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'Bioconversion' in keywords Facet   section ZfN Section C  [X]
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1994 (1)
1986 (1)
1Author    Dagmar Busmann, RalfG. Ünter BergerRequires cookie*
 Title    Oxyfunctionalization o f a-and ß-Pinene by Selected Basidiomycetes  
 Abstract    Several strains of basidiom ycetes were examined for their ability to transform a-and ß-pinene in agitated submerged cultures. Four major metabolites of a-pinene (verbenol, ver-benone, myrtenol, and rrorcs-pinocarveol) and three main metabolites of ß-pinene (1,4-cineol, myrtenol, and rrarcs-pinocarveol) were isolated from the fermentation broth. The metabolic pathways included allylic oxidation, oxidative cleavage and further regioselective oxidation. G anoderm a applanatum was found to carry out the stereoselective allylic hydroxylation of a-pinene to verbenol, and o f ß-pinene to trans-pinocarveol in trans position to the C -C bridge. The optimal conditions of the bioreaction were established with respect to substrate concentration, incubation time and conversion time. D ue to growth inhibition caused by elevated substrate concentration, the bioconversion of ß-pinene required pre-grown cultures. Generally, mycelial pellet cultures were supplemented with the terpene substrate when a residual glucose content of 50% was reached. Depending on strain this point was reached after about 48 h. A n incubation period of two to three days gave best yields. The transient accumulation of oxygenated products apparently reflected different reaction velocities of the successive catabolic steps. 
  Reference    Z. Naturforsch. 49c, 545 (1994); received May 26/June 20 1994 
  Published    1994 
  Keywords    Pinene, Cineol, Basidiomycetes, Bioconversion, Transformation 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0545.pdf 
 Identifier    ZNC-1994-49c-0545 
 Volume    49 
2Author    Hans-Jürgen Schuetz, H. Elm, Ut SimonRequires cookie*
 Title    Degradation of NAD(H ) by Endogenous Enzymes of Yeasts and Clostridia  
 Abstract    The time courses of degradation of exogenous NAD and NADH (2.5 m M) catalyzed by en­ dogenous enzymes present in Saccharom yces cerevisiae, Candida utilis, Clostridium spec. La 1, C lostridium kluyveri, and Clostridium sporogenes have been determined. The half lives of the pyridine nucleotides depend extremely on the organism and, for the same organism, on the growth conditions. C. spec. La 1 as well as C. kluyveri possess only negligible enzyme activities for NAD degradation. However, C. sporogenes shows activities leading to half lives of less than 2 h for NAD and 5 h for NADH. At 25 °C half lives in the order of 5 — 17 h have been observed for Candida utilis under different conditions. The half lives of NAD are roughly 5 times higher in the presence of Saccharom yces cerevisiae. 
  Reference    Z. Naturforsch. 41c, 172—178 (1986); received July 25. 1985 
  Published    1986 
  Keywords    NAD(H) Degradation, Clostridia, Yeasts, Bioconversion, Enzymatic Reductions 
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 TEI-XML for    default:Reihe_C/41/ZNC-1986-41c-0172.pdf 
 Identifier    ZNC-1986-41c-0172 
 Volume    41