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  • 1
    Electronic Resource
    Electronic Resource
    .beta.-Adrenergic blocking agents. V. 1-Amino-3-(substituted phenoxy)-2-propanols (1969)
    s.l. : American Chemical Society
    Journal of medicinal chemistry 12 (1969), S. 638-642 
    Details
    ISSN: 1520-4804
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jm00304a018
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  • 2
    Electronic Resource
    Electronic Resource
    Another Source of Cellulase (1969)
    [s.l.] : Nature Publishing Group
    Nature 222 (1969), S. 986-987 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Truly cellulolytic micro-organisms are therefore believed to produce both Cj and Cx enzymes, while pseudo-cellulolytic micro-organisms elaborate only the Cx enzymes. Unfortunately, however, the problem has been further complicated in the past by the fact that while cellulolytic fungi were ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/222986b0
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  • 3
    Electronic Resource
    Electronic Resource
    Xylan-hydrolysing enzymes from thermophilic and mesophilic fungi (1991)
    Springer
    World journal of microbiology and biotechnology 7 (1991), S. 475-484 
    Details
    ISSN: 1573-0972
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Screening of 40 mesophilic and 13 thermophilic fungi indicated that enzyme activities capable of degrading oat spelt xylan extensively were produced by only a few of the mesophilic species investigated. The relatively low degree of hydrolysis effected by the enzymes from thermophilic organisms could be explained, in part, by their lack of β-xylosidase. Several strains of Aspergillus awamori and Aspergillus phoenicis were notable in producing high xylanase and β-xylosidase and low protease activities. Of the fungl tested, 13 produced activities capable of removing O-acetyl, arabinosyl, 4-O-methylglucuronyl, feruloyl and coumaroyl substituents from the backbone of xylan polysaccharides as well as endo-1,4-β-d-xylanase and β-1,4-xylosidase. When the growth medium contained oat spelt xylan as carbon source, higher levels of xylanase, β-xylosidase and acetyl xylan esterase were found than in cultures containing meadow fescue grass but the latter were richer in ferulic acid and coumaric acid esterases and 4-O-methylglucuronidase. No single organism or carbon source used was capabie of producing high levels of all the debranching enzymes as well as high levels of enzymes capable of cleaving the glycosidic linkages of the xylan backbone. The best ballnce of enzymes was obtained in cultures of A. awamori IMI 142717 and NRRL 2276 and A. phoenicis IMI 214827. Either of these would be suitable for strain improvement studies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00303373
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  • 4
    Electronic Resource
    Electronic Resource
    Isolation of mutants of Aspergillus awamori with enhanced production of extracellular xylanase and β-xylosidase (1991)
    Springer
    World journal of microbiology and biotechnology 7 (1991), S. 343-354 
    Details
    ISSN: 1573-0972
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Plate screening tests were designed for the selection and isolation of mutant strains of the fungus Aspergillus awamori CMI 142717 showing over-production and constitutive synthesis of xylanase and β-xylosidase. Following mutation by N-methyl-N-nitro-N-nitrosoguanidine, nitrous acid and UV (254 nm), two generations of mutants were isolated and cultured in shake fiasks containing glucose, ball-milled oat straw or oat speit xylan as carbon source. Growth of a number of selected mutants in shake flask culture on medium containing oat spelt xylan produced the highest titres of xylanase and β-xylosidase. Thus, xylanase producton by mutant AANTG43 was 132 U/ml when the Somogyl-Nelson (alkaline copper) method of measuring reducing sugar released was used, or 1160 U/ml using the dinitrosalicylic acid method of reducing sugar analysis. These values were 8-fold higher than those produced by the wild type. A 20-fold improvement in β-xylosidase production was produced by mutant AANO19 (3.51 U/ml). The titres for these two enzyme activities are the highest recorded so far in the literature. Mutant AANTG43 also produced high levels of xylanase (49.8 U/ml) in submerged culture in a fermenter and showed a substantial improvement in the overall productivity of enzyme compared to the wild type strain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00329401
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  • 5
    Electronic Resource
    Electronic Resource
    Hydrolysis of oligosaccharides of the β-(1→4)-linked d-xylose series by an endo(1→4)-β-d-xylanase from the anaerobic rumen fungus Neocallimastix frontalis (1994)
    Springer
    World journal of microbiology and biotechnology 10 (1994), S. 64-68 
    Details
    ISSN: 1573-0972
    Keywords: Anaerobic fungus ; endo-(1→4)-β-d-xylanase ; Neocallimastix frontalis ; rumen fungus ; xylanase ; xylo-oligosaccharides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract An endo-(1→4)-β-d-xylanase from Neocallimastix frontalis was purified by anion-exchange chromatography. The enzyme had an apparent molecular mass of 30 kDa on SDS-PAGE and exhibited maximum activity at 50°C and at pH values between 6.0 and 6.6. Kinetic studies on the hydrolysis of xylo-oligosaccharides, ranging from xylobiose to xylodecaose, showed that xylohexaose and xyloheptaose were the preferred substrates for the enzyme and that xylobiose, xylotriose and xylotetraose were not hydrolysed. Xylose was not a product of the hydrolysis of any of the xylo-oligosaccharide substrates tested. The enzyme appeared to have a strong preference for the hydrolysis of the internal glycosidic bonds of the oligosaccharides, which is typical of endo-(1→4)-β-d-xylanase activity, but it differed from other fungal endo-(1→4)-β-d-xylanases in that it had uniform action on the various internal linkages in the xylo-oligosaccharides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00357566
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  • 6
    Electronic Resource
    Electronic Resource
    Some Pharmacological Properties of a New Adrenergic β-Receptor Antagonist (1966)
    [s.l.] : Nature Publishing Group
    Nature 212 (1966), S. 88-90 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Increases in heart rate were produced in anaesthetized cats by the constant intravenous infusion for 10 min of isoprenaline at 0-2 [xg/kg/min before and after the intravenous infusion for 30 min of 'I. C. I. 45,763' at 1, 5 or 25 [jLg/kg/min. (All drugs were in the racemic form and are here ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/212088a0
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  • 7
    Electronic Resource
    Electronic Resource
    The cellulose system of the anaerobic rumen fungus Neocallimastix frontalis: studies on the properties of fractions rich in endo-(1→4)-β-d-glucanase activity (1995)
    Springer
    Applied microbiology and biotechnology 44 (1995), S. 177-184 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Seven fractions rich in endoglucanase activity were separated from the extracellular cellulase system of the anaerobic rumen fungus Neocallimastix frontalis. The fractions (ES1, ES3, ES2U1, ES2U2, ES2U4, ES2U3C1 and ES2U3C2) were separated from each other and from a fraction that could solubilize crystalline cellulose (the so-called crystalline-cellulose-solubilizing component, CCSC) by the sequential use of differential adsorption on the microcrystalline cellulose Avicel, gel filtration and affinity chromatography on concanavalin-A—Sepharose. The molecular masses of the endoglucanase fractions, when determined by gel filtration, were 64, 30, 61, 113, 17, 38 and 93 kDa respectively. Each enzyme degraded carboxymethylcellulose and was rich in activity to cellulose swollen in phosphoric acid to break the hydrogen bonding: cellobiose, cellotriose and cellotetraose were released in differing proportions. Each fraction showed a characteristic gradient when the capacity of each enzyme to increase the fluidity of a solution of carboxymethylcellulose was plotted against the increase in reducing power of the solution. Although neither endoglucanase fraction, acting in isolation, could degrade crystalline cellulose, three of the fractions (ES1, ES3 and ES2U1) could act synergistically with the CCSC fraction in this regard. Remarkably, the same three fractions also acted in synergism with the cellobiohydrolase (CBH I and CBH II) of the aerobic fungus Penicillium pinophilum in degrading crystalline cellulose, but only when both cellobiohydrolase enzymes were present in the solution along with any one of the three endoglucanases. These observations support the conclusion that the mechanism of action of the cellulase system of N. frontalis in degrading crystalline cellulose may be similar to that operating in the aerobic fungi.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00164499
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  • 8
    Electronic Resource
    Electronic Resource
    Arabinoxylan-degrading enzyme system of the fungus Aspergillus awamori: purification and properties of an α-L-arabinofuranosidase (1996)
    Springer
    Applied microbiology and biotechnology 45 (1996), S. 538-545 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  An α-L-arabinofuranosidase produced by the fungus Aspergillus awamori had a molecular mass of approximately 64 kDa on sodium dodecyl sulphate/polyacrylamide gel electrophoresis (SDS-PAGE) and was optimally active at pH 4.6 and 50°C. The enzyme, which chromatographed as a single component on SDS-PAGE, appeared to consist of two isoenzymes of pI 3.6 and 3.2. Acting in isolation, the α-L-arabinofuranosidase had only a very limited capacity to release L-arabinose (less than 11%) directly from arabinoxylans that had been extracted from a number of plant cell wall preparations using 18% alkali, but a much higher proportion of the L-arabinose (46%) was released from a wheat straw arabinoxylan that had been isolated by steam treatment. There was a marked synergistic effect between the α-L-arabinofuranosidase and an endo-(1→4)-β-D-xylanase produced by A. awamori in both the rate and extent of the release of L-arabinose from both oat straw and wheat straw arabinoxylans, suggesting that L-arabinose-substituted oligosaccharides generated by the endoxylanase action were better substrates for enzyme action. A novel property of the α-L-arabinofuranosidase was its capacity to release a substantial proportion (42%) of feruloyl L-arabinose from intact wheat straw arabinoxylan. The concerted action of the α-L-arabinofuranosidase and endoxylanase released 71% of the feruloyl L-arabinose and 69% of the p-coumaroyl L-arabinose substituents from the wheat straw arabinoxylan.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00578468
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  • 9
    Electronic Resource
    Electronic Resource
    Arabinoxylan-degrading enzyme system of the fungusAspergillus awamori: purification and properties of an α-l-arabinofuranosidase (1996)
    Springer
    Applied microbiology and biotechnology 45 (1996), S. 538-545 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract An α-l-arabinofuranosidase produced by the fungusAspergillus awamori had molecular mass of approximately 64 kDa on sodium dodecyl sulphate/polyacrylamide gel electrophoresis (SDS-PAGE) and was optimally active at pH 4.6 and 50°C. The enzyme, which chromatographed as a single component on SDS-PAGE, appeared to consist of two iso-enzymes of pI 3.6 and 3.2. Acting in isolation, the α-l-arabinofuranosidase had only a very limited capacity to releasel-arabinose (less than 11%) directly from arabinoxylans that had been extracted from a number of plant cell wall preparations using 18% alkali, but a much higher proportion of thel-arabinose (46%) was released from a wheat straw arabinoxylan that had been isolated by steam treatment. There was a marked synergistic effect between the α-l-arabinofuranosidase and an endo-(1 → 4)-β-d-xylanase produced byA. awamori in both the rate and extent of the release ofl-arabinose from both oat straw and wheat straw arabinoxylans, suggesting thatl-arabinose-substituted oligosaccharides generated by the endoxylanase action were better substrates for enzyme action. A novel property of the α-l-arabinofurasidase was its capacity to release a substantial proportion (42%) of feruloyll-arabinose from intact wheat straw arabinoxylan. The concerted action of the α-l-arabinofuranosidase and endoxylanase released 71% of the feruloyll-arabinose and 69% of thep-coumaroyll-arabinose substituents from the wheat straw arabinoxylan.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00578468
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  • 10
    Electronic Resource
    Electronic Resource
    Studies on the capacity of the cellulase of the anaerobic rumen fungus Piromonas communis P to degrade hydrogen bond-ordered cellulose (1995)
    Springer
    Applied microbiology and biotechnology 43 (1995), S. 572-578 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The anaerobic rumen fungus Piromonas communis, when cultured on cotton fibre as the carbon source, produces an extracellular cellulase that is capable of solubilizing “crystalline” hydrogen-bond-ordered cellulose, in the form of the cotton fibre, at a rate that is greater than that of any other cellulases reported in the literature hitherto. The cell-free culture fluid is also very rich in xylan-degrading enzymes. The activity towards crystalline cellulose resides in a high-molecular-mass (approximately 700–1000 kDa) component (so-called crystalline-cellulose-solubilizing component, CCSC) that comprises endo (1 → 4)-β-D-gluconase (carboxymethylcellulase), β-D-glucosidase and another enzyme that appears to be important for the breakdown of hydrogen-bond-ordered cellulose. The CCSC is associated with only a small amount of the endo-(1 → 4)-β-D-glucanase (1.9%), β-D-glucosidase (0.7%) and protein (0.5%) found in the crude cell-free cellulase preparation. The CCSC, unlike the bulk of the endo-(1 → 4)-β-D-glucanase and β-D-glucosidase, is very strongly absorbed on the microcrystalline cellulose, Avicel.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00218468
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