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  • 1
    Electronic Resource
    Electronic Resource
    Alkaline detergent enzymes from alkaliphiles: enzymatic properties, genetics, and structures (1998)
    Springer
    Extremophiles 2 (1998), S. 185-190 
    Details
    ISSN: 1433-4909
    Keywords: Key words Alkaliphile ; Bacillus ; Detergent enzyme ; α-Amylase ; Debranching enzyme ; Protease ; Cellulase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The cleaning power of detergents seems to have peaked; all detergents contain similar ingredients and are based on similar detergency mechanisms. To improve detergency, modern types of heavy-duty powder detegents and automatic dishwasher detergents usually contain one or more enzymes, such as protease, amylase, cellulase, and lipase. Alkaliphilic Bacillus strains are often good sources of alkaline extracellular enzymes, the properties of which fulfil the essential requirements for enzymes to be used in detergents. We have isolated numbers of alkaliphilic Bacillus that produce such alkaline detergent enzymes, including cellulase (CMCase), protease, α-amylase, and debranching enzymes, and have succeeded in large-scale industrial production of some of these enzymes. Here, we describe the enzymatic properties, genetics, and structures of the detergent enzymes that we have developed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007920050059
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  • 2
    Electronic Resource
    Electronic Resource
    Catalytic decomposition of N2O over supported rhodium catalysts: high activities of Rh/USY and Rh/Al2O3 and the effect of Rh precursors (1997)
    Springer
    Catalysis letters 47 (1997), S. 173-175 
    Details
    ISSN: 1572-879X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The catalytic decomposition of nitrous oxide to nitrogen and oxygen has been studied over Al2O3-supported and zeolite-supported Rh catalysts. The activities of Rh/Al2O3 and Rh/USY (ultrastable Y zeolite) catalysts prepared from Rh(NO3)3 were higher than those of Rh/ZSM-5 and Rh/ZnO reported in the literature, while the activity of a Rh/Al2O3 catalyst prepared from RhCl3 was suppressed severely in spite of the high H/Rh and CO/Rh values. The catalytic activity of N2O decomposition was sensitive not only to the Rh dispersion but also to the preparation variables such as the Rh precursors and the supports used.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1019017407609
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  • 3
    Electronic Resource
    Electronic Resource
    Long lifetime operation of an ArF-excimer laser (1996)
    Springer
    Applied physics 63 (1996), S. 229-235 
    Details
    ISSN: 1432-0649
    Keywords: 42.55
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract An experimental investigation to improve the lifetime of a discharge-excited ArF-excimer laser is presented. The three dominant factors restricting its lifetime are CF4 generation in the laser gas, color-center formation in the optics and input power density reduction due to electrode ablation. Copper electrodes were superior to nickel electrodes in regard to electrode ablation. A gas lifetime of more than 109 shots (about one month at 400 Hz) is shown for an ArF-excimer laser with a liquid-nitrogen trap and high-temperature zirconium alloy trap.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01833791
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  • 4
    Electronic Resource
    Electronic Resource
    Long lifetime operation of an ArF-excimer laser (1996)
    Springer
    Applied physics 63 (1996), S. 229-235 
    Details
    ISSN: 1432-0649
    Keywords: PACS: 42.55
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract.  An experimental investigation to improve the lifetime of a discharge-excited ArF-excimer laser is presented. The three dominant factors restricting its lifetime are CF4 generation in the laser gas, color-center formation in the optics and input power density reduction due to electrode ablation. Copper electrodes were superior to nickel electrodes in regard to electrode ablation. A gas lifetime of more than 109 shots (about one month at 400 Hz) is shown for an ArF-excimer laser with a liquid-nitrogen trap and high-temperature zirconium alloy trap.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01833791
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  • 5
    Electronic Resource
    Electronic Resource
    Continuous operation up to 3 kHz in a discharge-pumped XeCl excimer laser (1996)
    Springer
    Applied physics 63 (1996), S. 1-7 
    Details
    ISSN: 1432-0649
    Keywords: 42.55
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Continuous operations at a high repetition rate up to 3 kHz for discharge-pumped XeCl excimer laser are presented. The dependence of the clearing ratio on laser-gas pressure and input energy densities is studied. It was found that suitable laser-gas pressures minimize the clearing ratio for various input-energy densities. It is also shown that few density disturbances in the discharge region are induced by gas heating in a discharge-pumped XeCl excimer laser with low input-energy density
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01112828
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  • 6
    Electronic Resource
    Electronic Resource
    Gas contaminant effect in a discharge-excited ArF excimer laser (1998)
    Springer
    Applied physics 66 (1998), S. 579-583 
    Details
    ISSN: 1432-0649
    Keywords: PACS: 42.55
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: 4 , O2 and N2 in a discharge-excited ArF-excimer laser. Measured characteristics include laser pulse energy, small-signal gain, and laser spectrum. Measurement results indicate that laser pulse energy degradation for such impurities (〈100 ppm) is mainly due to optical absorption. It has also been found that for O2 contaminants laser pulse energy degradation is strongly dependent on operational repetition rates; at higher repetition rates, an increased concentration of O2 impurities results in a reduced small-signal gain and a consequent decline in laser pulse energy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003400050438
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  • 7
    Electronic Resource
    Electronic Resource
    Purification and properties of an alkaline protease from alkalophilic Bacillus sp. KSM-K16 (1995)
    Springer
    Applied microbiology and biotechnology 43 (1995), S. 473-481 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  Alkaline protease (EC 3.4.21.14) activity, suitable for use in detergents, was detected in the alkaline culture medium of Bacillus sp. KSM-K16, which was originally isolated from soil. The enzyme, designated M protease, was purified to homogeneity from the culture broth by column chromatographies. The N-terminal amino acid sequence was Ala–Gln–Ser–Val–Pro–Trp–Gly–Ile–Ser–Arg–Val–Gln–Ala–Pro–Ala–Ala–His–Asn–Arg–Gly–Leu–Thr–Gly. The molecular mass of the protease was 28 kDa, and its isoelectric point was close to pH 10.6. Maximum activity toward casein was observed at 55 °C and at pH 12.3 in 50 mM phosphate/NaOH buffer. The activity was inhibited by phenylmethylsulfonyl fluoride and chymostatin. The enzyme was very stable in long-term incubation with liquid detergents at 40 °C. The enzyme cleaved the oxidized insulin B chain initially at Leu15–Tyr16 and efficiently at ten more sites. Among various oligopeptidyl p-nitro-anilides (pNA) tested, N-succinyl-Ala-Ala-Pro-Phe-pNA was efficiently hydrolyzed by M protease. M protease was precipitated in (NH4)2SO4-saturated acetate buffer (pH 5.0) as plank-like crystals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050437
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  • 8
    Electronic Resource
    Electronic Resource
    Purification of alkaline proteases from a Bacillus strain and their possible interrelationship (1996)
    Springer
    Applied microbiology and biotechnology 45 (1996), S. 63-71 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  Alkalophilic Bacillus sp. KSM-K16 produced three alkaline proteases, as detected by polyacrylamide gel electrophoresis (PAGE). The major protease, designated M protease, was recently purified to homogeneity and its properties were characterized. In the present study, two minor proteases, designated H protease and N protease, were purified to homogeneity from cultures of this organism. H protease had a molecular mass of 28 kDa, as estimated by sodium dodecyl sulfate/PAGE (SDS-PAGE) and its maximum activity against casein was observed at pH 11.0 and at 55°C. N protease consisted of two polypeptide chains with molecular masses of 12.5 kDa and 14.5 kDa, as estimated by SDS-PAGE, although it migrated as a single protein band during non-denaturing PAGE. Its maximum activity was observed at pH 11.0 and at 60°C. The amino-terminal sequences of H protease and of the 14.5-kDa polypeptide of N protease were identical to that of M protease. The electrophoretic relationship between the three enzymes was examined after they had been stored at different pH values and at 5°C. M protease was converted to H protease more rapidly at pH 11 than at pH 8 or below, and H protease was converted to M protease at pH 8 or below but not at pH 11. N protease appeared to be the autolytic product of the M and H proteases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050650
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  • 9
    Electronic Resource
    Electronic Resource
    Low-specificity l-threonine aldolase of Pseudomonas sp. NCIMB 10558: purification, characterization and its application to β-hydroxy-α-amino acid synthesis (1998)
    Springer
    Applied microbiology and biotechnology 49 (1998), S. 702-708 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Low-specificity l-threonine aldolase, catalyzing the reversible cleavage/condensation reaction between l-threonine/l-allo-threonine and glycine plus acetaldehyde, was purified to homogeneity from Pseudomonas sp. NCIMB 10558. The enzyme has an apparent molecular mass of approximately 145 kDa and consists of four identical subunits with a molecular mass of 38 kDa. The enzyme, requiring pyridoxal- 5′-phosphate as a coenzyme, is strictly l-specific at the α position, whereas it can not distinguish between threo and erythro forms at the β position. Besides the reversible cleavage/condensation of threonine, the enzyme also catalyzes the reversible interconversion between glycine plus various aldehydes and l-β-hydroxy-α-amino acids, including l-β-(3,4-dihydroxyphenyl)serine, l-β-(3,4-met‐hylenedioxyphenyl)serine and l-β-phenylserine, providing a new route for the industrial production of these important amino acids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530051235
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  • 10
    Electronic Resource
    Electronic Resource
    Purification and properties of an alkaline protease from alkalophilic Bacillus sp. KSM-K16 (1995)
    Springer
    Applied microbiology and biotechnology 43 (1995), S. 473-481 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Alkaline protease (EC 3.4.21.14) activity, suitable for use in detergents, was detected in the alkaline culture medium of Bacillus sp. KSM-K16, which was originally isolated from soil. The enzyme, designated M protease, was purified to homogeneity from the culture broth by column chromatographies. The N-terminal amino acid sequence was Ala-Gln-Ser-Val-Pro-Trp-Gly-Ile-Ser-Arg-Val-Gln-Ala-Pro-Ala-Ala-His-Asn-Arg-Gly-Leu-Thr-Gly. The molecular mass of the protease was 28 kDa, and its isoelectric point was close to pH 10.6. Maximum activity toward casein was observed at 55°C and at pH 12.3 in 50 mM phosphate/NaOH buffer. The activity was inhibited by phenylmethylsulfonyl flouride and chymostatin. The enzyme was very stable in long-term incubation with liquid detergents at 40°C. The enzyme cleaved the oxidized insulin B chain initially at Leu15-Tyr16 and efficiently at ten more sites. Among various oligopeptidyl p-nitro-anilides (pNA) tested, N-succinyl-Ala-Ala-Pro-Phe-pNA was efficiently hydrolyzed by M protease. M protease was precipitated in (NH4)2SO4-saturated acetate buffer (pH 5.0) as plank-like cyrstals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00218452
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