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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 44 (1995), S. 81-87 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract New thermostable enzyme activities of seven Thermus strains were compared using the API ZYM system. All the strains exhibited high levels of α- and β-glycosidases, esterase (C4) and esterase-lipase (C8) activities intracellularly. Only T. thermophilus HB8 (ATCC 27634) showed α-glucosidase and esterase activities in the supernatant. According to the intensity of β-galactosidase activity, Thermus strains were divided in three groups. Group 0, which showed a weak β-galactosidase activity, included Thermus spp. ATCC 31674 (T351) and 27978 (X-1) as well as T. thermophilus ATCC 27634 (HB8). Group I which consisted of T. aquaticus ATCC 25104 (YT-1), ATCC 25105 (Y-VII-51B) and Thermus sp. ATCC 27737 (T2), had a specific activity of approximately 40.0 U mg−1 and galactose as inducer. T. aquaticus ATCC 31558 (group 2) was particularly effective for β-galactosidase production (2840 U) with a specific activity of 98 U mg−1. For each strain, galactose (0.5%) was a better inducer of β-galactosidase production than lactose (1%). The detection of β-galactosidase activity was dependent on the derivative chromogenic substrates used (naphthyl or nitrophenol coupled to sugar). Oligosaccharides were synthesized from cellobiose, lactulose, maltose or lactose as substrates at high temperature in some strains of Thermus.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 44 (1995), S. 81-87 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  New thermostable enzyme activities of seven Thermus strains were compared using the API ZYM system. All the strains exhibited high levels of α- and β-glycosidases, esterase (C4) and esterase-lipase (C8) activities intracellularly. Only T. thermophilus HB8 (ATCC 27634) showed α-glucosidase and esterase activities in the supernatant. According to the intensity of β-galactosidase activity, Thermus strains were divided in three groups. Group 0, which showed a weak β-galactosidase activity, included Thermus spp. ATCC 31674 (T351) and 27978 (X-1) as well as T. thermophilus ATCC 27634 (HB8). Group I which consisted of T. aquaticus ATCC 25104 (YT-1), ATCC 25105 (Y-VII-51B) and Thermus sp. ATCC 27737 (T2), had a specific activity of approximately 40.0 U mg-1 and galactose as inducer. T. aquaticus ATCC 31558 (group 2) was particularly effective for β-galactosidase production (2840 U) with a specific activity of 98 U mg-1. For each strain, galactose (0.5%) was a better inducer of β-galactosidase production than lactose (1%). The detection of β-galactosidase activity was dependent on the derivative chromogenic substrates used (naphthyl or nitrophenol coupled to sugar). Oligosaccharides were synthesized from cellobiose, lactulose, maltose or lactose as substrates at high temperature in some strains of Thermus.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Stamford, Conn. [u.a.] : Wiley-Blackwell
    Polymer Engineering and Science 13 (1973), S. 102-112 
    ISSN: 0032-3888
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Filling cold mold cavities with hot polymer melts at high pressures is of great practical interest. The transport approach to this process of solving the general equations of change with suitable equations of state to describe the flowing material has been largely ignored. No analytic solution is possible, and the non-steady state flow adds a dimension which makes digital computation discouraging because of the core storage and execution time requirements.The mold filled in this simulation is a disk which hot polymer melt enters through a tubular entrance located at the center of the top plate. The tube is 2.54 cm. long and has a radius of 0.24 cm. The plate separation and outer radius of the disk cavity may be varied. A constant pressure applied at the entrance of the tube causes the flow. The cavity walls are kept at various low temperatures. The reported results are for rigid polyvinyl chloride (PVC).The general transport equations, i.e. continuity, momentum, and energy, for a constant density power law fluid are used to solve the flow problem. Convergence to the differential solutions is guaranteed but since a lower limit was imposed on the time increment by the core storage limit of the computer facilities (27K) and long execution times, all results are semiquantitative for the problem as stated.Using the results obtained it is possible to predict “fill times”. The formation of a frozen polymer skin as the cavity fills may be followed via the velocity profiles. The temperature profiles which reflect cooling and the amount of viscous heat generated provide the basis for studying resin thermal degradation effects.Finally, because so much of the total pressure drop is disispated in the entrance tube, and so much viscous heat is generated there, this study indicates that the design of the gate and runner system is perhaps the most important facet of success in mold filling.
    Additional Material: 14 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Biotechnology techniques 9 (1995), S. 601-606 
    ISSN: 1573-6784
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary β-galactosidases of Thermus aquaticus YT-1, exhibiting a galactosyl transferase activity, were immobilized using different techniques. Entrapment in agarose or gellan gum beads was unsuitable for enzyme immobilization due to enzyme leakage. A technique that efficiently immobilized the enzymes was developed using glutaraldehyde co-crosslinking of β-galactosidases with bovine serum albumin, followed by entrapment in agarose beads.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Biotechnology letters 17 (1995), S. 1077-1080 
    ISSN: 1573-6776
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Galactooligosaccharides (GalOS) production from a lactose solution (16% w/v) was studied at 70°C, pH 4.6 and 6.0 with free or immobilized β-galactosidases of Thermus aquaticus YT-1. Synthesis of OS and lactose conversion was significantly improved when using the immobilized preparation. At pH 4.6, OS accounted for approx. 35% of the total carbohydrates with a conversion rate of lactose of 80%. The general formula of OS synthesized in this way was Gal-(Gal)n-Glu with n being equal to 1 or 2 and a β anomeric configuration of the D-galactosyl moiety.
    Type of Medium: Electronic Resource
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