h1

% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@PHDTHESIS{Trivedi:62092,
      author       = {Trivedi, Archana Harendra},
      othercontributors = {Büchs, Jochen},
      title        = {{D}evelopment of immobilization and drying methods of
                      enzymes on support particles for enzymatic gas-phase
                      reactions},
      address      = {Aachen},
      publisher    = {Publikationsserver der RWTH Aachen University},
      reportid     = {RWTH-CONV-123686},
      pages        = {XV, 109 S. : Ill., graph. Darst.},
      year         = {2005},
      note         = {Aachen, Techn. Hochsch., Diss., 2005},
      abstract     = {In this research work, two mesophilic alcohol
                      dehydrogenases namely baker’s yeast alcohol dehydrogenase
                      (YADH) and Lactobacillus brevis alcohol dehydrogenase
                      (LBADH) and one thermophilic alcohol dehydrogenase namely
                      Thermoanaerobacter species alcohol dehydrogenase (ADH T)
                      were immobilized by physical adsorption method. The effects
                      of various immobilization and drying process parameters on
                      the residual activity and the protein loading of the
                      immobilized enzyme preparation were studied and thereby
                      different optimum preparations were observed for different
                      enzymes. Under the optimum immobilization conditions the
                      residual activity achieved with YADH, LBADH, and ADH T was
                      about $80\%,$ $316\%,$ and $325\%,$ respectively. The
                      hypothesis of bubble nucleation as a cause for loss of
                      enzyme activity during the low pressure drying process was
                      verified. The effects of various gas-phase reaction
                      conditions on the initial reaction rate and the half-life of
                      the optimized preparations were also studied. It was
                      observed that addition of a suitable buffer (50 mM phosphate
                      buffer, pH 7) or an optimum amount of sucrose (5 times
                      greater than the amount of protein on weight basis) during
                      the enzyme immobilization enhanced the half-life of the
                      immobilized enzymes in the gas-phase reaction. Water
                      activity significantly influenced the initial reaction rate
                      and the half-life of the immobilized enzyme preparations in
                      the gas-phase reaction. The optimum water activity found for
                      LBADH and ADH T was the same (0.55). Under the optimized
                      immobilization and gas-phase reaction conditions the
                      thermo-stability of the ADH enzymes was enhanced
                      tremendously. The space-time yield of (R)-phenylethanol was
                      about 1000 g l-1 d-1 with LBADH and the space-time yield of
                      (S)-phenylethanol was about 600 g l-1 d-1 with ADH T. The
                      total turn over number of LBADH was about and the same of
                      ADH T was about.},
      keywords     = {Alkoholdehydrogenasen (SWD) / Immobilisierung (SWD) /
                      Trocknung (SWD) / Alkohole (SWD) / Herstellung (SWD) /
                      Gasphasenreaktion (SWD) / Enantioselektivität (SWD) /
                      Enzymkatalyse (SWD)},
      cin          = {416510},
      ddc          = {660},
      cid          = {$I:(DE-82)416510_20140620$},
      typ          = {PUB:(DE-HGF)11},
      urn          = {urn:nbn:de:hbz:82-20050864},
      url          = {https://publications.rwth-aachen.de/record/62092},
}