| microbial transformation of sampangine. | microbial transformation studies of the antifungal alkaloid sampangine (2) have revealed that it is metabolized by a number of microorganisms. using a standard two-stage fermentation technique, beauvaria bassiana (atcc 7159), doratomyces microsporus (atcc 16225), and filobasidiella neoformans (atcc 10226) produced the 4'-o-methyl-beta-glucopyranose conjugate (3), while absidia glauca (atcc 22752), cunninghamella elegans (atcc 9245), cunninghamella species (nrrl 5695), and rhizopus arrhizus (atcc ... | 1999 | 10425122 |
| a first order experimental design to assess soluble proteins released by a new keratinase from doratomyces microsporus on human substrates. | the influence of temperature, ph, keratinase concentration, substrate concentration and incubation time on the soluble proteins released by a new keratinase from doratomyces microsporus was studied with an experimental design assisted by a simplex method. only 16 spectrophotometric analyses were required. this study was carried out by measuring, according to smith's method, the concentration of soluble proteins released by the enzyme on two human substrates: stratum corneum and nails. results gi ... | 1999 | 10564836 |
| keratinase of doratomyces microsporus. | the fungus doratomyces microsporus produced an extracellular keratinase during submerged aerobic cultivation in a medium containing a protein inducer for enzyme synthesis. the keratinase was purified to homogeneity using hydrophobic interaction chromatography followed by gel chromatography. the molecular weight was estimated to be 33 kda (from sds-page analysis) or 30 kda (by gel chromatography), suggesting a monomeric structure. the isoelectric point of the enzyme was determined to be around 9. ... | 2000 | 10709982 |
| comparison of two hard keratinous substrates submitted to the action of a keratinase using an experimental design. | the influence of temperature, ph, keratinase concentration, substrate concentration and incubation time on the soluble proteins released by a new keratinase from doratomyces microsporus was studied with a second-order experimental design. only 15 or 18 spectrophotometric analyses were required to determine the optimal experimental conditions for this keratinase on nail and hoof. this study was carried out by measuring, according to smith's method, the concentration of soluble proteins released b ... | 2001 | 11472820 |
| similarities and specificities of fungal keratinolytic proteases: comparison of keratinases of paecilomyces marquandii and doratomyces microsporus to some known proteases. | based on previous screening for keratinolytic nonpathogenic fungi, paecilomyces marquandii and doratomyces microsporus were selected for production of potent keratinases. the enzymes were purified and their main biochemical characteristics were determined (molecular masses, optimal temperature and ph for keratinolytic activity, n-terminal amino acid sequences). studies of substrate specificity revealed that skin constituents, such as the stratum corneum, and appendages such as nail but not hair, ... | 2005 | 16000744 |