The production of tyrosinase by Streptomyces antibioticus (p1J7O2) was investigated as a model system for recombinant protein production by Streptomyces. Product deactivation was found to have a severe effect on the levels of tyrosinase obtained. Tyrosinase deactivation was detected during all phases of batch cultures, with higher specific deactivation rates observed during the stationary phase. The specific deactivation rate exhibited an Arrhenius dependence on temperature, with approximately a twofold increase in the deactivation rate between 25 degrees C and 30 degrees C. The effect of deactivation on the determination of tyrosinase production kinetics is discussed. A strategy was implemented to increase tyrosinase productivity by enriching the growth medium and reducing the culture temperature during the period of maximum tyrosinase production. This strategy resulted in a shorter culture time and a 2.5-fold increase in tyrosinase activity compared to a culture grown at 25 degrees C using a standard growth medium.
An investigation was undertaken to determine the effect of short range barriers of two different strengths on the thermally activated motion of a dislocation through a random array of these barriers. The values of the activation energies and activation volumes indicate that there is synergistic affect, i.e. a coupling effect, between the strong and weak barriers. It was observed that the activation energy is not a mean value of the activation energy associated with the strong and weak barriers, but is larger than that associated with the strong barrier. The stress required to maintain a given average velocity also indicates that there is a synergistic effect between the strong and weak barriers.
Techniques are reviewed for the identification and enrichment of fimbriae-positive and fimbriae-negative Escherichia coli. Fimbriae-positive E. coli were observed to form a semistable suspension of pH 7.0 which settled at a rate much slower than the fimbriae-negative bacteria. Intense autoflocculation of fimbriae-positive E. coli was noted at pH values below 5.2.
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