earticle

영어

Biocatalysis is the use of natural catalysts, such as protein enzymes, to perform chemical transformations on organic compounds. In recent years, industry and academia has been interested in biocatalysis because of the advantageous characteristics of enzymes as catalysts [1]. Also, biocatalysis is applied nowadays in various processes, including the production of bulk and fine chemicals [2-3]. In spite of these, enzymes do not always show satisfying performance in terms of activity, stability and most importantly enantioselectivity, and also many classes of substrates can still not be efficiently converted. Esterase Est25 is currently considered as a biocatalyst for the production of a commercially valuable (S)- ketoprofen. Here, we have studied the predicted structure model of Est25 to find important amino acids that can enhance the enantioselectivity. Mutant L255W of Est25 showed most significant enantioselectivity enhancement (up to 80%). In addition to, we added some mutations to mutant L255W and the enantioselectivity of these mutants is enhanced. Substrate of Est25 is ketoprofen ethyl ester that has two benzene rings in R- and S-form. These various mutations have different hydrophobicity and size, may affect the approach to enzyme active site and the location of racemic-ketoprofen ethyl ester.