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Modeling simultaneous

sac~hari~cation and fermentation of

lignocellulose to ethanol in batch and

continuous reactors

C. R. South, D, A. L. Hogsett and L. R. Lynd

Thayer School of Engineering, Dartmouth College, Hanover, New Hampshire

**An adsorption-based kinetic model was sought that accurately predicts simultaneous saccharifcation and fer-
**

mentation (SSF) of insoluble lignoceihdosic substrates in batch and continuous reactors. With a common set of

three heuristic parameters, a hydrolysis rate equation of the form r = (k X (I - x)” + cl x (ES)/(C,) in

conjunction with Langmuir a~orption is capable of accurately representing batch SSF data from we&mixed

bioreactors for a variety of feed substrate concentrations and cellulase loadings (root mean squared (RMS)

difierence in predicted and measured conversion = 5.2%). Using a particle population model in conjunction

with the batch kinetics, conversion in a CSTR as a function of residence time is also well predicted (4.6% RMS

difference). In&ding both batch and continuous data, the model is successful over a four-fold range of enzyme

loadings and a 12 .&fold range of substrate concentrations. Commentary is offered on useful features of kinetic

models for processes including cellulose hydrolysis

Keywords: Enzymatic hydrolysis; celiulase kinetics; SSF: ethanol

**Introduction Trichoderma reesei cellulase and Saccharomyces cerevisiae
**

fermentation in both batch and continuous well-mixed sys-

The bioreactor in which enzymatic hydrolysis and fermen- tems.3 The purpose of this study was to develop a kinetic

tation occurs is a logical focal point in pursuing cost reduc- model and modeling approach for ethanol production from

tions for ethanol production from ceiluIosic biomass. ‘+2A cellulosic biomass as exemplified by SSF, and to test the

validated kinetic model capable of predicting simultaneous adequacy of the proposed model for correlating our previ-

sacch~~cation and fc~entation (SSF) performance over a ous ex~~mental results. Continuous systems are a partic-

range of substrate concentrations, cellulase loadings, and ular focus, as these have both significant applied potential

reactor configurations would be a useful tool in this en- and interesting fundamental features. The specific continu-

deavor, but is not available at present. The absence of such ous system considered here is well mixed and at steady state

a model is attributable primarily to the complexity and in- with continuous substrate and enzyme addition, and with

complete state of understanding of the action of cellulase enzyme and residual substrate continuously existing in the

enzyme systems acting on nonideal particulate lignocellu- reactor effluent.

losic substrates. By contrast, kinetic models have been pre-

sented in the literature for other processes involved in SSF

(see below) such as the action of &glucosidase and asso- Analytic framework

ciated inhibition by soluble sugars, and the fermentation of

soluble substrates and associated inhibition by ethanol. To be an effective tool for reactor design, a kinetic model

We recently reported experimental results for SSF using for SSF should predict substrate conversion, x [X = 1 -

(Remaining cellulose)/(Initial cellulose)], with reasonable

accuracy over a significant range with respect to input sub-

strate concentration, cellulase(s) loading, reaction time, and

Address reprint requests to Dr. L. R. Lynd, Thayer Schoof of Enginee~ng,

substrate conversion. We sought to develop such a model.

Dartmouth College, Hanover, NH 037% The approach taken here was to use the minimum level

Received 26 August 1994 of complexity required to obtain a useful model. Specifi-

**Enzyme and Microbial Technology 17:797-803, 1995
**

0 1995 by Elsevier Science Inc. 0141-0229/95/$10.00

655 Avenue of the Americas, New York, NY 10010 SSDI 0141-0229(94)00016-K

Papers

**tally, we considered a single measure of cellulase activity ticulate biomass in a CSTR can be considered equivalent to
**

(FPU), and used a Langmuir adsorption model as presented segregated micromixing with respect to the substrate and

by Ooshima et al. 4 in combination with a conversion- complete micromixing with respect to the aqueous phase.

dependent rate constant. The Langmuir affinity constants For such conditions, mean conversion can be calculated

for cellulose and lignin, respectively, were defined as: from the relationship between conversion and time, x(t), for

a given particle and the exit age distribution E(t,r), where t

is time and T = (Reactor volume)/(Volumetric flow rate) is

(1)

the mean residence time. Overall conversion as a function

of mean residence time under these conditions is given by a

particle population model as represented by Equation (8):

(2)

**where C, and C1 represent the capacity of substrate and
**

lignin, respectively, to bind enzyme, and may also be in-

X(T) =

I cc

0

x(t) x E(t,T) dt (8)

terpreted as the ratio of E to S or L in each enzyme com- where E(t,r), the reactor exit age distribution for an ideally

plex. The Langmuir constants reported by Ooshima et al. mixed CSTR, is given by Equation (9)“:

were for a similar, though not identical, substrate to that

modeled here. E(t,T) = i X exp - i (9)

Conservation equations for substrate, lignin, and enzyme ( 1

respectively are:

Equation (8) is used to account for the conversion and res-

idence time-dependent behavior of enzyme and substrate

(3) over the course of the reaction of a population of individual

particles in a CSTR, and represents a useful framework

within which to analyze continuous nonhomogeneous par-

(4) ticulate reactors. Thus, to successfully model particulate

substrate reactions that incorporate factors such as changing

adsorptive capacity or accessibility of substrate with con-

L$ = Er + ES + EL (5)

version, 12.13 declinin reactivity of the enzyme bound to

P

Enzyme adsorbed to cellulose and lignin is calculated from cellulose over time,7, or declining substrate reactivity as in

E,, S, and L, with the adsorption parameters of Ooshima et this analysis, it is necessary to account for the conversion

~1.~We also used the assumption by Ooshima et al. that the and residence time-dependent behavior of enzyme and sub-

capacity constants for both the lignin and cellulose do not strate over the course of the reaction of a population of

change during the course of hydrolysis. Equations (1) individual particles.

through (5) can readily be solved simultaneously to give ES

for values of initial substrate (cellulose and lignin), E,, K,,

SSF simulation

Kr, Cs, and Cr.

All studies known to us indicate a notable decline in Rate equations used to simulate SSF are presented below,

(r)/(ES) over the course of the reaction. Working with T. where r is the rate of formation of the component of interest.

reesei cellulase and a pretreated hardwood substrate similar Equations (10) and (11) account for the enzymatic hydro-

to that used here, Nutor and Converse’ found (r)/(ES) at lysis of cellulose and cellobiose, respectively; Equations

high conversion to be one to two orders of magnitude less (12) through (14) account for cell production, substrate up-

than at low conversion. Other investigators?” also re- take, and solvent production by the biocatalyst:

ported decreasing reactivity as reaction proceeds. Declining

reactivity with increasing conversion in combination with ES

an adsorption model suggests a rate equation of the general rs = - {k x (1 - x)” + c} x cs x

form

ES x [(Elhk:rE:&] (10)

r = k(x) X -

cs

Consistent with the trend exhibited by the data of Nutor and rc = 1.056 X rs -

Converse, we chose to consider k(x) of the form i(K- xk[:+‘k$ + C)]

k(x) = k x (1 - x)” + c (7)

(11)

Modeling reaction of particulate substrates in (Xc x vmaxx G) Eth

( --I

rx =

(12)

continuous reactors G+ko ’ ‘- kxiEth

The simplest type of continuous reactor for hydrolysis of

cellulose is the continuous stirred tank reactor (CSTR). Us- ro=(-l.O56~rs-rc)~ 1.053-rX (13)

ing the nomenclature of Danckwerts,” the reaction of par- YX/G

**798 Enzyme Microb. Technol., 1995, vol. 17, September
**

Modeling simultaneous saccbarification and fermentation of ~ignocelluiose to ethanol: C. R. South et al.

YEtWG

enzyme between lignin and cellulose fractions of the bio-

r&h = rx x - (14) mass, then summing the enzyme forms in the reactor. E,

Y%G

was varied iteratively until the enzyme inventory agreed

The form and associated constants for terms in the above with the specified value of E, to within 0.1%. The conver-

equations are from Gustakov et ~1.‘~ for the rate of cello- sion of each particle residing for a time t in the reactor in the

biose formation, Phillippidis et ~1.‘~ for inhibition by eth- presence of the free enzyme concentration calculated as

anol on cellulose hydrolysis, cellobiose inhibition of cellu- above was then determined. Cellulose solubilization, and

lose hydrolysis, and inhibition of P-glucosidase by glucose, hence cellobiose formation from the particulate substrate in

and van Uden” for the effect of ethanol on biocatalyst the CSTR, was computed from the discrete form of Equa-

growth. The Monod model is used for biocatalyst growth tion (8), given by Equation (18).

with kinetic constants from Ghose and Tyagii6 and van

x

Uden. The constants 1.053 and 1.056 arise from the addi-

tion of water during hydrolysis. X(T) = c q(t) x Wi(t) (18)

For continuous SSF at steady state the cont~butions of

the range of particle reaction times comprising the overall

hydraulic residence time distribution E(t,r) is represented Cellobiose pr~uction Equation (IO), and consumption,

by Equation (9), with x(t) evaluated in the presence of a Equations ( 11) and (15), are balanced by iteratively adjust-

common aqueous environment. Cellobiose concentration is ing the aqueous cellobiose level. A dilution curve is ob-

calculated from the CSTR mass balance Equation (15), tained by repeating this procedure at different hydraulic

which balances the rate of cehobiose pr~uction and con- residence times. In this manner conversion in a CSTR as a

sumption with loss due to liquid outflow: function of hydraulic residence time can be predicted with

no new parameter estimation from that used to calculate the

c batch SSF conve~ion .

rc = -

7

**The CSTR glucose concentration can be determined explic- Results
**

itly from he Monod equation and the steady-state material ~ar~~~ter fitting for Dutch data

balance for a well-mixed reactor by:

A single set of the parameters k, n, and c for the conversion-

ki dependent rate constant (7) were fit to the batch SSF data at

G= (16)

tT x Pmax - 1) all enzyme loadings, with the sum of squared residuals

(simuIated minus ex~~mental time to achieve the experi-

mental conversion) minimized by the use of a Hooke-

Methods Jeeves optimization procedure. Optimization using time-

The SSF data and associated methods have been previously re- based residuals weights the high conversion fit more heav-

ported.? Batch SSF performance was predicted by simultaneously ily; this is appropriate, as high-substrate conversion is a

solving Equations (10) through (14) via a fourth-order Runge- likely to be a requirement for financial viability. Figure 1

Kutta algorithm. At each time step, E, was varied iteratively, presents experimental data for batch SSF run together with

allowing calculation of ES and EL using ~uat~ons (1) and (2).

until convergence to Equation (5) (within a 0.1% tolerance) was

found. Enzyme p~itioning could be solved directly for the batch

case; however, an iterative approach was necessary for the simu-

lation of the continuous SSF case, and a common algorithm was

used.

In accordance with Equation (g) the composition of the partic-

ulate substrate was calculated as the weighted sum of particles that

spent varying times in the reactor as defined by the residence time

distribution E(t.7). The weight, W, allocated to the conversion of

a particle that resided in the reactor between t, and time ti + At

was given by evaluating the integral of the exit age distribution

E(t,r) over this time interval as per Equation (17),

Wi(t) = :;+‘t E(t,r) dt (17)

f

To ensure an adequate range of particle residence times, the

procedure was repeated until the time integral of the exit age 0 0.5 I 1.5 2 2.5 3 3.5 4 4.5 5

distribution, Zi[E(ti) X At], reached 0.999 (as Jb”E(t,r) dt Residencetime (days)

= 1).

In a steady-state CSTR, enzyme in the aqueous phase is Figure 1 Predicted and experimental conversion for batch SSF

with pretreated wood at 35 g I-’ cellulose, and cellulase load-

modeled as spatially homogeneous. The total enzyme in the ings as shown, using the parameter values given in Table 1.

reactor is calculated by solving the sets of coupled differ- Cellulase loadings were: U, 5 U g-‘; 0, 10 U g-‘; 0, 15 U g-l;

ential and Langmuir equilib~um equations that partition the andA,ZOUg-’

**Enzyme Microb. Technol., 1995, vol. 17, September 799
**

Papers

the predicted time-course conversion based on integration

of Equations (10) through (14) and the parameter values

indicated in Table I. Figure 2 compares the residuals of

Figure 2 with those obtained using a best-fit model with

constant k. We were unable to accurately represent the

batch data at varying cellulase loadings using a single pa-

rameter model for the rate coefficient k. The root mean

squared error in the time to reach a given conversion of the

constant rate model is five times higher than the declining

rate model (0.45 days versus 0.09 days). Further, the re-

siduals for the constant rate model are generally positive for

low conversion and negative for high conversion, whereas

the declining rate model residuals are distributed about zero

-1.5 ~,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,~,~

for all conversions. Figure 3 shows the (r)/(Eadsorbed) data of

0 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9

Nutor and Converse’ (specific rate based on total adsorbed

Conversion

enzyme), along with the rate per total adsorbed enzyme

independently calculated using the SSF adsorption model Figure 2 Normalized residuals for batch SSF predictions using

and the best-fit values for k, c, and n. The fit to Nutor and declining (r)/(EC) (open symbols), and constant (r)/(EC) (closed

Converse’s data is surprisingly good considering that the symbols). Cellulase loading symbols as per Figure 1

substrates used by Nutor and Converse and Ooshima et al.

were different from those used here, and that the data of

4.2%, respectively, indicating that the proposed CSTR

Nutor and Converse are for cell-free enzymatic hydrolysis,

framework performs well, particularly when the inherent

whereas our data are for SSF.

variability in the steady-state results is considered (standard

deviation conversion = 3.5%).

Prediction of conversion in a CSTR The particle population model can be compared to a

CSTR model, where the substrate is immediately diluted to

Table 2 shows the application of the kinetic model and its exit reactivity, as is the case for a soluble substrate. In

CSTR prediction algorithm to continuous data. To obtain this case the substrate reactivity corresponds to that of the

these predictions no further parameters were fit beyond material leaving the reactor, and conversion is given by:

those previously used to predict batch conversion. Equa-

tions (8) and (9) were used together with the rate equations ES

x(7) = k[x(T)] x -

and adsorption parameters used in the batch simulations as S, x Cs x 7

well as the CSTR solution framework described in Meth-

ods. The average absolute error (predicted - actual conver- Figure 4 presents the ratio of reaction times required to

sion) in the batch and continuous models were 3.8 and achieve a given conversion in a CSTR relative to a batch

reactor as a function of conversion. Whereas this ratio is

approximately 2.5 for prediction according to the soluble

Table 1 Parameters used in the generation of the models in substrate model, it is significantly lower (approximately 1.4

Figures 2 through 4 with some increase at high conversions) for prediction ac-

Symbol Value Source

**C 0.18125 h-’ This work 45 d 0
**

k 2.8625 h -’ This work

k, 0.020 g/(U h - ’) Gusakov and Sinitsyn14

0.05 g I-’ Ghose and Tyagi”

? 1.49 I u-1 Ooshima et a/.4

K: 0.66 I W’ Ooshima et a/.4

K, 10.56 g I-’ Phillippidis et a/l3

kC/G 0.62 g I-’ Phillippidis et aLI

ks/c 5.85 g 1-1 Phillipidis eta/.13

kS/Eth 50.35 g I -’ Phillipidis eta/.13

kWEth van Uden”

z?-’ This work

5s 98.3 U g-i Ooshima et aL4 L

I 1z.i pi- Ooshima et a/.4

bmax Ghose and Tyagi16 0 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9

Y x/S 0.69 Ghose and Tyagi” Conversion

Y Eth/S 0.47 Ghose and Tyagi”

Figure 3 Hydrolysis rate per cellulase adsorbed to cellulose, in

The data of Ooshima et aL4 for b, K,, C., and C, are reported in relation to conversion (data for similar substrate concentration

terms of adsorbed protein measurements. Activity was deter- and cellulase loading from Nutor and Converse5), shown with

mined from filter paper activity of the same enzyme solution declining MEadsorbed ) curve calculated from the batch SSF sim-

(1.22 U mg-‘1 measured by Girard and Conversez3 ulations and best-fit (r)/(EC) parameters

**800 Enzyme Microb. Technol., 1995, vol. 17, September
**

Modeling simultaneous saccharification and fermentation of lignocellulose to ethanol: C. R. South et al.

TABLE 2 Summary of continuous SSF data and model predic- Although the hydrolysis rate equation used here does not

tions incorporate mechanistic detail the success of this rate equa-

tion as well as the general modeling approach is not without

fundamental implications, and may provide some guidance

g I-’

Hydraulic Cellulase in understanding biomass hydrolysis and subsequent formu-

residence loading Experimental Predicted lation of mechanistically based models. In particular, our

time (days) In out (U g-11 conversion conversion

results support the utility and validity of the following fea-

tures in the context of modeling processes that involve cel-

0.93 39.9 17.5 12.9 0.54 0.58

lulose hydrolysis:

1.25 60.5 25.8 14.6 0.62 0.67

1.39 40.4 15.6 14.6 0.65 0.69 An adsorption model that allows for either enzyme or

2.03 60.8 12.5 11.6 0.79 0.73

substrate to be in relative excess;

3.26 33.9 6.1 15.3 0.86 0.83

1.50 42.1 10.2 24.0 0.76 0.77 A conversion-dependent rate equation that reflects the

0.58 4.7 3.3 16.0 0.31 0.38 declining ratio of (r)/(ES) as the reaction proceeds;

For CSTRs, and we believe continuous reactors in gen-

Experimental data is from South et al.3 eral, a particle-population model that accounts for vari-

ation in rate over the time individual particles spend in

the reactor.

cording to the particle population model. Experimental data

agree much better with the particle population model, sug- These features are discussed successively in the paragraphs

gesting that such an approach is necessary to accurately that follow.

represent continuous conversion of particulate substrates. The incorporation of an adsorption model into the hy-

drolysis rate equation allows for the prediction of rate sat-

uration with enzyme, a phenomenon that has frequently

Discussion been reported for biomass hydrolysis’7-‘0 and limits the

utility of the Michaelis-Menten model to biomass hydroly-

The proposed SSF model satisfactorily fit batch data. Data sis. Langmuir models have been shown to adequately

obtained in continuous culture are predicted well by the describe adsorption of T. reesei cellulase onto bio-

same model with the application of a particle population- mass, 4.‘o,2@22 although the matter of adsorption reversibil-

based analytic framework. The average error for fitted batch ity appears to be an open question.“.*’

data and predicted continuous data was comparable in mag- In light of the success of the model reported here, and the

nitude to that of the analytic techniques used. We thus con- similar pattern for measured and fitted data for (r)/(ES), we

clude that the model works well for reproducing, and at believe it highly likely that a sharp decline in (r)/(ES) over

least for a CSTR predicting, experimental SSF data over the the course of hydrolysis actually occurs and should be in-

range of conditions to which it has been applied. As this corporated into kinetic models for biomass hydrolysis. Al-

range includes conditions encompassing enzyme loadings though we use Ooshima et ~1,‘s [4] assumptions with re-

that differ by a factor of 4 and feed substrate concentrations spect to lignin availability we have found that the trend of

that differ by a factor of 12, and encompass both batch and declining (r)/(ES) is insensitive to lignin availability as-

continuous systems, the model would appear to be rather sumptions, including full availability over the course of

robust. reaction to availability proportional to conversion (data not

shown). Loss of cellulase activity over time has been re-

ported by investigators.7s However, the high recovery of

free-enzyme activity (up to 50% relative to initial activity),

and the conservation of specific enzyme activity in the study

of Ooshima et al., exclude loss of activity as the major

factor underlying the observed decline in (r)/(ES). More

widespread investigation of this reactivity decline and ex-

planation at the level of interactions between individual en-

zyme components and their binding sites are important ar-

eas for future research.

Based on the results presented here, and Figure 4 in

particular, it is believed that variation of substrate reactivity

over the time individual substrate elements spend in a re-

actor is a fundamental difference between insoluble and

soluble substrates. Whereas soluble substrates are brought

0.5 0.55 0.6 0.65 0.7 0.75 0.6 0.65 0.9 by dilution to their exit reactivity upon introduction into the

Conversion reactor, this does not occur with an insoluble substrate.

During the time a biomass particle spends in a CSTR, for

Figure 4 Ratio of time achieve conversion in CSTR versus that example, the fractional conversion of an individual particle

in batch for population-based model, and a soluble substrate

CSTR model. Simulations are using 50 g cellulose I-’ pretreated

progresses from zero upon entry to some value < 1 upon

wood, with cellulase loading of 15 U g-’ cellulose, and the pa- exit. Simultaneously, the reactivity of the particle declines

rameter values given in Table 1. Experimental data, A radically, with a maximum at x = 0 and declining there-

**Enzyme Microb. Technol., 1995, vol. 17, September 801
**

Papers

after. The reactivity of an element of a particulate substrate Cs Specific ca acity of cellulosic component for cellu-

over time in a CSTR is thus much like that of a soluble lase, U g- P

substrate in a batch or plug flow reactor, but is decidedly C, Specific capacity of lignaceous component for cellu-

different from that of a soluble substrate in a CSTR. lase, U gP

p+,,,,Maximum cell growth rate, hh ’

7 Average CSTR hydraulic residence time, h

Symbols

B B-glucosidase concentration in solution, U 1-l

Acknowledgments

C Conversion-independent component in rate

function, h- ’ The authors are grateful to A. 0. Converse for useful dis-

C Cellobiose concentration, g l- ’ cussions, and for the support provided by NREL subcon-

Eth Ethanol concentration, g 1- ’ tract RE-2-13005-1, as well as the John Merck Fund and

Er Cellulase enzyme in solution, U 1- ’ NSF Grant BCS 9058392.

E, Total cellulase enzyme added, U 1-l

EL Concentration of lignin-cellulase complex, References

u 1-l

ES Concentration of cellulose~ellulase complex, I Chem Systems. Technical and Economic Evaluation, Wood IO Erh-

anol Process. Office of Energy Demand Policy, Department of En-

u1-’

ergy, Washington, DC, 1992.

E(t,r) Residence time distribution in CSTR, hh ’ 2 Lynd. L. R.. Cushman, J. H.. Nichols, R. J. and Wyman, C. E.

G Glucose concentration, g 1- ’ 1991. Fuel ethanol from cellulosic biomass. Science 251, 1318-

Increment counter, Dimensionless 1323

Hydrolysis rate constant, h - ’ 3 South. C. R., Hogsett. D. A. and Lynd, L. R. Continuous fermen-

f(

tation of cellulosic biomass to ethanol. Appl. Biochem. Biotechnol.

k Rate constant for hydrolysis of cellobiose to glu- 1993. 39/40, 587-600

cose, g/(U h- ‘1 4 Ooshima. H., Bums, D. F. and Converse, A. 0. Adsorption of

Monod constant, g 1- ’ cellulase from Trichoderma ressei on cellulose and lignacious resi-

Inhibition of cellobiose hydrolysis by glucose, due in wood pretreated by dilute sulphuric acid with explosive de-

compression. Biotechnol. Bioeng. 1990, 36, 446-452

g 1-l

5 Nutor, J. R. K. and Converse, A. 0. The effect of enzyme and

k SIC Inhibition of cellulose hydrolysis by cellobiose, substrate levels on the specific hydrolysis rate of pretreated poplar

g 1-l wood. Appl. Biochem. Biotechnol. 1991. 28129, 757-771

k S/Eth Inhibition of cellulose hydrolysis by ethanol, 6 Borchert. A. and Buchholz, K. Enzymatic hydrolysis of cellulosic

materials. Proc. Biochem. 1987, 22, 173-180

g 1-l

7 Gusakov, A. V.. Sinitsyn, A. P. and Anatole, A. K. Factors affect-

k XlEth Inhibition of cell growth by ethanol, g I- ’ ing the enzymatic hydrolysis of cellulose in batch and continuous

H-4 Hydrolysis rate at conversion X, h - ’ reactors: Computer simulation and experiment. Biorechnol. Bioeng.

K,

Adsorption constant for cellulosic fraction of 1987. 29, 906-910

biomass, 1 U - ’ 8 Ooshima. H., Kurakake, M.. Kato, J. and Harano, Y. Enzymztic

activity of cellulase adsorbed on cellulose and its change during

Adsorption constant for lignaceous fraction of

hydrolysis. Appl. Biochem. Biotechnol. 1991, 31, 253-265

biomass, 1 U - ’ 9 Ryu, D. D. Y.. Lee, S. B.. Tassinari, T. and Macy, C. Effect of

K,

Michaelis constant of B-glucosidase for cellobi- cdmpression milling on cellulose structure and on enzymatic hydro-

ose, g 1-l lvsis kinetics. Biofechnol. Bioena. 1982, 24, 1047-1067

Lignaceous component of the biomass substrate, 10 Wang, S. and Converse, A. 0. dn the use ofenzyme adsorption and

L

specific rate to characterize enzymatic hydrolysis of poplar thermal-

g 1-l chemical pretreatment. Appl. Biochem. Biotechnol. 1991. 34135,

Lf Lignaceous component not bound to cellulase, 61-74.

g1-’ 11 Danckwerts. P. V. The effect of incomplete mixing on homoge-

n Exponent of the declining substrate reactivity, neous reactions. Chem. Eng. Sri. 1953, 2, 93-102

12 Nidetzky. B. and Steiner. W. A new approach for modeling cellu-

Dimensionless

lase-cellulose adsorption and the kinetics of the enzymatic hydroly-

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