Titlebook: Biotechnology for Fuels and Chemicals; The Twenty-Ninth Sym William S. Adney,James D. McMillan,K. Thomas Klass Conference proceedings 2008

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Effects of Gene Orientation and Use of Multiple Promoters on the Expression of , and , in ,ffect of gene orientation. To test the possible dilution of promoter strength due to multiple use of the same promoter, we examined the level of expression of . driven by either the . or . promoter when carried on a single copy plasmid. We then coexpressed . from either a single or multicopy plasmid

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Bioreactors for H2 Production by Purple Nonsulfur Bacteriawas observed for more than 8 months. The bubble-train bioreactor was built using polyvinyl chloride (PVC) tubing, wound helically on a vertical cylindrical supporting structure. Small bubbles containing CO were injected continuously through a needle/septum connection from the gas reservoir (20% CO).

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Solid-state Fermentation of Xylanase from , in a Multi-layer-packed Bed Reactorty is obtained after 7 days of fermentation and attains 10,200 U/g of soya oil cake. These levels are higher than those presented in the literature and, therefore, show all the potentialities of this stock and this technique for the production of xylanase.

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Effects of pH and Temperature on Recombinant Manganese Peroxidase Production and StabilityCultivation of . mycelia in stationary flasks for production of heme peroxidases is commonly conducted at low pH (pH 4.2). However, shake flask and fed-batch fermentation experiments with . αMnP1-1 demonstrated that rMnP production is highest at pH 6, with rMnP concentrations in the medium declining

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Xylanase Production by , D1 Using Maltose as Carbon Sourcely). Unlike that observed in the xylan medium, glucose repressed xylanase production in the maltose medium, leading to a reduction of 55% on the enzyme production at 24 h of cultivation. Xylose, at 1.0 g/L, induced xylanase production on the maltose medium. On this medium, the repressive effect of x

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Immobilization of , Lipase—A Comparison of Stability of Physical Adsorption and Covalent Attachment immobilization by covalent attachment led to complete enzyme inactivation. Thermal deactivation was studied at a temperature range from 25 to 45°C and pH varying from 5.0 to 9.0 and revealed that the hydrophobic adsorption on octadecyl-sepabeads produced an appreciable stabilization of the biocataly