3 research outputs found

    A perspective on the economic valorization of gene manipulated biotechnology: Past and future

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    Three distinct fields of gene manipulated biotechnology have so far been economically exploited: medical biotechnology, plant biotechnology and industrial biotechnology. This article analyzes the economic evolution and its drivers in the three fields over the past decades, highlighting strong divergences. Product and market characteristics, affecting firms’ financing options, are shown to be important enablers or inhibitors. Subsequently, the lack of commercialization in a fourth type of gene manipulated biotechnology, namely environmental biotechnology, is explained by the existence of strong barriers. Given the latter’s great promises for environmental sustainability, we argue for a need to push the commercial valorization of environmental biotechnology. Our research has strong implications for (technology) management research in biotechnology, pointing to a need to control for and/or distinguish between different biotechnology fields

    Influence of physical properties of cuvette surface on measurement of serum lipase

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    Background: Despite striking similarities among colorimetric lipase assay recipes, marked intervendor differences are noted in the reported lipase values. In the present study, the effect of physical properties of the cuvette surface on measurement of serum lipase was investigated. Methods: Lipase activity was measured concomitantly in cuvettes from three different analyzers: Vista (Siemens), Modular (Roche), and Synchron (Beckman Coulter). The surface/volume ratio of the cuvettes and the contact angle of the cuvette polymers were determined. The effects of various characteristics of serum (biochemical parameters, surface tension) were also examined. Results: Serum lipase activities based on the colorimetric methylresorufin assay differed markedly according to the cuvettes used. More specifically, in the lower activity rate, marked differences were reported. The physical properties of the various cuvettes showed remarkable differences, especially in the contact angles. Other biochemical parameters (bilirubin, alkaline phosphatase, total cholesterol, high-density lipoprotein cholesterol, low-density lipoprotein cholesterol, and triglycerides) and serum surface tension did not affect the results. Conclusions: Serum lipase activity is affected by the physical properties of the cuvette surface

    Isolation and characterisation of an equol-producing mixed microbial culture from a human faecal sample and its activity under gastrointestinal conditions

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    Only about one third of humans possess a microbiota capable of transforming the dietary isoflavone daidzein into equol. Little is known about the dietary and physiological factors determining this ecological feature. In this study, the in vitro metabolism of daidzein by faecal samples from four human individuals was investigated. One culture produced the metabolites dihydrodaidzein and O-desmethylangolensin, another produced dihydrodaidzein and equol. From the latter, a stable and transferable mixed culture transforming daidzein into equol was obtained. Molecular fingerprinting analysis (denaturing gradient gel electrophoresis) showed the presence of four bacterial species of which only the first three strains could be brought into pure culture. These strains were identified as Lactobacillus mucosae EPI2, Enterococcus faecium EPI1 and Finegoldia magna EPI3, and did not produce equol in pure culture. The fourth species was tentatively identified as Veillonella sp strain EP. It was found that hydrogen gas in particular, but also butyrate and propionate, which are all colonic fermentation products from poorly digestible carbohydrates, stimulated equol production by the mixed culture. However, when fructo-oligosaccharides were added, equol production was inhibited. Furthermore, the equol-producing capacity of the isolated culture was maintained upon its addition to a faecal culture originating from a non-equol-producing individual
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