15 research outputs found

    Supercritical water gasification of microalgae: The impact of the algal growth water

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    This is the final version. Available on open access from Elsevier via the DOI in this recordData availability: Data will be made available on request.Investigation into the supercritical water gasification (SCWG) of microalgae has largely used deionized water as the reaction medium. However, real systems would use the algal growth water directly, containing ions that have been known to catalyse SCWG (K+, Na+, OH-, Fe3+, Cl-). Investigation into the effect of the growth water on SCWG was carried out for a range of temperatures (450–550), biomass concentrations (1–3wt%) and catalysts (KOH, Ru/C), using glucose or Chlorella vulgaris as the feedstock was performed. A significant increase in CO2 and reduction in CO content in the gas was observed without a catalyst and with a Ru/C catalyst. An increase in char/tar was also observed without a catalyst. As a result, the impact of the growth water should be considered for the SCWG of microalgae, in laboratory experiments and the selection of algal growth media in industrial applications.Engineering and Physical Sciences Research Council (EPSRC

    Enhancement of lipase activity in non-aqueous media upon immobilization on multi-walled carbon nanotubes

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    <p>Abstract</p> <p>Background</p> <p>Immobilization of biologically active proteins on nanosized surfaces is a key process in bionanofabrication. Carbon nanotubes with their high surface areas, as well as useful electronic, thermal and mechanical properties, constitute important building blocks in the fabrication of novel functional materials.</p> <p>Results</p> <p>Lipases from <it>Candida rugosa </it>(CRL) were found to be adsorbed on the multiwalled carbon nanotubes with very high retention of their biological activity (97%). The immobilized biocatalyst showed 2.2- and 14-fold increases in the initial rates of transesterification activity in nearly anhydrous hexane and water immiscible ionic liquid [Bmim] [PF6] respectively, as compared to the lyophilized powdered enzyme. It is presumed that the interaction with the hydrophobic surface of the nanotubes resulted in conformational changes leading to the 'open lid' structure of CRL. The immobilized enzyme was found to give 64% conversion over 24 h (as opposed to 14% with free enzyme) in the formation of butylbutyrate in nearly anhydrous hexane. Similarly, with ionic liquid [Bmim] [PF6], the immobilized enzyme allowed 71% conversion as compared to 16% with the free enzyme. The immobilized lipase also showed high enantioselectivity as determined by kinetic resolution of (±) 1-phenylethanol in [Bmim] [PF6]. While free CRL gave only 5% conversion after 36 h, the immobilized enzyme resulted in 37% conversion with > 99% enantiomeric excess. TEM studies on the immobilized biocatalyst showed that the enzyme is attached to the multiwalled nanotubes.</p> <p>Conclusion</p> <p>Successful immobilization of enzymes on nanosized carriers could pave the way for reduced reactor volumes required for biotransformations, as well as having a use in the construction of miniaturized biosensensor devices.</p
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