Learn More
Nitrile hydratase of Pseudomonas chlororaphis B23 was completely stabilized by the addition of 22 mM n-butyric acid. The enzyme was purified from extracts of methacrylamide-induced cells of P. chlororaphis B23 in eight steps. At the last step, the enzyme was crystallized by adding ammonium sulfate. The crystallized enzyme appeared to be homogeneous from(More)
Nitrile hydratase was purified and crystallized from the crude extract of Brevibacterium R312 and found to be homogeneous by the results of disc gel electrophoresis, analytical ultracentrifuge and double diffusion in agarose. The enzyme has a molecular mass of about 85,000 Da and contains approximately 3 g atoms iron/mol enzyme. The enzyme was composed of(More)
In this paper an explanation is given of howPseudomonas (P.) chlororaphis B23 can accumulate so much acrylamide of such high purity. One reason is thatP. chlororaphis B23 exhibits much greater nitrile hydratase activity than amidase activity; the rate of formation of acrylamide through the nitrile hydratase reaction is at least 4000 times higher than its(More)
We studied the antibacterial effect of Hinokitiol against Staphylococcus aureus. As reference, we studied also the antibacterial effects of the oil and water from Thujopsis dolablata var. hondai Makino which contains Hinokitiol an important element of its antibacterial effect. Interestingly, Hinokitiol showed the double zone phenomenon, i.e., minimum(More)
  • 1