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  • discrete-parameter Markov processes  (1)
  • xylanase  (1)
  • 1995-1999  (2)
  • 1985-1989
  • 1995  (2)
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  • 1995-1999  (2)
  • 1985-1989
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  • 1995  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of theoretical probability 8 (1995), S. 417-432 
    ISSN: 1572-9230
    Keywords: Discrete-parameter martingales ; discrete-parameter Markov processes ; Hermite polynomials
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Notes: Abstract We investigate, for a given martingaleM={M n: n≥0}, the conditions for the existence of polynomialsP(·,·) of two variables, “time” and “space,” and of arbitrary degree in the latter, such that{P(n, M n)} is a martingale for the natural filtration ofM. Denoting by ℘ the vector space of all such polynomials, we ask, in particular, when such a sequence can be chosen so as to span ℘. A complete necessary and sufficient condition is obtained in the case whenM has independent increments. For generalM, we obtain a necessary condition which entails, under mild additional hypotheses, thatM is necessarily Markovian. Considering a slightly more general class of polynomials than ℘ we obtain necessary and sufficient conditions in the case of general martingales also. It is moreover observed that in most of the cases, the set ℘ determines the law of the martingale in a certain sense.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    World journal of microbiology and biotechnology 11 (1995), S. 359-360 
    ISSN: 1573-0972
    Keywords: α-L-Arabino furanosidase ; Termitomyces clypeatus ; xylanase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Termitomyces clypeatus produced xylanase and α-L-arabinofuranosidase simultaneously in various media. The arabinofuranosidase had pH and temperature optima of 5.5 and 50°C, respectively, and was stable at 50°C for 30 min and at pH values from 2 to 5. The partially purified enzyme was distinct from xylanase present in the same medium.
    Type of Medium: Electronic Resource
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