ABSTRACT
We measured the ultrashort XUV pulse width by the pump-probe method, using femtosecond dynamics of field ionization. We measured the pulse width of the ninth harmonic (88.3 nm) of a Ti:sapphire laser, using the difference of the absorption cross section between Kr and Kr(+). The change of transmission of the ninth harmonic for the delay between the pump and the probe pulses gives both the pulse width of the ninth harmonic and the recombination time of Kr(+). The measured pulse width of the ninth harmonic was 260 fs. The recombination time of Kr(+) was ~2 ps, which does not contradict the estimated time of the threebody recombination.
Subject(s)
Basidiomycota/enzymology , Glycoside Hydrolases/isolation & purification , Ammonium Sulfate , Arabinose , Chromatography, Gel , Chromatography, Ion Exchange , Culture Media , Drug Stability , Electrophoresis, Disc , Hot Temperature , Hydrogen-Ion Concentration , Kinetics , Methods , Polysaccharides , UltracentrifugationABSTRACT
When Corticium rolfsii is grown under aerobic conditions in a medium containing one of several simple sugars or polysaccharides, it release alpha-L-arabinofuranosidase into the culture fluid. Araban and bran extract were found to be the most effective carbon sources in stimulating the production of the enzyme. Pectin and arabinose stimulated the production of the enzyme to a lesser degree, whereas xylose, glucose, galactose, and sucrose caused the formation of a relatively small amount of alpha-L-arabinofuranosidase. alpha-L-Arabinofuranosidase was demonstrated by its ability to hydrolyze phenyl-alpha-L-arabinofuranoside, araban, and arabinoxylan. The pH optimum of the enzyme was 2.5. At pH values of 2 to 9, the enzyme lost less than 15% of its activity during a 72-hr period at 2 C. At 70 C, its stability was greatest at pH values of 4 to 6.
