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                     Enzymatic modifi cation of polyacrylonitrile and
                               cellulose acetate fi bres for textile and
                                                         other applications


                                      T. MATAMÁ and A. CAVACO-PAULO,
                                                    University of Minho, Portugal



                     Abstract: The enzymatic reactions that lead to the creation of
                     hydrophilic groups at the surface of polyacrylonitrile and cellulose
                     acetate are reviewed and the main advantages and drawbacks are briefl y
                     discussed. New materials with distinct surface properties can be achieved
                     using eco-friendly catalysts that preserve the desirable bulk properties of
                     polyacrylonitrile and cellulose acetate.

                     Key words: biomodification, polymer side chains, biotechnology,
                     polyacrylonitrile, nitrilase, acetyl esterase, cellulose acetate.





              5.1    Introduction

              In the textile industry, the impact of biotechnology has been observed at
              three main levels: the introduction of enzymes in manufacturing wet pro-
              cesses and laundry detergents, the design of new and biodegradable fi bres
              and the treatment of textile effl uents.
                Biocatalysis is present in some of the oldest transformations known to
              humans: descriptions of various beer recipes were found in Sumerian writ-
              ings (Ball, 2001). Studies on fermentation processes led to a ‘big bang’ in
              the knowledge of life’s chemistry. In the 19th century, Louis Pasteur came
              to the conclusion that the fermentation of sugar to alcohol by yeast was
              catalyzed by a vital force contained within the yeast cells called ‘ferments’,
              which were thought to function only within living organisms.  Wilhelm

              Kühne was the first to use the term ‘enzyme’ and, years later, Emil Fisher
              proposed the ‘Lock and Key Model’ to visualize the substrate and enzyme
              interaction (Cabral et al., 2003).
                Enzymes are the subgroup of proteins that catalyse the chemistry of life,
              transforming both macromolecules and small molecules; they are the focus
              of current biocatalysis research (Walsh, 2001). The chiral nature of enzymes
              results in a remarkable chemical precision seen as different types of selec-
              tivity, even in the absence of functional-group protection (Rozzell, 1999;

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