Now showing items 6-10 of 47

  • A cell-associated oligo-1,6-alpha-glucosidase from an extremely thermophilic anaerobic bacterium, Thermoanaerobium Tok6-B1.

    Plant, Adrian R.; Parratt, S.; Daniel, Roy M.; Morgan, Hugh W. (1988)
    Cell-associated oligo-1,6-alpha-glucosidase (EC was isolated from Thermoanaerobium Tok6-B1 grown on starch-containing medium. Activity was purified 11.4-fold by salt precipitation, gel filtration, hydroxyapatite ...
  • The cellulase activity of an extreme thermophile

    Hudson, J. Andrew; Morgan, Hugh W.; Daniel, Roy M. (Springer, 1991)
    The carboxymethylcellulase activity concentrated from the extremely thermophilic anaerobe H173 was found to have a pH optimum of 6.5–7.0. The enzyme activity was stabilised by the addition of dithiothreitol and CaCl₂•2H₂O ...
  • Cellulases from extremely thermophilic bacteria

    Sharrock, Keith R.; Sissons, Christopher H.; Daniel, Roy M.; Morgan, Hugh W. (New Zealand Institute of Chemistry, 1983)
    Cellulose is the most abundant biopolymer on earth, and is the major component of urban waste. Thus cellulose must be seen as a very significant renewable source of chemical foodstocks when fossil fuels become restricted.
  • Cellulolytic properties of an extremely thermophilic anaerobe

    Hudson, J. Andrew; Morgan, Hugh W.; Daniel, Roy M. (Elsevier, 1990)
    An extremely thermophilic anaerobe was isolated from a New Zealand hot spring by incubating bacterial mat strands in a medium containing xylan. The Gramreaction-negative organism that was subsequently purified had a ...
  • The characterisation of a thermostable endo-β-1,4-mannanase cloned from “Caldocellum saccharolyticum”

    Bicho, Paul A.; Clark, Tom A.; Mackie, Keith; Morgan, Hugh W.; Daniel, Roy M. (Springer, 1991)
    An endo-gb-1,4-mannanase cloned from caldocellum saccharolyticum and expressed in Escherichia coli was partially purified. The purification involved heat treatment, anion exchange and gel filtration. The mannanase was ...