| solid state production of a mucor bacilliformis acid protease. | acid protease production by a local strain of mucor bacilliformis was performed by solid state cultivation on different agricultural by-products as substrate. the effects of different parameters on enzyme biosynthesis were studied: wheat bran wetted at 120% with a 200 mm hcl solution and inoculated with 5 x 10(5) spores/g produced a milk clotting activity of 7500 u/g bran after 72 h cultivation at 24 degrees c. | 2017 | 9160434 |
| isolation and biochemical analysis of mucor bacilliformis monomorphic mutants. | fourteen stable mutants of mucor bacilliformis which grew yeastlike under both aerobic and anaerobic conditions were isolated after treatment of growing mycelium with n-methyl-n'-nitro-n-nitrosoguanidine. biochemical characterization of the mutants included determination of growth in different carbon and nitrogen sources, determination of sensitivity of respiration to cyanide and salicylhydroxamate, analysis of cytochrome spectra, determination of glutamate dehydrogenases, glutamine synthase, an ... | 1983 | 6137477 |
| structural aspects of the mucor bacilliformis proteinase, a new member of the aspartyl-proteinase family. | bovine chymosin is considered the best milk-clotting enzyme for cheese manufacture; however, the thermophilic mucor pusillus proteinase is also used nowadays. we herein report structural aspects of the aspartyl proteinase from the local mesophilic mucor bacilliformis strain. sequence data indicate a high similarity degree to those of other family members. the protein is monomeric, not glycosylated, has two disulfide bridges, and mainly includes beta structure. a molecular model was built by usin ... | 2006 | 16524637 |
| further characterization and kinetic parameter determination of a milk-clotting protease from mucor bacilliformis. | further characterization of an aspartyl protease from mucor bacilliformis with milk-clotting activity was performed. an extinction coefficient, epsilon 278 cm = 1.61 ml/mg/cm, a molecular mass of 35,400 da and a pi of 5.2 were determined. proteolytic activity and kinetic parameters were evaluated by using the hexapeptide leu-ser-pno2-phe-nle-ala-leu-ome as the substrate. the effect of ph and temperature on peptide cleavage, as well as protease heat stability, was determined. such properties, tak ... | 1997 | 9429300 |
| phenoloxidase production and vanillic acid metabolism by zygomycetes. | the ability of 23 strains of zygomycetes to produce extracellular phenoloxidases was examined on solid media by using 10 different reagents. the results varied depending on the reagent and indicated that most of the strains were devoid of phenoloxidase activity. the production of inducible phenoloxidases was demonstrated by the bavendamm reaction. the study of the biotransformation of vanillic acid in synthetic medium indicated that the reaction most often obtained was the reduction of vanillic ... | 1992 | 1602986 |
| tetramethyl-p-phenylenediamine oxidase reaction in azotobacter vinelandii. | it was possible to quantitate the tetramethyl-p-phenylenediamine (tmpd) oxidase reaction in azotobacter vinelandii strain o using turbidimetrically standarized resting cell suspensions. the q(o2) value obtained for whole cell oxidation of ascorbate-tmpd appeared to reflect the full measure of the high respiratory oxidative capability usually exhibited by this genera of organisms. the q(o2) value for the tmpd oxidase reaction ranged from 1,700 to 2,000 and this value was equivalent to that obtain ... | 1975 | 174491 |
| [production of a concentrate of mucor bacilliformis acid protease]. | a concentrate of milk-clotting enzyme was produced by culture of mucor bacilliformis on wheat bran medium moistened to 120% water on dry bases with hc1 2 n solution. the wheat bran was autoclaved, spread on trays and inoculated with 5.10(6) spore/gr of dry bran. after 10 days of culture at 21 degrees c, the enzyme produced was extracted with water and adjusted to ph 4.4. the precipitation was performed with ethanol. the precipitate was dissolved in hcl solution (ph 4.5) and it was concentrated b ... | 1982 | 6765621 |
| purification and characterization of a milk clotting protease from mucor bacilliformis. | an acid protease having milk clotting activity has been isolated from mucor bacilliformis cultures. the enzyme was basically purified by ionic exchange chromatography. an average yield of 29 mg purified product was obtained from 100 ml crude extract. as purity criteria, sds-page, reverse-phase hplc, and n-terminal analysis were performed. the protease is a protein composed of a single polypeptide chain with glycine at the n-terminus. the mol wt is approx 32,000, and its amino acid composition is ... | 1992 | 1303065 |