Catalysis Communications 9 (2008) 1815–1816

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Catalysis Communications
journal homepage: www.elsevier.com/locate/catcom

On Langmuir kinetics and zero order reactions

Dmitry Yu. Murzin *
Laboratory of Industrial Chemistry and Reaction Engineering, Process Chemistry Centre, Åbo Akademi University, Biskopsgatan 8, FIN-20500 Turku/Åbo, Finland

a r t i c l e i n f o a b s t r a c t

Article history: Approximation of Langmuir kinetics to zero order is discussed in relation to photocatalytic reactions.
Received 25 November 2007 Ó 2008 Elsevier B.V. All rights reserved.
Received in revised form 12 February 2008
Accepted 14 February 2008
Available online 29 February 2008

Keywords:
Photocatalysis
Kinetics
Langmuir equation
Zero order

Kinetics of catalytic reactions is an established field of research
in heterogeneous catalysis [1–4]. Analysis of catalytic and photo-
catalytic kinetics in various reactions over solid catalysts is based
essentially on the application of Langmuir approach of ideal
surfaces.
In photocatalysis the following rate expression is applied:
kKC
r¼
1 þ KC
which stems from a mechanism allowing one relatively rapid (e.g.
adsorption equilibrium) reaction followed by a single, slow surface
reaction step:
1: AðliquidÞ ¡AðadsÞ ðequilibriumÞ
2: AðadsÞ ! products ðslowÞ
Photocatalytic oxidation of water contaminants, such as organic
dyes, hydrocarbons, conversions of dissolved metals was explained
with such kinetics [5,6], which was recently discussed in the liter-
ature [7–9] in connection with several photocatalyzed oxidation
reactions in the liquid phase and the limitations of such approach
were highlighted.
An attempt to analyze Langmuir kinetics in relation with photo-
catalysis was published [6] and it was proposed that it is impossi-
ble and inappropriate to approximate this kinetics to zero order.
We would like in the present communication to consider the
arguments put forward in [6].
* Tel.: +358 2 215 4985; fax: +358 2 215 4479.
E-mail address: dmurzin@abo.fi.
Note that Eq. (1) is often used in enzymatic catalysis [4,10–12]
and is known in somewhat modified form as Michaelis–Menten
equation. Similar to photocatalytic data linearization and applica-
tion of double reciprocal plots (e.g. 1/r vs. 1/C) [6] is utilized in
enzymatic catalysis as well.
A set of data, acquired in [13] for photocatalytic degradation of
Eosyn Y over titania was used in [6] for modeling. The fit of data
ð1Þ from [13] is presented in Fig. 1.
As can be easily seen the experimental data set could be ex-
plained by the Langmuir kinetics. Fig. 1 also contains a data fit
for the case when the value of equilibrium constant is fixed to be
equal to unity. Obviously the description is worse, which is not sur-
prising. Similar analysis was performed in [6], where it was stated
ð2Þ that deviations of the simulated data from experimental show the
significance of the KC term in Eq. (1), therefore Langmuir kinetics
cannot be approximated to zero order kinetics. It is obvious that
if the whole data set is taken into consideration, then the simulated
curve is affected by the choice of the equilibrium constant K. It
does not mean, however, contrary to the statement in [6], that
Langmuir kinetics in a certain range of conditions cannot be
approximated to zero order kinetics.
Let us make the analysis for a subset of data (Fig. 2).
As follows quite clearly from Fig. 2 since the reaction rate at
high substrate concentration is independent on it (which means
in essence zero order kinetics) the term KC in Langmuir kinetics
cannot be determined only based on this limited data set, as
KC  1.
Thus it can be concluded (contrary to [6]) that the Langmuir
kinetics can be approximated to zero order kinetics for a certain
range of experimental conditions and the rate is independent on

1566-7367/$ - see front matter Ó 2008 Elsevier B.V. All rights reserved.
doi:10.1016/j.catcom.2008.02.016
1816 D.Yu. Murzin / Catalysis Communications 9 (2008) 1815–1816

0.9 substrate concentration. Obviously if the whole data set is used for
kinetic modeling (Fig. 1), the term KC becomes significant.
0.8
The theoretical explanation for zero order kinetics is complete
0.7 K=1 covering of active sites by the substrate, thus presence of any addi-
tional substrate in the reaction milieu does not have any influence
0.6
on kinetics.
Rate, mg L/min

0.5
Model: Langmuir Model: Langmuir
Chi2/DoF= 0.01529 Chi2/DoF= 0.00299 Acknowledgement
0.4 R2 = 0.60134 R2 = 0.93325

k 0.79 ±0.05 k 0.92 ±0.04

0.3 K 1 ±0 K 0.26 ±0.06 This work is part of the activities at the Åbo Akademi Process
Chemistry Group within the Finnish Centre of Excellence pro-
0.2
gramme (2000–2011) by the Academy of Finland.
0.1
References
0.0
0 10 20 30 40 50 60
Concentration, mg/L [1] M. Boudart, G. Djéga-Mariadassou, Kinetics of Heterogeneous Catalytic
Reactions, Princeton University Press, Princeton, 1984.
[2] J.B. Butt, Reaction Kinetics and Reactor Design, second ed., Marcel Dekker Inc.,
Fig. 1. Reaction rate as a function of substrate concentration. Experimental data New York, 1999.
from [13]. Solid line: numerical data fitting and dotted line: the value of equilibrium [3] M.I. Temkin, Adv. Catal. 28 (1979) 173.
constant is fixed to unity. [4] D. Murzin, T. Salmi, Catalytic Kinetics, Elsevier, Amsterdam, 2005.
[5] N. Serpone, A. Salinaro, A. Emeline, V. Ryabchuk, J. Photochem. Photobiol. A
Chem. 130 (2000) 83.
1.0 [6] K.V. Kumar, K. Prokodi, F. Rocha, Catal. Commun. 9 (2008) 82.
[7] D.F. Ollis, J. Phys. Chem. B 109 (2005) 2439.
[8] D.F. Ollis, Top. Catal. 35 (2005) 217.
[9] D.Yu. Murzin, React. Kinet. Catal. Lett. 89 (2006) 277.
0.8
[10] H. Bisswanger, Enzyme Kinetics, Principles and Methods, Wiley-VCH,
Weinheim, 2002.
[11] A. Cornish-Bowden, Fundamentals of Enzyme Kinetics, third ed., Portland
0.6 Press, London, 2004.
Rate, mg/L min

Model: Langmuir Model: Langmuir

Chi2/DoF= 0.00086
[12] V. Leskovac, Comprehensive Enzyme Kinetics, Kluwer Academic/Plenum
Chi2/DoF= 0.00102
R2 = 0.01047 R2 = -0.03661 Publishers, NY, 2003.
0.4 [13] I. Poulios, E. Micropoulou, R. Panou, E. Kostopoulou, Appl. Catal. B Environ. 41
k 0.82 ±0.03 k 0.82 ±0
K 5.4 ±26.9 K 83 ±2477 (2003) 345.

0.2

0.0

0 10 20 30 40 50 60
Concentration, mg/L

Fig. 2. Reaction rate as a function of substrate concentration. Experimental data

from [13]. Solid line: numerical data fitting and dotted line: the value of rate con-
stant is fixed.