TABLE 10.1 Typical Osygen Upeake Rates in Different Cell Cultures ‘Maximum Maximum Maximum specific oxygen specific volumetric uptake nite, 40 oxygen uptake (mmol g* dry rate, Qo Type of cell culture Carbon source __weighth7?) (exmol “Reference MICROBIAL Aerobacter aerogenes Peptone 32xW" 74 tol Aspergillus niger Glucose 16 88 va Bacillus subtilis Peptone 15x 107% 1 Beneclew ntregens ePropanl 2 60 pI Escherichia cli Peptone saxw" 50 tol Peniciliom cirysogemum Lactose 2 30 ho Saccharomyes cerevisiae Ethanol 0 0 no Streptomyces aurojaciens Corn starch 70 10 nay Streptomyces ceelnlor Glucose 74 55 ns} Streptomyces griseus Meat extract 4 6 nay Xerhomonas campestris Glucose 45 n ns} PLANT Catharanthus roseus Sucrose 04s 27 isl Nicoti talncum Sucrose 090 wo na ANIMAL Chinese hamster evary Glucose /glutamine 29x10" 060 hs} (CHO Hybridoma Glucose/glutamine 29x10 057 ng)TABLE 10.2 Solubility of Oxygen in Water under 1 atm Air Pressure ‘Oxygen solubility under Henry's constant ‘Temperature (°C) ‘atm air pressure (kg m *) (m? atm gmol*) 0 148x107 0.454 10 1.15 107 0.582 15 1.0410 0.646 » 9.45 10° 0.710 3B 869x 10> O74 26 855x10> 0.787 7 842x10° 0.797 2B 8.29 10° 0.810 2» 817x10° 0.822 x” 805x107 0.835 6 7.52 10° 0.893 7.07% 10° 0.950 Calculated from data in international Critical Tables, 1928, vol. II, McGraw-Hill, New York, p. 257. TABLE 10.3 Solubility of Oxygen in Aqueous Solutions at 25°C under 1 atm Oxygen Pressure ‘Oxygen solubility at 25°C under 1 atm oxygen pressure (kg m~ Concentration (M) HCL % H,SOy NaCl ° 414x107 44x 107 414x107 05 387x107 377x107 343x107 10 375x107 3.60 x 107 291x107 350x102 328 107 207x107 Clete fom data in International Critical Tables, 1928, onl Ill, MeGraa> Hil, New York, p.271TABLE, 10.4 Solubility of Oxygen in Aqueous Solutions of Sugars ndet 1 atm Oxygen Pressure ‘Concentration ‘Temperature ‘Oxygen solubility under 1 atm Sugar (gmol per kg H20) co oxygen pressure (kg mv") Glucose 0 20 450107 o7 20 381x107 15 20 318x107 30 20 254x107 Sucrose 0 15 495107 ot 5 425x107 09 15 347x107 12 15 3.08. 107 Caleulated from data in International Critical Tables, 1928, vol IL, McGraw-Hil, New York, p. 272 TABLE 10.5 Values of H, and K, in Eq, (10.49) at 25°C. Cation HOUT Gt mol) Anion ——«HLXI0 mol) Sugar“ XI (a mol) w ~0774 on sat Glucose 0.119 x =05%6 o sas Lactose 0.197 Nat 0550 coe 08s Sucrose 0.49" NHS 0720 se oss Mg 0314 Noy 0.802 ca 0303 HOS 1058 Mat 0311 HPO, 1037 Hog 01485 Poe 0820 “Approximately valid for sucrose concentrations upto about 200g From A. Schumpe, 1 Aer, nd W-D. Decker, 1978, Solubility of oxygen in cloctolyte solution. Biotechnol. Bioeng. 20, 145180; and ©. Quiker A Schonpe, B. Kani, and WD, Deceer, 1981, Compara of mstsure ard calculated oxygen slits fermentations ‘matia, Biotechnol. Bioeng. 23, 635-5.TABLE 13.2 Genemaliced Thiele Moduli rape oye yl Pm Ka ¥Ox aE ES)” K, a= Km Oo Ors shee Sasa) [oma] rape og EEL) vom ( 2 Michaelis—Menten reaction: r= is a)”TABLE 13.3 Effectiveness Factors (¢ for each geometry and kinetic order is defined in Table 13.2) First-order reaction: r=, Cq 1 Sphere* = 4.66, coth39,—1) pl m= 56H " Flat plate’ m= mh Zero-order reaction: r4 = ky Sphere® no=1 for 0< 6) =0.577 for go> 0.577 Flat plate no=1 _a "0 “Cath i the abbreviation for hyperbolic cotangent. Coth x is defined as: eet coth x= aoe Tan is the abbreviation for hyperbolic tangent. Tank x is defined as: tanh x= 22 ater “Cos is the abbreviation for cosine. The notation cos x (or arceos x) denotes any angle the cosine of twhtich is x. Angles used to determine cos and cos? are in radians. TABLE 13.4 Observable Thiele Moduli = (RY) _tAsbs Sphere ee () TaeCan Flat plate ob =p TAs “AsTABLE 13.5 Minimum Intracatalyst Substrate Concentration for Zero-Order Kinetics (@ for each geometry is defined in Table 13.4) Sphere Camin=0 Comin = e.(1 - 3°) Flat plate Camin=0 - 1 Cas ( 30) TABLE 13.6 Observable Moduli for Extemal Mass Transfer Camin Sphere TiC Rat phate 2= re TABLE 13.7 First-order reaction: ra =k Ca Zoro-order reaction: 14 =ko ‘Michaelis—Menten reaction: r4 = Umax Kan ¥Ca for = 0.667 for &< 0.667 for P=2 for <2 Extemal Effectiveness Factors yy 2 a8 aor no=l = Cas(Km + Cas) te Tan(Rm Cas)TABLE 13.8 Effective Diffusivity Values Tne Substance Solid Temperature Jams) Tay Reference Onsen ‘Agar (2% w/v) containing Bec 194x10 — 070 Cantidetipolytica cols Microbial aggregates from 20e 197%10 —062 (25) domestic waste treatment plant “Teichting-iter sine ae ose 10 ie Glucose Microbial aggregates from 20c osx? 037 (25) domestic waste treatment plant Glas fibre discs containing 30°C 030x100 043 [3] Saccharomyces wourun cells Calcium alginate 3 wt) 30°C osx? 087 (281 Calcium alginate 24-28 wt) 30C 06x10 037 (28) containing 50 wi bakers’ yeast sucrose Calcium alginate 2% w/W) ae o4sx1r? ase (23) Calcium alginate 2% w /¥) 25C oxi 025 (23) containing 125% (v/v) atharantius roses cols Ltyptophan Calcium alginate 2%) 30°C osrxi 19 Carrageenan (4%) 30°C osx 088 Lactate Agar (1%) containing 1% Ehrlich 37°C 1axie? 037 ascies tumour ells Agar (1%) containing 6% Ehrlich — 37°C 7x1? — 048 (32) asctes tumour calls Btanol ‘eCarragesnan (4%) 30°C tox? 092 (BI) Calcium alginate 4-28 wt) 30°C 125x107 092 (28) Calcium alginate 24-28 wi%) 30°C o4sx10 033 (23) containing 50 wi% bakers’ yeast Nitrate Compressed film of nitrifying 14x10? 090 (25) organisms Ammonia Compressed film of nitrifying 13x10 080 (25) organisms, Bovine serumalbumin Agarose 6.5% v/v) 20C 00x10 03833) Agarose 0.2% v/v) 20e oo1sx 10 028 (33) Lysozyme Cation exchange resin, pH 7 o0sx10 04534)FIGURE 13.9 Measured and calculated oxy- ‘gen concentrations in a spherical agarose bead containing immobilised enzyme. Particle diame- ter=4 mm; Cay =0.2 mol m”°. The enzyme load ings are: 0.0025 kg m~ of gel (m); 0.005 kgm”? of gel (2) 00125 kg m™ of gel (4), and 0025 kg me? of gel (@). Measured concentrations are shown using symbols; calculated profiles are shown as limes. From CM. Hooijmans, SGM. Geraats, and K.Ch. A.M, Liyben, 1990, Use of an oxygen micro sensor for the determination of intrinsic kinetic parameters of an immobilised oxygen reducing enzyme. Biotechnol. Bioeng, 35, 1078-1087. Cx Relative oxygen concentration ( on os 1 5 10 % FIGURE 13.11 Intemul elfeciveness factor yp, a8 @ function of the genemlised Thisle modulis $y for first- oonter kinetics and spherical. cylindrical and flat-plate geometries. The dots represent calculations on finite or hol- low cylindess and parallelepiped. From R. Aris, 1975, Mathematical Theory of Diffusion and Reaction in Pemmeable Catalysts, vol. 1, Oxford University Press, London.0 FIGURE 13.12 _Intemal effectiveness factor no as a function of the generalised Thiele modulus « for zero- order kinetics and spherical and flat-plate geometries.B= 0 (zero-order) on 1 10 Pon FIGURE 13.13 Internal effectiveness factor tim as a function of the generalised Thiele modulus dm and parameter @ for Michaelis~Menten kinetics and flat-plate geometry. =Kn/ Cae From R. Aris, 1975, Mathematical Theory of Diffusion and Reaction in Permeable Catalysts, vol. 1, Oaford University Press, London.q % 14 oor on 1 10 100 ° FIGURE 13.14 Internal effectiveness factor mp as a function of the observable Thiele modulus # for spherical geometry and first-order, zero-order, and Michaelis~Menten kinetics. = Kn/Cas- From WH. Pitcher, 1975, Design and operation of immobilized enzyme reactors. In: R.A. Messing (Ez.), Immobilized Enzymes for Industrial Reactors, pp. 151-199, Academic Press, New York.(qumol min-t per mg eazy ney! os 08 03 02 ou 00 Increasing @y, Inmobilised enzyme Free emyme 1 0 tx108ar) 15 —a 20 FIGURE 13.20 Lineweaver-Burk plots for free and immobilised galactosidase. Enzyme concen- ‘rations within the gel are: 0.10mg ml" (®); 0.7 mg mI ©); and 0.50 mg mI ‘Data from P'S. Bunting an KJ. Laidler, 1972, Kinetic studies on solid sepported 8-galactosdase. Biochemistry 11,4477 4483.