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At least 19 recordsLinked to original sources

PubMed1979

Penicillin G production by immobilized whole cells of Penicillium chrysogenum.

Penicillium chrysogenum was immobilized in polyacrylamide gel prepared from 5% acrylamide monomers (85% acrylamide and 15% N,N'-methylene bisacrylamide). Penicillin produced from glucose by the immobilized mycelium was 17% of that produced by washed mycelium. However, the activity of penicillin production of the washed mycelium decreased with repeated use. On the other hand, the activity of the immobilized mycelium increased initially and decreased gradually with repeated use. The rate of oxygen uptake of the immobilized mycelium was about 30% of that of the washed mycelium. The immobilized mycelium required oxygen for the production of penicillin.

2-Aminoadipic Acid↗

PubMed1977

A taxonomic study of the Penicillium chrysogenum series.

The taxonomy of the Penicillium chrysogenum series is reconsidered. On account of the observations of the available type strains and numerous isolates mainly obtained from food products, Penicillium notatum Westling, P. meleagrinum Biourge and P. cyaneofulyum Biourge are placed in synonymy with P. chrysogenum Thom. Synonymy and variability of the species are discussed.

Mutation↗

PubMedDate not supplied

[Biosynthesis of penicillin upon periodic culturing of Penicillium chrysogenum with an exponentially increasing glucose supply].

Penicillium chrysogenum was cultivated under controlled conditions and at constant specific growth rates regulated by glucose supply. The rate of penicillin synthesis (units/mg dry weight.hr) and pattern of time changes of the synthesizing capacity of the culture depended on the specific growth rate (hr-1). The arrest of penicillin synthesis was induced by the inherent changes of the culture rather than by external factors, e.g. use of substrates, changed limitation, accumulation of inhibitory metabolites, etc.

Culture Media↗

PubMed1979

The site of benzyl penicillin accumulation in Penicillium chrysogenum.

Benzyl penicillin was localized in cells of Penicillium chrysogenum by means of enzymatical and immunological methods, enabling the determination of minute amounts of penicillin. The reactions were performed on ultrathin sections. They allow to determine the antibiotic inside of the cells. The results indicate that benzyl penicillin is present in the vesicles belonging to the Golgi apparatus. Benzyl penicillin is transported from the cytoplasm outside the cell membrane by the Golgi vesicles.

Golgi Apparatus↗

PubMed1977

Effects of lysine analogs on Penicillium chrysogenum.

Compounds structurally related to lysine were tested against Penicillium chrysogenum Wis. 54-1255 for inhibition of growth, sporulation, and penicillin formation. This strain is relatively resistant to lysine analogs. The compounds that were the more active inhibitors of growth and whose activities were reversed by L-lysine were diaminohexynoic acid, N-epsilon-methyllysine, N-alpha-methyllysine, and diaminopimelic acid. These four compounds also inhibited sporulation, which was more sensitive to inhibition than growth was. Analogs strongly inhibiting benzyl-penicillin formation by resting mycelia were diaminohexynoic acid and N-epsilon-methyllysine. The action of the most active analog (diaminohexynoic acid) on penicillin synthesis was reversed by DL-alpha-aminoadipic acid.

2-Aminoadipic Acid↗

PubMed1979

Genetic and biochemical studies of mutants of Penicillium chrysogenum impaired in penicillin production.

Seventy-eight mutants of Penicillium chrysogenum strain NRRL 1951, that were impaired in penicillin production, were isolated following treatment with various mutagens. Twelve that yielded about 10% of their parental penicillin titre were studied in detail. Analyses of heterozygous diploids formed between them revealed the existence of at least five complementation groups with respect to penicillin production--V, W, X, Y and Z. Most mutants belonged to group Y. A biochemical investigation of the intracellular peptides in strains representing the five groups demonstrated the absence of the tripeptide alpha-aminoadipoylcysteinyl-valine from mutants of groups X, Y and Z. Extracts of mutants of groups W, Y and Z were able to catalyse a penicillin acyl-exchange reaction, a mutant of group V showed only a trace of activity and mutant from group X completely lacked this ability.

Amino Acids↗

PubMed1979

Lysine regulation of penicillin biosynthesis in low-producing and industrial strains of Penicillium chrysogenum.

The inhibitory effect of L-lysine on penicillin biosynthesis by Penicillium chrysogenum has been compared in a low-producing strain (Wis. 54-1255) and a high-producing strain (ASP-78). Lysine inhibited total penicillin synthesis to a similar extent in both strains. However, in the high-producing strain the onset of penicillin synthesis occurred even at a high lysine concentration, whereas in the low-producing strain lysine had to be depleted before penicillin production commenced.

Culture Media↗

PubMed1979

[Penicillin biosynthesis and amino acid metabolism in Penicillium chrysogenum in experiments with washed mycelium].

The study of the amino acid metabolism in Penicillium chrysogenum with the use of washed mycelium showed that the amount of the free intracellular amino acids significantly decreased during the process of penicillin production. Still, such a decrease did not cover the nitrogen requirements of the culture for the antibiotic synthesis and mobilization of the protein nitrogen took place. By the end of the process the amount of the protein nitrogen markedly decreased. At the same time alpha-amino nitrogen was absent in the fermentation broth filtrate. About 14 amino acids (including cysteine and valine) which participate in constriuction of the penicillin molecule nucleus were found in the amino acid poll. However, the amounts of cysteine and valine were not high and probably other free intracellular amino acids participated in their synthesis. It was shown that one of the limiting factors in the process of penicillin biosynthesis was synthesis of cysteine, a sulphur-containing amino acid which is one of the precursors of the antibiotic molecule nucleus.

Amino Acids↗

PubMed1978

Uptake and metabolism of alpha-aminoadipic acid by Penicillium chrysogenum Wis 54-1255.

The uptake of 1-14C-DL-alpha-aminoadipate in resting mycelium of Penicillium chrysogenum Wis 54-1255 and its metabolism during benzylpenicillin formation were studied. The pH optimum for uptake at 25 degrees C was 6.4. Over a range of concentrations from 0.01--1.0 mM, approximately 45% of 1-14C-DL-alpha-aminoadipate was taken up by carbon-starved mycelium. 14CO2 was formed at a low rate, and the total formed amounted to only 1--3% of the 1-14C-DL-alpha-aminoadipate supplied. The intracellular pool of alpha-aminoadipate appears to be expandable, depending on the concentration of alpha-aminoadipate in the medium. The rate of penicillin synthesis depended on the intracellular concentration of alpha-aminoadipate. Penicillin biosynthesis achieved half of the maximum rate at an intracellular concentration of 0.06 nmol alpha-aminoadipate/mg dry cell weight. This low concentration, the result of adding 0.01 mM DL-alpha-aminoadipate to the medium, was sufficient to reverse the inhibition of penicillin biosynthesis caused by 10 mM extracellular L-lysine. Aminoadipate appears to be recycled during penicillin formation. Labeled alpha-ketoadipate was formed from alpha-aminoadipate to the extent of about 25%.

2-Aminoadipic Acid↗

PubMed1979

The ultrastructure of Penicillium chrysogenum in the course of benzyl-penicillin biosynthesis.

The find structures of high- and low-yield mutants of Penicillium chrysogenum, producing 100 and 10,000 units/ml of penicillin G, were compared. The cells of both mutants demonstrated a typical eukaryotic ultrastructure. In the cytoplasm nuclei, mitochondira, lipid bodies, endoplasmic reticulum, and Golgi vesicles were observed. In the cells of high-yield mutant, during the biosynthesis of penicillin, the number of lipid bodies decreased. It is possible that the lipids are metabolized in the process of biosynthesis of penicillin. In the cytoplasm more multivesicular bodies and small vesicles, about 40 nm in diameter, could be seen. These Golgi vesicles, present in largest number in cells of high-yield mutant, fuse with the cell membrane and play an important role in the transport of penicillin from the cytoplasm to the cell environment. The cell walls of the high-yield mutant become three times thicker during the antibiotic biosynthesis. No comparable changes were observed in the ultrastructure of the low-yield mutant. The cell wall thickness did not increase, the cytoplasm contained few Golgi vesicles only, and the lipid bodies can be seen in all cells.

Cell Membrane↗

PubMed1979

ATP sulfurylase from Penicillium chrysogenum: is the internal level of the enzyme sufficient to account for the rate of sulfate utilization?

The in vivo rate of sulfate activation in Penicillium chrysogenum (wild-type strain ATCC 24791) was determined to be 0.19 +/- 0.09 mumol g(-1) (dry weight) min(-1) by the following methods. (i) The maximum growth of the organism in synthetic medium was a linear function of the initial Na(2)SO(4) concentration between 0 and 8 x 10(-4) Na(2)SO(4). The growth yield was 1.64 x 10(-2) g (dry weight) of mycelium per mumol of added sulfate, corresponding to a minimum sulfur requirement of 61 mumol/g (dry weight). Under these conditions (limiting sulfate) the minimum doubling time of P. chrysogenum in submerged culture was about 3.8 h, corresponding to a maximum exponential growth rate constant of 3.0 x 10(-3) min(-1). If all the sulfur in this mycelium passed through adenosine-5'-phosphosulfate, the rate of sulfate activation in vivo must have been 0.183 mumol min(-1) g(-1) (dry weight). (ii) In the presence of excess (35)SO(4) (2-), the total organic (35)S produced varied with the mycelial growth rate. However, until the culture approached maximum density, the product of [(growth rate constant) x (organic (35)S content)] was nearly constant at 0.24 to 0.28 mumol min(-1) g(-1) (dry weight). (iii) A sulfur-starved mycelium pulsed with 10(-4) M (35)SO(4) (2-) produced organic (35)S at a rate of about 0.10 mumol min(-1) g(-1) (dry weight) under conditions where the internal concentrations of ATP and sulfate would permit ATP sulfurylase to operate at about 70% of its V(max). Cell-free extracts of P. chrysogenum growing rapidly on excess sulfate contained 0.22 U of ATP sulfurylase per g (dry weight). Thus, in spite of the relatively low specific activity of homogeneous ATP sulfurylase (0.13 U/mg of protein, corresponding to an active site turnover of 7.15 min(-1)), the mycelial content of the enzyme was sufficient to account for the observed growth rate of the organism on inorganic sulfate as the sole sulfur source.

Biological Transport, Active↗

PubMed1976

Incorporation of double-labelled valine into delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine by Penicillium chrysogenum.

The incorporation of valine into the LLD-tripeptide, delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine, a precursor of penicillin, was studied by incubating mycelial mats of Penicillium chrysogenum Wis. 49-2105 with double labelled valines. L-valine was incorporated into the LLD-tripeptide without formation of an alpha, beta-didehydrovaline intermediate. Intact D-valine was not incorporated into the LLD-tripeptide.

Carbon Radioisotopes↗

PubMed1976

The absolute configuration of the amino acids in delta-(alpha-aminoadipyl)cysteinylvaline from Penicillium chrysogenum.

Radioactive carbon-14 L-alpha-aminoadipic acid, L-cysteine, or L-valine were readily incorporated into the intracellular tripeptide, delta-(alpha-aminoadipyl)cysteinylvaline (ACV), by washed starved cells of Penicillium chrysogenum. The labeled ACV in each case was oxidized with performic acid and isolated as its corresponding sulfonic acid derivative. After acid hydrolysis, the configuration of the component acids was determined by L- and D-amino acid oxidases, which showed the tripeptide (ACV) from P. chrysogenum to be delta-(L-aminoadipyl)-L-cysteinyl-D-valine.

2-Aminoadipic Acid↗

PubMed1976

[Mutagenic action of N-nitrosodimethylurea on Actinomyces rimosus and Penicillium chrysogenum].

High mutagenic activity of N-nitrozodimethylurea (NDMU), an agent of the group of the nitrozo compounds not studied in detail was shown with respect to prototrophic and auxotrophic strains of Actinomyces rimosus, an organism producing oxytetracycline and Penicillium chrysogenum, an organism producing penicillin. The rate of direct and back mutations in the auxotrophic strain of Act. rimosus under the effect of NDMU was many times higher than that of spontaneous mutations. NDMU was used at one of the selection stages at which a more active variant of Act. rimosus was obtained. This is evident of a possible use of the mutagen for induction of variation with respect to the quantitative feature of oxytetracycline production. A great number of morphologically changed forms and biochemical mutants of Pen. chrysogenum formed under the effect of this substance. NDMU induced a mutant of Pen. chrysogenum capable of selective synthesis of 6-aminopenicillinic acid without addition of the precursor.

Genetic Variation↗

PubMed1977