@misc{Sroga_Grażyna_E._Glutathione_2002,
 author={Sroga, Grażyna E.},
 volume={58},
 number={3},
 copyright={Creative Commons Attribution BY-SA 4.0 license},
 journal={Biotechnologia, vol.58, 3 (2002)-.},
 howpublished={online},
 year={2002},
 publisher={Committee on Biotechnology PAS},
 publisher={Institute of Bioorganic Chemistry PAS},
 language={pol},
 abstract={Research of the past decade has demonstrated that the use of enzymes andwhole-cell biocatalysts is environmentally friendly, economical and surprisingly,faces few barriers when applied in organic syntheses. In nature, enzymesevolved to function within a living system and may not exhibit features desirable for large-scale in vitro syntheses. Thus, protein engineering has the potential to dramatically enhance enzyme performance in a wide variety of unusual -but technologically important - environments. Site-directed, cassette-mutagenesis and construction of chimeric enzymes commonly used in rational protein engineering are important strategies which reveal the structure-functionrelationship of a given enzyme. Notably, construction of hybrid enzymes has become increasingly important in the rational design of novel biocatalysts withdesired properties and activities. However, “irrational” protein design based onrandom mutagenesis technologies or the combination with directed evolutionapproaches has truly revolutionized the generation offunctional biological molecules.},
 title={Glutathione Transferases and Serine Proteases: From Probing Mechanism of Enzyme Catalysis by Rational Protein Engineering to Evolutionary Design of Enzyme Function},
 type={Text},
 URL={http://www.rcin.org.pl/Content/137870/PDF/POZN271_172999_biotechnologia-2002-no3-sroga.pdf},
 keywords={biotechnology},
}