Publications
| Title | Abstract | Year Filter | PMID(sorted ascending) Filter |
|---|
| [comparative characteristics of catalase from the fungus penicillium vitale, which is synthesized under different nutritional conditions]. | a comparative study of properties (absorption spectra, thermostability, ph optimum, polyacrylamide gel electrophoresis, deae-cellulose separation) and structure (amino acid composition, finger-prints, carbohydrate composition) was performed for p. vitale catalase synthesized under different medium conditions. in all cases the results were similar. the only difference occured in the amount of synthesized proteins. a conclusion is drawn that under different nourishing conditions of the fungus the ... | 2006 | 3004 |
| [industrial experiment in obtaining catalase from penicillium vitale pidopl. et bilai]. | 2006 | 11395 | |
| [dissociation of penicillium vitale catalase under the effect of urea and acid ph]. | conditions are studied for penicillium vitale catalase dissociation into subunits under the effect of urea (0.7-8.5 m) and acid ph (5.0-2.0). in 8.0 m urea (ph 5.0) a molecule of the p. vitale catalase dissociates with formation of the components, the sedimentation coefficient of which is 2.4+/-0.2s, the molecular weight is 153000+/-2800. dissociation at ph 2.2 in 4.0 m urea results in formation of components with the sedimentation coefficient 2.2+/-0.3 s. the catalase molecule dissociation unde ... | 2013 | 18833 |
| kinetics and stability of glucooxidase from penicillium vitale. | the kinetics, thermal stability and ultrasonic resistance of glucosoxidase from penicillium vitale have been investigated. its oxidative constant is close to, catalytic constant is 1.7 times less and the reductive constant is 5.4 times more than the respective constants of the enzyme from aspergillus niger. the relationship between the thermal inactivation constant (k(i)=2.1 pt 15.3. the same relationship is true of the ultrasonic inactivation constant and ph in the ph range of 6.5-8.0. in a mor ... | 1978 | 27781 |
| [total activity of glucose oxidase, catalase and invertase and their distribution in the mycelial subcellular fractions of penicillium vitale pidopl. et bilai]. | 2006 | 32465 | |
| [immobilization of penicillium vitale glucose-oxidase on aminosilochrome and properties of immobilized enzyme]. | penicillium vitale glucose-oxidase modified by means of the carbohydrate component oxidation is added covalently to aminoorganosylochrome. the activity of the immobilized preparations is 20-38% depending on the protein-carrier ration in immobilization. comparison of some properties of native and immobilized glucose-oxidase showed that the rh optimum of the immobilized glucose-oxidase is slightly widened towards the alkaline regions; the immobilized glucose-oxidase possesses a considerably higher ... | 2015 | 38549 |
| action of crystalline acid carboxypeptidase from penicillium janthinellum. | acid carboxypeptidase (ec 3.4.12.-) crystallized from culture filtrate of penicillium janthinellum has been investigated for its use in carboxy-terminal sequence determination of z-gly-pro-leu-gly, z-gly-pro-leu-gly-pro, angiotensin i, native lysozyme, native ribonuclease t1, and reduced s-carboxy-methyl-lysozyme. the examination indicated that proline and glycine were liberated from z-gly-pro-leu-gly-pro. at high enzyme concentration, the enzyme catalyzed complete sequential release of amino ac ... | 1975 | 239751 |
| penicillopepsin from penicillium janthinellum crystal structure at 2.8 a and sequence homology with porcine pepsin. | the polypeptide chain of the acid protease penicillo pepsin folds via an 18-stranded mixed beta-sheet into two distinct lobes separated by a 30-a long groove which is the extended substrate binding site. the catalytic residues asp-32 and asp-215 are located in this groove and their carboxyl groups are in intimate contact. alignment of the amino acid sequence with that of pepsin shows regions of high homology. | 1977 | 323722 |
| penicillopepsin: 2.8 a structure, active site conformation and mechanistic implications. | the crystal structure of penicillopepsin, an extracellular acid protease isolated from the mold penicillium janthinellum, has been determined at 2.8 a resolution by the method of multiple isomorphous replacement. the resulting electron density map computed from the native structure factor amplitudes and mir phases has an overall mean figure of merit of 0.90. the molecule is decidedly nonspherical, with the majority of residues in beta-structure. there is an 18-stranded mixed beta-sheet which for ... | 1977 | 339694 |
| the primary structure of calf chymosin. | the complete amino acid sequence of calf chymosin (rennin) (ec 3.4.23.4) has been determined. the sequence consists of a single peptide chain of 323 amino acid residues. the primary structure of the precursor part of calf prochymosin was published previously (pedersen, v.b., and foltmann, b. (1975) eur. j. biochem. 55, 95-103), thus we are now able to account for the total 365 amino acid residues of calf prochymosin. comparison of the sequence of calf prochymosin with that of pig pepsinogen a (e ... | 1979 | 381305 |
| production of tremorgenic toxins by penicillium janthinellum biourge: a possible aetiological factor in ryegrass staggers. | topsoil, herbage and faeces collected during an outbreak of ryegrass staggers in sheep were examined for tremorgenic penicillia. no such fungi were recovered from the plant material, but they were found among the predominant fungi in the soil and faecal samples. the commonest species of penicillium, and almost the only tremorgenic species encountered, was penicillium janthinellum biourge. when fed to sheep, the mycelium of this fungus evoked a number of the clinical signs seen in field cases of ... | 1979 | 475667 |
| the effects of temperature on growth of four high arctic soil fungi in a three-phase system. | the effect of temperature on the growth of chrysosporium pannorum, cylindrocarpon sp., penicillium janthinellum, and phoma herbarum, isolated from tundra soils, was studied. the growth in two systems, glucose-mineral agar plates and sand, moistened with glucose-mineral broth, was compared. all isolates showed an exponential increase in mass (measured as protein increase) in sand and a linear rate of extension on agar. radial increase on agar was shown not to be a good index of growth in sand. tr ... | 1978 | 565246 |
| [effect of amino acids on transformation of glucose oxidase as antigen in tissues of immunized animals]. | the effect of certain amino acids on transformation of glucoseoxidase as an antigen in different tissues of the animals immunized with it showed that the used glucoseoxidase of the fungus penicillium vitale pidopl. et bilaj possesses antigenic properties peculiar to this enzyme isolated from other sources. 1.5 minutes after a single administration of the antigen to nonimmunized rabbits it is determined in them in descending amounts in such an order: blood, lungs, liver, kidneys, lymphatic nodes. ... | 1978 | 567396 |
| [ultrastructure of penicillium vitale pidopl. et bilai--producer of catalase and glucose oxidase]. | 2006 | 604723 | |
| [stabilization of modified glucose oxidase from penicillium vitale incorporated into the polymeric chains of gels]. | glucose oxidase from penicillium vitale was modified by unsaturated compounds, e.g. acrolein, allylisothiocyanate, acryloyl chloride and maleic anhydride. the degree of modification for the respective agents made up to 27.2, 8.3, 11.1 and 35.0% of the amine residues; the enzymatic activity was thereby retained by 98, 100, 0.03 and 58%, respectively. the thermal stability of modified enzymes was decreased 2-7 times. the modified preparations were copolymerized with acrylamide or 2-hydroxyethyl me ... | 1978 | 656485 |
| [spectral properties of the prosthetic group of penicillium vitale catalase]. | differences in the absorption spectrum of the penicillum vitale catalase in the visible region as compared to the absorption spectrum for catalase of animal origin are established to be due to the prosthetic group of the enzyme. a molecule of p. vitale catalase is determined to contain 0.051 +/- 0.0003% of iron. it corresponds to two iron atoms per enzyme molecule and to a twice as low content of iron as in a molecule of the bovine liver catalase. an assumption is advanced that the p. vitale cat ... | 1978 | 664035 |
| purification & properties of an extracellular dextranase from penicillium janthinellum. | 1978 | 748164 | |
| [mechanism of labilization of penicillium vitale glucose oxidase]. | the article deals with conditions for splitting the penicillium vitale glucosooxidase molecule into apoenzyme and coenzyme, for reconstruction of the enzyme from apoenzyme and fad as well as for the effect of some factors ("labilizing" fraction, dithiotreitol) on it. specific activity of the reconstructed enzyme is on the average 85% of the initial enzyme specific activity: "the labilizing" fraction inhibits reconstruction of glucosooxidase from apoenzyme and fad, that is due to oxidation of the ... | 2008 | 867542 |
| [stabilizing effect of calcium ions on glucose oxidase of penicillium vitale]. | reconstruction of p. vitale glucose oxidase from apeonzyme and coenzyme (fad) was studied as affected by iodine acetate as well as mercury and calcium ions. mercury ions, iodine acetate as well as the labilizing fraction (flavin adenine-containing component) are established to inhibit the reconstruction affecting the sulphydryl groups of the apoenzyme which take part in addition of fad to it. calcium ions prevent the effect of the "labilizing" fraction, iodine acetate and mercury ions on the glu ... | 2013 | 888220 |
| [natural variability of penicillium vitale pidopl. et bilai and characteristics of active variants of the fungus that produce glucose oxidase]. | 2008 | 916914 | |
| [comparative evaluation of the enzymatic activity of the mycelial homogenates from penicillium vitale pidopl. et bilai broken down by different methods]. | 2006 | 994870 | |
| [method of purification of glucose oxidase by means of affinity chromatography on immunoabsorbent]. | the possibility to purify glucose oxidase from penicillium vitale on immunosorbent containing specific antibodies to the enzyme covalently bound with sepharose 4b is studied. the method of affinity chromatography was applied, beside routine methods of fractionating blood serum proteins, to isolate specific antibodies from antiserum of rabbits immunized with glucose oxidase. immobilized on sepharose glucose oxidase was used as biospecific sorbent. specific antibodies to the enzyme were isolated u ... | 1975 | 1203397 |
| [preparation in crystalline form of catalase from penicillium vitale pidopl. et bilai]. | 1975 | 1204470 | |
| kininase and anti-inflammatory activities of acid carboxypeptidase from penicillium janthinellum. | the acid carboxypeptidase from penicillium janthinellum catalyzed the rapid release of arginine, and the slow release of phenylalanine, proline, serine and glycine from the carboxy-terminal of bradykinin at ph 4.15 to 4.8. anti-inflammatory activity of the acid carboxypeptidase seems to suggest that the enzyme hydrolyzed bradykinin in vivo. | 1975 | 1204716 |
| [variability in penicillium janthinellum biourge, a producer of the antibiotic janthinellin, under the action of nitrosomethylurea]. | variation of the janthinellin-producing organism p. janthinellum was induced by nitrozomethylurea (nmu). the following concentrations of nmu were tested: 0.5; 0.25, 0.125 per cent at the exposure time of 15 minutes, 1 and 10 hours. the conidia survival had back dependence on the concentration and exposure time. the morphological variation was evident from the presence of forms with changed colour of the colony surface mycelium, light green, brown, light yellow, yellow-pink and white conidia and ... | 1975 | 1211902 |
| [formation of beta-fructofuranosidase by penicillium vitale pidopl. et bilai and other species of the genus penicillium lk]. | 2006 | 1219324 | |
| microbial degradation of the thiolcarbamate herbicide, diallate, in soils and by pure cultures of soil microorganisms. | the disappearance of the herbicide, avadex (40% diallate), from five agricultural soils (differing in either ph, carbon content, or nitrogen content), incubated under sterile and non-sterile conditions, was followed for a period of 20 weeks. avadex was rapidly lost from microbiologically active soils, with over 50% of the applied (2.5 ppm) dosage disappearing within four weeks; losses from sterile soils were much slower with recoveries of over 50% after 20 weeks. incubation of soil with avadex t ... | 1976 | 1267481 |
| [dermatomycoses in workers in enterprises of the microbiological industry]. | mycologic examination of 54 patients with clinical manifestations of dermatomycosis, engaged in glucose oxidase and catalase production has found a producer fungus, penicillium vitale in 31 (38%); 3 out of 37 people contacting with producers of glucamylase and pectofetidine appeared to be infected by aspergillus awamori (1.1%) and aspergillus foetidus (1.1%), respectively. the producers were isolated from the skin of 40 (16.44%) out of 243 workers having no clinical signs of dermatomycosis, main ... | 1992 | 1427292 |
| [identification of toxigenic mould in soft drink causing food poisoning]. | in a soft drink caused food poisoning, white floccus was found and mould count was 6.0 x 10(2) cfu/ml. the mycoflora was made of only one kind of mould which was identified as penicillium janthinellum biourge. this isolate can grow under anaerobic condition. the culture liquid of the isolate was fed to mice orally for toxicity test, which made the mice lose weight. an extract of the culture liquid was tested in weaned mice inaberitoneally for toxicity and all mice died in 24h. the toxic symptoms ... | 1992 | 1606874 |
| laminarinase from penicillium funiculosum and its role in release of beta-glucosidase. | an extracellular laminarinase (1----3)-beta-glucan glucohydrolase (ec 3.2.1.6) was purified from culture filtrates of penicillium funiculosum. it was homogeneous on polyacrylamide gel electrophoresis in the presence and absence of sodium dodecyl sulfate. it had a mr of 14,000 and isoelectric point of ph 4.2. the apparent km value for lamimarinase was 8.3 mg/ml and vmax was 8 mumol/min/mg. the distribution of beta-glucosidase activity in two different species of penicillium showed that p. funicul ... | 1991 | 1904246 |
| differentiation of species and strains among filamentous fungi by dna fingerprinting. | we have analyzed 11 strains and clones, representing five species (penicillium janthinellum, p. citrioviridae, p. chrysogenum, aspergillus niger, trichoderma harzianum) and three genera of filamentous fungi, for the presence of hypervariable loci in their genomes by hybridization with simple repeat oligonucleotides and the dna of phage m13. the oligonucleotide probes (ct)8, (gtg)5 and (gaca)4, as well as m13 dna, are informative probes for fingerprinting in all genera and species tested. the pro ... | 1991 | 1907892 |
| electrophoretic karyotype of cellulolytic penicillium janthinellum strains. | the genome of the cellulolytic fungus penicillium janthinellum biourge was resolved completely by rotating field electrophoresis. the gel pattern revealed 8-10 different chromosomes. on the basis of data for yeast chromosome size standards from schizosaccharomyces pombe and saccharomyces cerevisiae, chromosome sizes in the range from 2.0 to 8 mb were estimated. by southern hybridization with heterologous probes, the chromosomal locations of rdna, the elongation factor ef1, actin and ubiquitin ha ... | 1991 | 1934133 |
| comparative spectral analysis of mammalian, fungal, and bacterial catalases. resonance raman evidence for iron-tyrosinate coordination. | resonance raman spectra are reported for catalases from bovine liver, the ascomycete fungus aspergillus niger, and the bacterium micrococcus luteus. the vibrational frequencies of the oxidation-, spin-, and coordination number-sensitive spectral bands are indicative of high spin pentacoordinate hemes in the resting ferric enzymes of each of these organisms. this result is in accord with the crystal structure of bovine catalase (fita, i., and rossmann, m.g. (1985) j. mol. biol. 185, 21-37). in co ... | 1989 | 2753885 |
| carboxypeptidase s-1 from penicillium janthinellum: enzymatic properties in hydrolysis and aminolysis reactions. | carboxypeptidase s-1 from penicillium janthinellum has been isolated by affinity chromatography and characterized. the enzyme activity is unusually stable in organic solvents, e.g. 80% methanol. the hydrolysis of peptide substrates is apparently dependent on three ionizable groups. one group, with pka of 4.0-4.5, is a catalytically essential residue in its deprotonated form, and another group with a pka of 6.5-7.0 functions in its protonated form, apparently as the binding site for the c-termina ... | 1988 | 3256309 |
| amino acid sequence of endothiapepsin. complete primary structure of the aspartic protease from endothia parasitica. | the amino acid sequence of endothiapepsin, the aspartic protease from endothia parasitica has been determined. the enzyme consists of 330 residues. the sequence determination was performed exclusively at the protein level. the homology of this fungal milk-clotting enzyme with aspartic proteases is demonstrated by alignment with pepsin, chymosin, gastricsin, renin, and cathepsin d from various vertebrates and proteinase a from saccharomyces cerevisiae showing 25-30% identity. the identity with mu ... | 1987 | 3305016 |
| nucleotide sequence of the saccharomyces cerevisiae ctt1 gene and deduced amino-acid sequence of yeast catalase t. | a 2642-base-pair dna fragment containing the catalase t (ctt1) structural gene of the yeast saccharomyces cerevisiae and its flanking regions has been sequenced. the gene codes for a protein of 562 amino acids (relative molecular mass 64,449) and appears to contain no intron. the amino acid sequence of catalase t derived from the dna sequence shows 40.7% homology (52.2% including conservative replacements) to that of bovine liver catalase. all amino acids previously postulated to participate dir ... | 1986 | 3536508 |
| three-dimensional structure of catalase from penicillium vitale at 2.0 a resolution. | the three-dimensional structure analysis of crystalline fungal catalase from penicillium vitale has been extended to 2.0 a resolution. the crystals belong to space group p3(1)21, with the unit cell parameters of a = b = 144.4 a and c = 133.8 a. the asymmetric unit contains half a tetrameric molecule of 222 symmetry. each subunit is a single polypeptide chain of approximately 670 amino acid residues and binds one heme group. the amino acid sequence has been tentatively determined by computer grap ... | 1986 | 3712443 |
| comparison of beef liver and penicillium vitale catalases. | the structures of penicillium vitale and beef liver catalase have been determined to atomic resolution. both catalases are tetrameric proteins with deeply buried heme groups. the amino acid sequence of beef liver catalase is known and contains (at least) 506 amino acid residues. although the sequence of p. vitale catalase has not yet been determined chemically, 670 residues have been built into the 2 a resolution electron density map and have been given tentative assignments. a large portion of ... | 1986 | 3712444 |
| the nadph binding site on beef liver catalase. | beef liver and human erythrocyte catalases (ec 1.11.1.6) bind nadp tenaciously [kirkman, h. n. & gaetani, g. f. (1984) proc. natl. acad. sci. usa 81, 4343-4348]. the position of nadp on beef liver catalase corresponds to the carboxyl-terminal polypeptide hinge in penicillium vitale fungal catalase, which connects the common catalase structure to the additional flavodoxin-like domain. in contrast to nearly all other known structures of protein-bound nadp, nad, and fad, the nadp molecule of beef l ... | 1985 | 3856839 |
| autoradiographic method to screen for soil microorganisms which accumulate zinc. | an autoradiographic method was developed to screen for and isolate soil microorganisms which accumulate zinc (zn). diluted soil samples (rubicon fine sand, entic haplorthods [ph 5.9]) were plated on soil extract-glucose agar containing radioactive 65zn. after 7 days of incubation, individual colonies which accumulated sufficient 65zn could be detected by autoradiography. these colonies were isolated and confirmed as zn accumulators in pure culture by using the autoradiographic plate technique. m ... | 1985 | 3883897 |
| action of serine carboxypeptidases on endopeptidase substrates, peptide-4-methyl-coumaryl-7-amides. | carboxypeptidase y hydrolyzed n-substituted peptide-4-methylcoumarin-7-amides (peptide-nh-mec) at ph 7 by releasing 7-amino-4-methylcoumarin (nh2-mec) which was then followed by carboxypeptidase action. in particular, a chymotrypsin-directed substrate, suc-leu-leu-val-tyr-nh-mec, was hydrolyzed by the enzyme with a second-order rate constant of 7200 m-1 s-1, which is compatible with the rate for an anilide substrate and some n-substituted dipeptides. the activity was completely inhibited by phen ... | 1985 | 3905405 |
| penicillopepsin, the aspartic proteinase from penicillium janthinellum: substrate-binding effects and intermediates in transpeptidation reactions. | 1985 | 3912235 | |
| [study of the subunit structure of catalase from penicillium vitale]. | a molecule of penicillium vitale catalase is shown to dissociate into subunits with the molecular weight 75-80 kdalton. when hemin is splitted off the molecule also disintegrates into subunits equalling 1/4 of the enzyme molecule. the amino acid composition and fingerprints of the catalase subunits were studied. it is supposed that n-terminal residue of the subunit is blocked. | 2015 | 4035792 |
| the active center of catalase. | the refined structure of beef liver catalase (i. fita, a. m. silva, m. r. n. murthy & m. g. rossmann, unpublished results) is here examined with regard to possible catalytic mechanisms. the distal side of the deeply buried heme pocket is connected with the surface of the molecule by one (or possibly two) channel. the electron density representing the heme group, in each of the two crystallographically independent subunits, is consistent with degradation of the porphyrin rings. the heme group app ... | 1985 | 4046038 |
| purification and properties of an extracellular acid ribonuclease from penicillium janthinellum. | 1974 | 4371002 | |
| [carbohydrate components of the glucose oxidase from penicillium vitale]. | 2013 | 4441570 | |
| [variability of penicillium janthinellum biourge--producer of the antibiotic janthinellin and study of the nuclei during ontogenesis of the fungus]. | 2008 | 4453214 | |
| submerged production, purification, and crystallization of acid carboxypeptidase from penicillium janthinellum ifo-8070. | penicillium janthinellum ifo-8070 produced an acid carboxypeptidase of molecular weight 51,000 in a liquid medium at 25 c. maximum enzyme concentration was obtained within 3 to 6 days in a medium containing 2% wheat bran, 1% defatted soybean, and 1% kh(2)po(4); the initial ph was 2 to 4. when submerged aerobic conditions were used, a 51,000-molecular-weight acid carboxypeptidase was produced and no detectable amounts of 160,000-molecular-weight acid carboxypeptidase were produced. acid carboxype ... | 1974 | 4474829 |
| [obtaining purified preparations of catalase from the fungus penicillium vitale pidopl. et bilai]. | 1972 | 4661073 | |
| [formation of glucose oxidase and catalase during the growth of penicillium vitale pidopl. et bilai on media with different nitrogen and carbon ratios]. | 1972 | 4667024 | |
| [study of tubular crystals of penicillium vitale glucose oxidase and its quaternary structure]. | 1973 | 4754779 | |
| influence of inorganic nitrate on the formation of extracellular protease and ribonuclease by penicillium janthinellum. | 1973 | 4762798 | |
| [composition and properties of the catalase from penicillium vitale pidopl. et bilai]. | 2000 | 4790749 | |
| [hydrodynamic properties and molecular weight of penicillium vitale catalase]. | 2016 | 4823742 | |
| [study of the amino acid makeup of the proteins in the mycelial pellicle of penicillium vitale pid. et bil]. | 2006 | 4840331 | |
| a pepsin-like enzyme from penicillium janthinellum. | 1968 | 4866867 | |
| [conditions of direct biosynthesis of catalase by penicillium vitale pidopl. et bilai]. | 2001 | 5153535 | |
| [the effect of the quality of the sowing material on the enzyme activity and flavinogenesis of penicillium vitale pidopl. et bilai under industrial conditions]. | 2015 | 5153983 | |
| a crystalline proteinase (peptidase a) from penicillium janthinellum: preliminary x-ray data. | 1969 | 5346053 | |
| large-scale preparation and some properties of penicillopepsin, the acid proteinase of penicillium janthinellum. | 1970 | 5418964 | |
| [role of inoculum in formation of glucose oxidase and catalase of the penicillium vitale fungus]. | 2000 | 5519073 | |
| [composition and structure of glucose oxidase from penicillium vitale]. | 2013 | 5556037 | |
| [natural variability of the strain penicillium janthinellum biourge--producer of janthinellin]. | 1968 | 5707360 | |
| [glucosooxidase from penicillium vitale pidopl. and bilai]. | 2000 | 5733674 | |
| [on some properties of crystalline and purified non-crystalline glucose-oxidase preparations from penicillium vitale pidopl. et bilai]. | 1965 | 5869922 | |
| [on the mechanism of the stimulatory effect of calcium carbonate on the glucose oxidase and catalase activities of penicillium vitale]. | 2013 | 5871568 | |
| the role of a protease in sporulation of penicillium janthinellum. | 1966 | 5961655 | |
| growth of penicillium janthinellum on glycine as sole carbon and nitrogen source. | penicillium janthinellum is able to grow on glycine as the sole carbon and nitrogen source. the amino acid is transaminated to glyoxylate which is further metabolised to pyruvate by the glycerate pathway. the reaction product of partially purified glycerate kinase from this fungus is 2-phosphoglycerate. phosphoglycerate mutase initiates gluconeogenesis from glycine. partially purified phosphoglycerate mutase is inhibited by fructose 6-phosphate. the possible significance of this regulation is di ... | 1980 | 6251917 |
| [immobilization of penicillium vitale pidopl. et bilai catalase by inorganic carriers]. | an efficient method is developed for p. vitale catalase immobilization through the oxidized carbohydrate enzyme component, using silochrome. the method provides the enzyme binding without losing its catalytic capacity in the immobilized preparation. when the enzyme is immobilized by high-dispersed silica containing isocyanate, aldehyde groups or active atoms of chlorine, 8, 15, and 20 mg of the enzyme is bounded per 1 g of the carrier, respectively, its catalytic capacity being completely retain ... | 2015 | 6266097 |
| [application of ultrafiltration for concentration and purification of penicillium vitale catalase]. | various factors are studied for their effect on the ultrafiltration of penicillium vitale catalase. it is established that acetate cellulose and polyamide membranes may be used for additional purification and deep concentration of native preliminarily purified enzyme solutions. membranes yam-300 and yam-450 are most preferable. at the temperature of 10 degrees c, pressure 0.2 mpa and 100-fold concentration of the catalase solution the enzyme yield at the ultrafiltration stage is 96-100%. | 2015 | 6636309 |
| repression of endo-1,4-beta-glucanase formation in penicillium janthinellum and product inhibition of its 1,4-beta-glucanases and cellobiases. | endo-1,4-beta-glucanase formation of penicillium janthinellum was repressed by glucose, sophorose, and glycerol. chromatography on deae-sephadex a-50 was employed to separate the 1,4-beta-glucanases from two cellobiases. the 1,4-beta-glucanases were inhibited competitively by cellobiose and glucose, and the two cellobiases were inhibited by glucose and glucono-delta-lactone. | 1982 | 6799497 |
| [immobilization of penicillium vitale glucose oxidase by aminoethyl cellulose and properties of immobilized enzyme]. | penicillium vitale glucose oxidase modified by oxidation of the carbohydrate component is in a covalent combination with aminoethyl cellulose (ae-cellulose). with the optimal enzyme: carrier ratio the manifested activity of glucose oxidase in the preparation is 4.3 +/- 0.8% of the attached enzyme activity. it is established that thermostability, stability to an inactivating effect of a labilizing fraction and ph-stability with ph alkaline values in the immobilized glucose oxidase are higher than ... | 2015 | 7281253 |
| [immobilization of penicillium vitale catalase on aminoethyl cellulose and properties of the obtained preparations]. | preparations of penicillium vitale catalase immobilized by aminoethyl cellulose (ae-cellulose) are obtained using two methods: by the enzyme covalent cross-linking with the carrier by glutaric aldehyde and by the covalent binding of catalase to the carrier aminogroups through the carbohydrate enzyme component. a dependence is established for the degree of catalase binding and catalase activity of the immobilized enzyme on the enzyme carrier in immobilization ratio. the optimal enzyme-carrier rat ... | 2015 | 7281254 |
| [stability of penicillium vitale immobilized catalase in continuous decomposition of hydrogen peroxide]. | the process of hydrogen peroxide continuous decomposition by the preparation of the fungus penicillium vitale catalase immobilized by aminoorganosilica which were activated by glutaric aldehyde, cyanuric chloride or 2,4-toluylene diisocyanate. catalase with an oxidized carbohydrate component was used as well. such a modified enzyme was directly bound with the surface of aminocontaining silica and alumina. it is shown that in the process of h2o2 decomposition the preparations of immobilized catal ... | 2015 | 7281255 |
| [comparative kinetics of reactions catalyzed by glucose oxidase in the presence of different electron acceptors]. | it was shown that six redox indicators, beside oxygen, can be used as substrates for glucose oxidase from penicillium vitale. the ph dependence of the rate of glucose oxidase-catalyzed reactions in the presence of oxygen and artificial electron acceptors was studied. in contrast to the reaction involving oxygen, in which the maxima of the ph activity profile were observed at ph 5.6, glucose oxidase reveals maximal ph activity profile at ph 7.5 -- 7.6 in the presence of phenasine methosulfate, ba ... | 1981 | 7284485 |
| the janthitrems: fluorescent tremorgenic toxins produced by penicillium janthinellum isolates from ryegrass pastures. | new tremorgenic mycotoxins named janthitrem a, b, and c (molecular weights 601, 585, and 569, respectively) were produced by more than half of 21 penicillium janthinellum isolates obtained from ryegrass pastures involved in ryegrass staggers outbreaks in sheep. | 1980 | 7356319 |
| [effect of microelements on growth of penicillium vitale pidopl. et bilai and synthesis of a number of extracellular enzymes]. | 2006 | 7402104 | |
| [formation of coenzyme vitamins and flavin-adenine dinucleotide during the growth of penicillium vitale pidopl. et bilai]. | 2006 | 7432204 | |
| the oxidation of pyrene and benzo[a]pyrene by nonbasidiomycete soil fungi. | the purpose of this study was to determine the ability of nonbasidiomycete soil fungi to oxidize pyrene (four rings) and benzo[a]pyrene (bap) (five rings). fungi were isolated from five different soils in which the polycyclic aromatic hydrocarbon content ranged from 0.8 to 80 micrograms/g dry soil. approximately 50% of the isolates in all sites were able to oxidize pyrene. the pyrene-oxidizing species belonged to all fungal divisions except basidiomycetes. the most common were penicillium spp. o ... | 1995 | 7627908 |
| crystal structure of catalase hpii from escherichia coli. | catalase is a ubiquitous enzyme present in both the prokaryotic and eukaryotic cells of aerobic organisms. it serves, in part, to protect the cell from the toxic effects of small peroxides. escherichia coli produces two catalases, hpi and hpii, that are quite distinct from other catalases in physical structure and catalytic properties. hpii, studied in this work, is encoded by the kate gene, and has been characterized as an oligomeric, monofunctional catalase containing one cis-heme d prosthetic ... | 1995 | 7663946 |
| the primary structure of carboxypeptidase s3 from penicillium janthinellum ibt 3991. | the complete amino acid sequence of penicillopeptidase s3, a serine carboxypeptidase isolated from penicillium janthinellum ibt 3991, has been determined. the enzyme consists of 481 amino acids arranged in a single polypeptide chain. six glycosylation sites were established in positions 41, 218, 256, 326, 384 and 392. the molecule contains six cysteinyl residues among which disulfide bridges was established between cys-71-cys-333 and cys-233-cys-289. carboxypeptidase s3 is homologous to carboxyp ... | 1995 | 7664873 |
| novel serine penicillocarboxypeptidase cpd-s3 from penicillium janthinellum ibt 3991: purification, characterization, and uses in peptide synthesis and modification. | a novel carboxypeptidase (cpd-s3) from penicillium janthinellum ibt 3991 has been isolated in a two-step purification procedure by cation exchange and affinity chromatography. the enzyme is a serine carboxypeptidase with a denatured molecular mass determined by sds of 62 kda of which 32% is carbohydrate. the isoelectric point is 5.1. cpd-s3 exhibits a high stability towards organic solvents and elevated temperatures. besides the carboxypeptidase activity, cpd-s3 exhibits esterase, amidase, and c ... | 1993 | 7764295 |
| production of extracellular xylanases by penicillium janthinellum. effect of selected growth conditions. | xylanase production by penicillium janthinellum using 10-100 mm of 2,2-dimethylsuccinate (dms) buffer, in a range of ph 4.5-6.0 was studied. the enzyme activity was enhanced using oat xylan as the carbon source. under these conditions a culture produced 1.14 mumol/min (11.4 u/ml or 84.4 u/mg) of beta-xylanase after 5 d of growth in a 10-mm buffer solution at ph 4.5. protease was absent in the dms buffer except when 100 mm phosphate buffer at ph 6.0 was used (4 u/ml). beta-xylosidase was only fou ... | 1994 | 7944349 |
| pea (pisum sativum l.) seed isolectins 1 and 2 and pea root lectin result from carboxypeptidase-like processing of a single gene product. | the complete amino acid sequences of the alpha-subunits of pea (pisum sativum l.) seed and root lectin, the c-terminal amino acids of the beta-subunits of pea seed lectin, and most of the sequence of the beta-subunit of pea root lectin were determined. in contrast to earlier reports it was shown that the beta-subunits of both seed isolectins end at asn-181. the alpha 1 subunits end at gln-241 (major fraction) or lys-240 (minor fraction), whereas the alpha 2 subunits end at ser-239, ser-238, ser- ... | 1994 | 8111028 |
| the primary structure of carboxypeptidase s1 from penicillium janthinellum. | the complete amino acid sequence of carboxypeptidase s1 from penicillium janthinellium has been determined by n-terminal sequencing of the reduced and vinylpyridinated protein and of peptides obtained by cleaved with cyanogen bromide, iodosobenzoic acid, hydroxylamine, endoproteinase lysc, endoproteinase aspn and glu-specific proteinase from b. licheniformis. the enzyme consists of a single peptide chain of 433 amino acid residues and contains 9 half-cystine residues and one glycosylated asparag ... | 1993 | 8224168 |
| cloning, sequencing, and heterologous expression of a cellulase-encoding cdna (cbh1) from penicillium janthinellum. | from a penicillium janthinellum cdna library, two clones with 1.8- and 1.9-kb inserts were isolated by hybridization to a trichoderma reesei cellulase-encoding gene probe (egl1). both cdnas have identical 5' ends and coding sequences, but different polyadenylation start points in their 3' untranslated regions. in the nucleotide (nt) sequence, one open reading frame of 537 amino acids was detected which shows 56% homology with endoglucanase i of t. reesei and 70% homology with cellobiohydrolase i ... | 1993 | 8440481 |
| molecular analysis and overexpression of the gene encoding endothiapepsin, an aspartic protease from cryphonectria parasitica. | the gene, epn-1, encoding endothiapepsin (epn), an aspartic protease (aspp) synthesized and secreted by the ascomycete fungus responsible for chestnut blight, cryphonectria (endothia) parasitica, was identified and characterized. inspection of the nucleotide and deduced amino acid (aa) sequences revealed perfect agreement with the experimentally derived 330-aa sequence of mature epn [barkholt, eur. j. biochem. 167 (1987) 327-338] and an additional 89 aa of putative preprosequence. of the nine fu ... | 1993 | 8462868 |
| distribution and properties of fructosyl amino acid oxidase in fungi. | fructosyl amino acid oxidase, and enzyme that can be used for the determination of glycated proteins in blood samples from diabetic patients, was used to screen cultures in our microorganism culture collection. fructosyl amino acid oxidase was found only in the strains of four genera of fungi, aspergillus, fusarium, gibberella, and penicillium and exhibited different substrate specificities against fructosyl valine and n epsilon-fructosyl n alpha-z-lysine. a fructosyl valine-specific enzyme from ... | 1995 | 8534116 |
| structure of the heme d of penicillium vitale and escherichia coli catalases. | a heme d prosthetic group with the configuration of a cis-hydroxychlorin gamma-spirolactone has been found in the crystal structures of penicillium vitale catalase and escherichia coli catalase hydroperoxidase ii (hpii). the absolute stereochemistry of the two heme d chiral carbon atoms has been shown to be identical. for both catalases the heme d is rotated 180 degrees about the axis defined by the alpha-gamma-meso carbon atoms, with respect to the orientation found for heme b in beef liver cat ... | 1996 | 8621527 |
| endoglucanase ii (egii) of penicillium janthinellum: cdna sequence, heterologous expression and promotor analysis. | the cdna coding for the endoglucanase egii of p. janthinellum was cloned and sequenced. the open reading frame comprises 1230 nucleotides and the deduced amino-acid sequence shows an overall homology of 63% with the t. reesei egl2. the cellulose-binding domain of egii represents a typical member of the a family of cellulases. the egl2 gene is only induced by cellulose or cellobiose and not by sophorose. a promotor fragment including 1 kb was cloned and sequenced. three major transcription startp ... | 1996 | 8625430 |
| [the kinetic and catalytic properties of penicillium vitale catalase]. | the steady-state kinetics of catalytic action of penicillium vitale catalase has been studied. the enzyme reaction conforms to the michaelis-menten equation, which is shown by considering the initial velocity of the enzyme-catalytic reaction with increased concentrations of hydrogen-peroxide and sodium perborate. the parameter km value is rather large (231-259) mm. on the other hand the pen, vitale catalase is one of the more active enzymes and shows kcat values equal to 0.8-3.0 x 10(-6) s-1 and ... | 2015 | 9005665 |
| primary structures of fungal fructosyl amino acid oxidases and their application to the measurement of glycated proteins. | fructosyl amino acid oxidase (faod), which is active toward model compounds of the glycated proteins in blood, n epsilon-fructosyl n sigma-z-lysine and n-fructosyl valine, was purified to homogeneity from aspergillus terreus gp1. though the enzyme did not use glycated proteins directly as its substrate, it used glycated human serum albumin (hsa) when hsa was treated with a protease. linear relationships between both the concentration and the increase in absorbance and the glycation rate of glyca ... | 1996 | 9022674 |
| [complete amino acid sequence of catalase from the fungus penicillium vitale]. | the polypeptide sequence of the unmodified catalase from penicillium vitale containing 696 amino acid residues was deduced. the sequences of 76 tryptic peptides of the unmodified catalase, 63 tryptic peptides of the catalase with modified lys residues, 48 peptides resulting from catalase cleavage by the staphylococcus aureus v8 protease, and 9 fragments obtained by brcn-treatment were considered, and a comparison with the sequences of other catalases was made. | 1998 | 9612556 |
| the amino acid sequences of carboxypeptidases i and ii from aspergillus niger and their stability in the presence of divalent cations. | the amino acid sequences of serine carboxypeptidase i (cpd-i) and ii (cpd-ii), respectively, from aspergillus niger have been determined by conventional edman degradation of the reduced and vinylpyridinated enzymes and peptides hereof generated by cleavage with cyanogen bromide, iodobenzoic acid, glutamic acid cleaving enzyme, aspn-endoproteinase and endolysc proteinase. cpd-i consists of a single peptide chain of 471 amino acid residues, three disulfide bridges and nine n-glycosylated asparagin ... | 1998 | 9748653 |
| optimization of pyrene oxidation by penicillium janthinellum using response-surface methodology. | at present, there is little information on the optimization of the degradation of polycyclic aromatic hydrocarbons (pah) by deuteromycete filamentous fungi, a reaction catalyzed by cytochrome p450 monooxygenases. we utilized response-surface methodology to determine the optimal growth conditions for the oxidation of the pah pyrene by penicillium janthinellum sfu403, with respect to the variables glucose concentration, nitrate concentration and bioconversion time. models were derived for the rela ... | 1999 | 10341435 |
| inactivation of mucor plumbeus by the combined actions of chitinase and high hydrostatic pressure. | sporangiospores were treated with high hydrostatic pressure and/or fungal chitinase in order to study the inhibition of germination and growth of the food spoiling mold mucor plumbeus. total fungal inhibition was obtained either at 4.0 kbar or by 10 u/ml of chitinase from penicillium janthinellum. a pretreatment with 1 u/ml of the same chitinase reduced the pressure necessary to obtain complete spore inhibition to 3 kbar. | 1999 | 10573398 |
| degradation and mineralization of high-molecular-weight polycyclic aromatic hydrocarbons by defined fungal-bacterial cocultures. | this study investigated the biodegradation of high-molecular-weight polycyclic aromatic hydrocarbons (pahs) in liquid media and soil by bacteria (stenotrophomonas maltophilia vun 10,010 and bacterial consortium vun 10,009) and a fungus (penicillium janthinellum vuo 10, 201) that were isolated from separate creosote- and manufactured-gas plant-contaminated soils. the bacteria could use pyrene as their sole carbon and energy source in a basal salts medium (bsm) and mineralized significant amounts ... | 2000 | 10698765 |
| beta-xylosidase recovery by reversed micelles. use of cationic surfactant. | beta-xylosidase, an enzyme produced by penicillium janthinellum fungus, was prepurified by fractionated precipitation with ethanol and extracted by reversed micelles of n-benzyl-n-dodecyl-n-bis(2-hydroxyethyl) ammonium chloride (bdbac) cationic surfactant. a 2(5-1) fractional factorial design was employed to evaluate the influence of the following factors on the enzyme extraction: ph (a), conductivity (b), surfactant concentration (c), cosolvent concentration (d) and temperature (e). a statistic ... | 2000 | 10849861 |
| penicillopepsin-jt2, a recombinant enzyme from penicillium janthinellum and the contribution of a hydrogen bond in subsite s3 to k(cat). | the nucleotide sequence of the gene (pepa) of a zymogen of an aspartic proteinase from penicillium janthinellum with a 71% identity in the deduced amino acid sequence to penicillopepsin (which we propose to call penicillopepsin-jt1) has been determined. the gene consists of 60 codons for a putative leader sequence of 20 amino acid residues, a sequence of about 150 nucleotides that probably codes for an activation peptide and a sequence with two introns that codes for the active aspartic proteina ... | 2000 | 10850809 |
| [taxonomic position and nitrogen-containing secondary metabolites of the fungus penicillium vitale pidoplichko et bilai apud bilai]. | the type strain penicillium vitale pidoplichko et bilai apud bilai 1961 vkm f-3624 was found to considerably differ from a sibling species p. janthinellium (syn. p. simplicissimum) in some physiological and morphological features (growth rates at different temperatures, the size of philiades, and the shape of conidia), as well as in the pattern of the nitrogen-containing secondary metabolites produced (roquefortine, 3,12-dihydroroquefortine, meleagrin, aurantioclavine, indole-3-acetic acid, and ... | 2013 | 10920814 |