Page 422 - Elements of Chemical Reaction Engineering Ebook
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Sec. 7.5   Bioreactors                                         393


                                              glucose(Sr)  ( G.O*(Eo)      (H,O,(P,)
                                               6-lactone(P,)   G.O.H,(Er)    O,(S,)

                                Derivation of the rate laws for this reaction sequence is given on the CD-R.OM.

                                Enzyme Cofactors.  In many enzymatic reactions, and in particular biological
                                reactions, a second substrate (i.e., species) must be introduced to activate the
                                enzyme. This substrate, which is referred to  as  a cofactor or coenzyme  even
                                though it is not. an enzyme as such, attaches to the enzyme and is most (often
                                either reduced or oxidized during the course of the reaction. The enzyme-cofac-
                                tor  complex  is  referred  to  as  a  holoenzyme.  The  inactive  form  of‘  the
                                enzynne-cofactor complex for a specific reaction and reaction direction is called
                                an apoenzyme. An  example of the type of  system in which a cofactor is used is
                                the formation of ethanol from acetaldehyde in the presence of the enzyme alco-
                                hol dehydrogenase (ADH) and the cofactor nicotinamide adenine dinucleotide
                                (NAD):
                                                         alcohol dehydrogenase
                                                      ethanol (PI) IC..
                                                 acetaldehyde (S 1)     NADH (S,)


                                                                        NAD+
                                                                              (S;)
                                Derivation of the rate laws for this reaction sequence is given on the CD-E!OM.

                                7.5  Bioreactors

                                Because enzymatic reactions are involved in the growth of microorganisms, we
                                now  proceed to  study microbial growth and bioreactors. Not  surprisingly, the
                                Monod equation, which describes the growth law for a number of  bacteria, is
                                similar to the Michaelis-Menton equation. Consequently, even though bioreac-
                                tors  are not  truly  homogeneous because  of  the presence of  living cells,  we
                                include them in this chapter as a logical progression from enzymatic reactiions.
                                     The  use  of  living  cells  to  produce  marketable  chemical  products  is
                                becorning  increasingly important. By  the  year  2000,  chemicals,  agricultural
                                products, and food pro  cts produced by biosynthesis will have risen from the
                                                    ‘llion
                    The growth of   1990 market of $275 2 to around $17 bi1li0n.l~ Both microorganisms and
                     bio@chnologY   mammalian cells are being used to produce a variety of products, such as insu-
                                 lin, most antibiotics, and polymers. It is expected that in the future a number
                                 of  organic chemicals currently derived  from petroleum will  be produced by
                                 living cells. ‘The advantages of  bioconversions  are mild  reaction  conditions,
                                 high yields (e.g., 100% conversion of glucose to gluconic acid with Aspergillus
                                 niger), that  organisms contain several  enzymes that  can  catalyze  successive
                                 steps in  a reaction,  and  most  important, that  organisms act  as stereospecific
                                             -
                                 l5  Frontiers  in  Chemical  Engineering, National  Academy  Press,  Washington,  D.C.,
                                   1988.
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