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At least 127 records · Page 7Linked to original sources
PubMed2000

Production of cephalosporin C by immobilized cells of Cephalosporium acremonium.

Cephalosporium acremonium ATCC 48272 cells were immobilized on various adsorbents and in various entrapment matrices. The influence of the incubation period, the best immobilization technique and the optimum concentrations of the selected matrices were investigated. From the results of the repeated batch fermentation in shake flasks, a good level of antibiotic was maintained for a period of about 19 days using 4% calcium alginate and 1% glass wool as entrapment and adsorbent supports, respectively.

Acremonium↗
PubMed2001

[Studies on chemical constituents of mycelium of fungus Cephalosporium sp. AL031(I)].

Five compounds were isolated from the mycelium of the fungus Cephalosporium sp. AL031 whose metabolites have been proven to possess antifungal and antibacterial activities. Based on the spectral data and elemental analysis, they were identified as ergosterol(I), 2,4,6-octatrienoic acid(II), succinic acid(III), uracil(IV), and D-mannitol(V). All of these compounds were obtained from the culture of this fungus for the first time.

Acremonium↗
PubMed2001

[The effect of culture conditions on the fatty acid composition in the mycelium of the Cephalosporium sp].

The optimal condition of Cephalosporium sp. to culture mycelia and accumulate polyunsaturated fatty acid (PUFA) was researched. The optimal culture condition to get mycelium productivity was: maltose 60 g/L, KNO3 3 g/L, initial pH 6.0, 100 mL medium in 500 mL flask, seeding 25% (v/v), 25 degrees C culture it for 10 days. The optimal condition to accumulation PUFA proportion to total fatty acid was: glucose 10-20 g/L, NH4Cl or (NH4)2SO4 3 g/L, initial pH 4.0, 100 mL medium in 500 mL falsk, seeding 10-20% (v/v) and lighted it when it was cultured. It was suggested that two step could be used in the producing progress. A proposal was put forward that the oileic acid transformed to linoleic acid was the key step to produce PUFA. This proposal gave a base to research the optimal culture condition and enzyme regulation.

Acremonium↗
PubMed2003

[Studies on chemical constituents of mycelium of fungus Cephalosporium sp. AL031(II)].

Three compounds were isolated from the mycelium of the fungus Cephalosporium sp. AL031 whose metabolites have been proven to possess antifungal and antibacterial activities. Based on the spectral data and elemental analysis, they were identified as 3-hydroxy-ergosta-7,22-dien-6-one(A), penicillic acid(B), 4-hydroxy-3,6-dimethyl-2-pyrone(C). All of these compounds were obtained from the culture medium of this fungus for the first time.

Acremonium↗
PubMed2004

[Phenolic acid from culture broth of fungus Cephalosporium sp. AL031].

Three phenolic acids were isolated from the culture broth of the fungus Cephalosporium sp. AL031 whose metabolites have been proven to possess antifungal and antibacterial activities. Their structures were elucidated as 2,4-dihydroxy-3,6-dimethyl-benzoic acid (1),3,6-dihydroxy-2,4-dimethylbenzoic acid(2) and 4-hydroxy-phenylacetic acid(3) by IR, EIMS, 1HNMR, 13CNMR, DEPT, HMQC and HMBC.

Acremonium↗
PubMed2004

[Studies on antibacterial activities of secondary metabolites from fungus Cephalosporium sp. AL031].

The antibacterial activity of fourteen identified compounds from secondary metabolites of fungus Cephalosporium sp. AL031 against eleven gram-positive or gram-negative bacteria in vitro was investigated by agar diffusion assay. The results suggested that two new compounds [S-(+)-5-hydroxymellein, S-(+)-7-hydroxymellein], together with four known compounds [S-(+)-mellein, 2,4-dihydroxy-3,6-dimethylbenzoic acid, 3,6-dihydroxy-2,4-dimethylbenzoic acid and succinic acid] had broad spectrum antibacterial activity. The minimum inhibitory concentrations (MIC) of these six compounds against Shigella sonnei, Mycobacterium tuberculosis and Streptococcus pneumoniae were determined. Their MIC were 0.03125 to approximately 0.5 mg/ml.

Acremonium↗
PubMed1987

Regulation of sulphur amino acids metabolic enzymes in Cephalosporium acremonium strains differing in antibiotic production.

Three strains of Cephalosporium acremonium with different potential of cephalosporin C production show differences in the levels of sulphur amino acid metabolic enzymes. The regulation of these enzymes is also different in the strains. In the superior producing strain two enzymes directly involved in cysteine synthesis are the least susceptible to repression by methionine. In this strain cystathionine metabolizing enzymes seem to favour cysteine synthesis. Antibiotic producing strains, in contrast to the non-producing strain, are highly sensitive to chromate.

Acremonium↗
PubMed1988

Sulphate and methionine as sulphur sources for cysteine and cephalosporin C synthesis in Cephalosporium acremonium.

Three prototrophic strains of Cephalosporium acremonium with different potentials for cephalosporin C production show pronounced differences in pools of intracellular sulphur amino acids. The superior strain exhibits the largest pool, particularly of cysteine (four times that of the non-producing strain). In fermentations with this strain methionine was found to be a much better sulphur source than sulphate for both cysteine and antibiotic synthesis. In the presence of methionine the utilization of sulphate is strongly depressed.

Acremonium↗
PubMedDate not supplied

[Isolation and properties of an alpha-galactosidase preparation from Cephalosporium sp. 237].

Different methods for preparing alpha-galactosidase from the culture fluid of the micromycete Cephalosporium sp. 237 were tested. They included precipitation with ethanol, isopropanol, and acetone. Precipitation with two volumes of acetone gave the best results with respect to specific activity (12 units) and yield of the enzyme (78%). Properties of alpha-galactosidase (optimum pH at 5.5, temperature optimum at 40 degrees C. thermolability, etc), when different substrates were used, were examined.

Acremonium↗
PubMed1984

Cerulenin resistance in a cerulenin-producing fungus. III. Studies on active-site peptides of fatty acid synthetase from Cephalosporium caerulens.

Active-site peptides of acetyl transferase, condensing enzyme and acyl carrier protein in the neighborhood of the prosthetic group, 4'-phosphopantetheine, of Cephalosporium caerulens fatty acid synthetase were investigated. The enzyme was reacted with [14C]acetyl-CoA or [14C]iodoacetamide. 14C-Labeled enzyme was digested with pepsin, trypsin or both. 14C-Labeled peptides were isolated by several purification procedures. The amino acid sequence of the active site of condensing enzyme was determined to be Tyr-Gln-Val-Glu-Ser-Cys-Pro-Ile-Leu-Glu-Gly-Lys and that of acetyl transferase was Phe-Ser-Gly-Ala-Thr-Gly-His-Ser-Gln-Gly. The amino acid composition around the 4'-phosphopantetheine-carrying serine was determined to be Asx2, Thr, Ser, Glx3, Gly2, Ala, Ile, Leu3, and Lys. When these active-site peptides were compared with those of Saccharomyces cerevisiae synthetase, a high degree of homology was observed in the active-site peptides of the acetyl transferase and acyl carrier protein domains. However, that of the condensing enzyme domain gave lower homology. These findings may support the assumption that the low reactivity of cerulenin with C. caerulens synthetase is a consequence of the structure of the condensing enzyme domain.

Acetyl Coenzyme A↗
PubMed1996

Refolding and purification of Cephalosporium acremonium deacetoxycephalosporin C synthetase/hydroxylase from granules of recombinant Escherichia coli.

The gene for bifunctional deacetoxycephalosporin C synthetase/hydroxylase of Cephalosporium acremonium was cloned and overexpressed as an insoluble and inactive enzyme in granules of recombinant Escherichia coli. About 40-60% of expected synthetase activity along with 50-80% protein purity could be recovered directly from granular extracts with only a single empirically optimized refolding step. Further purification to homogeneity was achieved by a single anion-exchange-chromatographic step in the presence of denaturing concentrations of urea. The main obstacle to converting the homogeneous unfolded protein into the active enzyme was a urea-dependent aggregation during refolding that led to irreversible enzyme inactivation. Information obtained from refolding studies using gel-filtration HPLC, fluorescence spectroscopy and disulphide analysis led to an optimal enzyme refolding scheme that resulted in a highly active (i.e. 65-75% of the expected activity) and moderately stable fungal synthetase/hydroxylase.

Acremonium↗