Publications
| Title | Abstract | Year Filter | PMID(sorted descending) Filter |
|---|
| asperfuran, a novel antifungal metabolite from aspergillus oryzae. | asperfuran is a novel antifungal dihydrobenzofuran derivative produced by a strain of aspergillus oryzae. asperfuran weakly inhibited chitin synthase from coprinus cinereus. this inhibition could be abolished by the addition of egg lecithin. in the agar diffusion assay asperfuran induced morphological changes in mucor miehei at very low concentrations (20 ng/disc) while growth was only partly inhibited. in hela s3 and l1210 cells it showed weak cytotoxicity, the ic50 was 25 micrograms/ml. | 1990 | 2143181 |
| a model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. | lipases are hydrolytic enzymes which break down triacylglycerides into free fatty acids and glycerols. they have been classified as serine hydrolases owing to their inhibition by diethyl p-nitrophenyl phosphate. lipase activity is greatly increased at the lipid-water interface, a phenomenon known as interfacial activation. x-ray analysis has revealed the atomic structures of two triacylglycerol lipases, unrelated in sequence: the human pancreatic lipase (hpl)4, and an enzyme isolated from the fu ... | 1991 | 2046751 |
| a kinetic and equilibrium study of the denaturation of aspartic proteinases from the fungi, endothia parasitica and mucor miehei. | kinetic and equilibrium analyses of the denaturation of endothia parasitica and mucor miehei aspartic proteinases were performed using enzyme activity and ultraviolet absorption as indices of denaturation. denaturation of these proteinases was shown to be irreversible, suggesting that the conformations of these aspartic proteinases may be predetermined in their zymogens. thermal and guanidine hydrochloride denaturation of these proteinases produced first-order, two-state, kinetic behaviour. equi ... | 1991 | 2001389 |
| cloning and structure of the mono- and diacylglycerol lipase-encoding gene from penicillium camembertii u-150. | a gene (mdla) encoding mono- and diacylglycerol lipase (mdgl) from penicillium camembertii u-150 has been cloned using a 0.9-kb dna fragment, generated by mixed oligodeoxyribonucleotide (oligo)-primed polymerase chain reaction (pcr), as a probe. comparison of the nucleotide sequence of the gene and its cdna clone, obtained by pcr, revealed the presence of two short introns (56 and 53 bp). two transcription start points (tsp) were localized by primer extension analysis at 37 and 30 bp upstream fr ... | 1991 | 1879699 |
| relationships among serine hydrolases: evidence for a common structural motif in triacylglyceride lipases and esterases. | a detailed analysis of the highly refined (1.9 a resolution) molecular model of the fungal (rhizomucor miehei) triglyceride lipase reveals a unique conformation of the oligopeptide containing the active serine (ser 144) residue. it consists of a six-residue beta-strand (strand 4 of the central sheet), a four-residue turn of type ii' with serine in the epsilon conformation, and a buried alpha-helix packed in a parallel way against strands 4 and 5 of the central beta-pleated sheet. it is shown tha ... | 1991 | 1818588 |
| cloning, expression and characterization of a cdna encoding a lipase from rhizopus delemar. | a lambda gt11 cdna library was constructed in escherichia coli using poly(a)-selected mrna from the fungus, rhizopus (rp.) delemar. lipase-producing members of the library were identified by means of a phenotypic score wherein the release of fatty acids by lipase causes a characteristic color change in the growth medium. one such isolate contained a 1287-bp insert (lip cdna) which hybridizes to 1.25- to 1.35-kb mrna species from rp. delemar. the lipase produced in e. coli containing the lip cdna ... | 1991 | 1756969 |
| catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase. | the crystal structure of an extracellular triglyceride lipase (from a fungus rhizomucor miehei) inhibited irreversibly by diethyl p-nitrophenyl phosphate (e600) was solved by x-ray crystallographic methods and refined to a resolution of 2.65 a. the crystals are isomorphous with those of n-hexylphosphonate ethyl ester/lipase complex [brzozowski, a. m., derewenda, u., derewenda, z. s., dodson, g. g., lawson, d. m., turkenburg, j. p., bjorkling, f., huge-jensen, b., patkar, s. a., & thim, l. (1991) ... | 1992 | 1737010 |
| lipases from different sources vary widely in dependence of catalytic activity on water activity. | we have measured the rates of esterification in hexane catalysed by suspended immobilised lipases (triacylglycerol acylhydrolase, ec 3.1.1.3), with pre-equilibration to known thermodynamic water activity (a(w)). there were important differences between the enzymes from five different microbes in their retention of activity at low a(w). that from rhizomucor miehei showed over 40% maximal activity at an a(w) of 0.12, and that from rhizopus niveus was also fairly active at low a(w). lipases from ot ... | 1992 | 1643087 |
| rhizomucor miehei lipase remains highly active at water activity below 0.0001. | the lipase from rhizomucor miehei adsorbed on polymer beads retains substantial catalytic activity even after exhaustive drying, and the use of dry box procedures to prevent entry of atmospheric water. rates of esterification and transesterification (alcoholysis) were measured while stirred in hexane pre-dried to similar low water activity (aw). the rate of dodecyl decanoate synthesis was over 30% of that at the optimum (aw 0.55) after drying with anhydrous cuso4 (aw less than 10(-3)) or mgo (aw ... | 1992 | 1577162 |
| stereoselectivity of lipases: esterification reactions of octadecylglycerol. | stereoselectivity of several triacylglycerol lipases (ec 3.1.1.3) has been investigated in the enzymatic esterification of rac-1-o-octadecylglycerol with oleic acid in the presence of organic solvents, such as hexane. x-1(3)-o-octadecylmonooleoylglycerols were the only products formed with most lipases; considerable proportions of x-1(3)-o-octadecyldioleoylglycerols were also formed with the lipase from candida cylindracea. the mixtures of unesterified enantiomeric substrates, i.e., x-1(3)-o-oct ... | 1992 | 1511492 |
| proteolytic activity of proteinases on macropeptide isolated from kappa-casein. | proteolytic activities of chymosin, bovine pepsin, mucor miehei rennet, cryphonectria parasitica (formerly endothia parasitica) rennet, trypsin, and chymotrypsin on kappa-casein macropeptide were measured. macropeptide solutions (10 mg/ml of .05 m, ph 6.6 phosphate buffer) were incubated with the enzymes at 37 degrees c for various times, and their reactions were stopped by adding .025 ml of pepstatin (1 mg/ml of methanol). peptides released from kappa-casein macropeptide were then fractionated ... | 1992 | 1500545 |
| the crystal and molecular structure of the rhizomucor miehei triacylglyceride lipase at 1.9 a resolution. | the crystal and molecular structure of a triacylglyceride lipase (ec 3.1.1.3) from the fungus rhizomucor miehei was analyzed using x-ray single crystal diffraction data to 1.9 a resolution. the structure was refined to an r-factor of 0.169 for all available data. the details of the molecular architecture and the crystal structure of the enzyme are described. a single polypeptide chain of 269 residues is folded into a rather unusual singly wound beta-sheet domain with predominantly parallel stran ... | 1992 | 1404390 |
| strategies for enzymatic esterification in organic solvents: comparison of microaqueous, biphasic, and micellar systems. | the kinetics of butyl butyrate synthesis by a lipase from mucor miehei in different types of organic media were investigated. the three systems studied were a microaqueous medium containing enzyme in suspension in hexane, a water-hexane two-phase system, and reverse micelles. the synthesis of butyl butyrate was possible in all cases because of a favorable partition of the ester into the organic solvent. a sufficient stirring rate was necessary to achieve good reaction rates in the case of the li ... | 1992 | 1368967 |
| cloning and sequence analysis of cdna encoding rhizopus niveus lipase. | complementary dna encoding rhizopus niveus lipase (rnl) was isolated from the r. niveus if04759 cdna library using a synthetic oligonucleotide corresponding to the amino acid sequence of the enzyme. a clone, which had an insert of 1.0 kilobase pairs, was found to contain the coding region of the enzyme. the lipase gene was expressed in escherichia coli as a lacz fusion protein. the mature rnl consisted of 297 amino acid residues with a molecular mass of 32 kda. the rnl sequence showed significan ... | 1992 | 1368341 |
| recovery of metal ions by microfungal filters. | many microfungi contain chitin/chitosan as an integral part of the cell wall structure. the binding of toxic and heavy metal ions by chitosan or partly deacetylated chitin is a direct consequence of the base strength of the primary amine group and is most effective for those metals that form complexes with ammonia. of the microfungi studied, hyphae from mucor mucedo and rhizomucor miehei, after treatment with hydroxide to expose the chitin/chitosan, were found to be most effective in the capture ... | 1990 | 1366966 |
| interesterification of phosphatidylcholine with lipases in organic media. | lipases were investigated with respect to their ability to catalyse the incorporation of fatty acids into phosphatidylcholine (pc) by interesterification reactions. the enzymes were dried onto solid support materials and the conversions were carried out in water-saturated toluene. three lipases (two fungal and one plant enzyme) had the desired activity; immobilized lipase from mucor miehei (lipozyme) was the most active enzyme. the lipozyme-catalysed interesterification was selective for the sn- ... | 1990 | 1366637 |
| acid proteases from species of mucormii. partial characterization of the acid protease produced by a strain of mucor miehei isolated in cuba. | the acid protease produced by a strain of mucor miehei isolated in cuba was purified by column electrofocusing and partially characterized as to amino-acid composition, molecular weight, helical content, total carbohydrate content, and approximate isoelectric point; a detailed comparison of these results was reported previously for mucor miehei protease (ottesen, m. & rickert, w;s. (1970) c.r. trav. labmcarlsberg 37, 301) suggested that the two enzymes are similar but not identicalmthis conclusi ... | 1975 | 1125813 |
| some effects of temperature on zygospore formation in mucor miehei. | 1976 | 1012305 | |
| amylase production by mucor miehei and m. pusillus. | 1976 | 980001 | |
| hydrolysis of animal fat and vegetable oil with mucor miehei esterase. properties of the enzyme. | 1977 | 893842 | |
| structural and functional determinants of mucor miehei protease vi. inactivation of the enzyme by diazoacetyl norleucine methyl esters, pepstatin and 1,2-epoxy-30(p-nitro-phenyoxy)propane. | mucor miehei protease (ec 3.4.21 -- ), an acid protease of fungal origin, was rapidly inhibited at ph 5.0 and 10 degrees c by a 78-fold molar excess of diazoacetyl norleucine methyl ester (n2ac-nle-ome) when simultaneously added with a 78-fold molar excess of cu(ii). preincubation with cu(ii) before the addition of n2ac-nle-ome reduced the initial rate of activity loss presumably due to a copper-induced structural change as deduced from an examination of cd spectra. cof norleucine and 1.02 +/- 0 ... | 1977 | 831836 |
| action of milk-clotting enzymes on beta-caseins from buffalo's and cow's milk. | beta-caseins isolated from buffalo's and cow's milk were hydrolysed either with rennet or with microbial proteases from mucor miehei, m. pusillus lindt or endothia parasitica. the degradation products were separated by polyacrylamide-gel electrophoresis and the residual beta-casein was determined quantitatively after various times. the electrophoretic patterns of the degradation products of buffalo and bovine beta-casein produced by the different enzymes were not identical. beta-casein of buffal ... | 1976 | 791978 |
| structural and functional determinants of mucor miehei protease. v. enthalpy changes upon thermal denaturation in solution of varying ph. | the thermal denaturation of mucor meihei protease was studied as a function of ph by differential scanning calorimetry. in both citric acid-na2hpo4 and in acetic acid-sodium acetate buffers, maximum thermal stability was at ph 4.0-4.2. however, the maximum enthalpy changes associated with the denaturation process were buffer-dependent and occurred between ph values of 4.7 and 5.7. | 1975 | 235314 |
| carbohydrate nutrition of mucor miehei and m. pusillus. | 1976 | 6908 | |
| acid proteases from species of mucor. iv. hydrogen-tritium exchange of mucor miehei protease. | the kinetics of hydrogen-tritium exchange were studied in the range ph-3 for both the fully and partially tritiated protein. exchange constants for an intermediate class and slow class of hydrogens were determined and found to give a parabolic curve characteristic of acid and base catalysis about the observed phmin of 4.03. the anomalous rate retardation on the acid portion of the curve was attributed to electrostatic interactions which could be evaluated quantitatively from the titration data. ... | 1976 | 5184 |
| acid proteases from species of mucor. iii. interaction with concanavalin a and concanavalin a sepharose. | the reaction of mucor miehei protease with concanavalin a was followed by a turbidimetric assay in the ph range 5-8. at ph 4.0, no turbidity developed but binding of the enzyme to concanavalin a could be demonstrated by gel filtration. two fractions of apparent molecular weight 65000 and 52000 were isolated, the 65000 molecular weight species apparently representing a protomer of concanavalin a (24000) bound to the enzyme. an analysis of the circular dichroism spectrum of this complex suggested ... | 1976 | 4202 |