. While optimizing the extraction process, it was found that 10% ethanol with 3% glycerol was the best solvent for protease extraction, when the soaking time was 2 hours and temperature 30°C. It was further observed that double wash of fermented biomass yielded almost total enzyme in the leachate.

Unlike currently licensed therapies to manage osteoporosis, parathyroid hormone (PTH) and its analogs represent a new class of anabolic agents, which act primarily to inhibit bone resorption and remodeling. The hormone's recombinant form is a bioactive peptide, 1-34 residues, which is inherently very unstable. Prior understanding of the molecular degradation pathway will help in development of a process that will yield a better product with respect to its quality and stability. The current work focuses on detailed characterization of the product-related impurities generated during storage of recombinant human PTH. The study depicted the various routes through which the molecule can degrade during its shelf life. Through a combination of forced degradation and accelerated study, it was established that the impurities were generated owing to oxidation, deamidation, and peptide bond cleavage of/at various amino acid residues. Until this study, it was presumed that oxidation is the primary route of degradation in PTH and most of the published reports were on native (1-84) forms of the hormone. The present research confirms that the recombinant hormone (1-34) degraded not only because of oxidation but that deamidation and peptide bond cleavage are also prominent modes of degradation. Therefore, owing to the unstable nature of the molecule it is suggested that stringent conditions should be maintained during manufacturing to obtain a stable molecule with fewer impurities.