Uutta biotekniikkaa luonnonvarojen hyödyntämiseksi: VTT Teollinen biotekniikka -ohjelma soveltaa luonnon omaa kemiaa ihmisen ja ympäristön parhaaksi

H. Söderlund, S. Keränen, Merja Penttilä, Laura Ruohonen, Kristiina Takkinen, L. Viikari

    Research output: Contribution to journalArticleProfessional


    Enzymes, the catalysts of living systems, direct and control the biochemical reactions of all organisms. What kinds of enzymes an organism can produce is controlled by its genes. Over billions of years of evolution, the set of enzymes an organism carries has been optimized for the survival of that organism. The number of chemical reactions carried out by enzymes is enormous. One of the major challenges in biotechnology today is to exploit enzymes in industrial processes. In most cases, enzymes perform the same catalytic processes in isolated form as in the living organism, and many of these reactions are of industrial value. Nevertheless, evolution has not designed enzymes for industrial processes. Thus, application of novel methods of molecular biology, directed evolution and site-specific mutagenesis, can be helpful in "improving" enzyme performance. Complex chains of reactions such as those occurring in metabolic pathways are often impossible to perform with isolated enzymes. It is possible, however, to control the metabolism of microbes, for example, with the aid of metabolic pathway engineering - a toolset including genetical and physiological methods. The aim of VTT's research programme Industrial Biotechnology is to use advanced enzyme technology and metabolic pathway engineering for industrial applications with specific emphasis on the utilization of renewable natural resources. The specific subtopics are molecular recognition, protein production, enzyme technology and metabolic pathway engineering. These areas are briefly described in this article.

    Original languageFinnish
    Pages (from-to)158-164
    Number of pages7
    Issue number3
    Publication statusPublished - 1 Jan 2001
    MoE publication typeD1 Article in a trade journal

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