Diffusion process in enzyme–metal hybrid catalysts

doi:10.1007/s11705-022-2144-4

Front. Chem. Sci. Eng.

2022, Vol. 16

Issue (6) : 921-929 https://doi.org/10.1007/s11705-022-2144-4

RESEARCH ARTICLE

Diffusion process in enzyme–metal hybrid catalysts

Shitong Cui¹, Jun Ge^1,²(

)

¹. Key Lab for Industrial Biocatalysis, Ministry of Education, Department of Chemical Engineering, Tsinghua University, Beijing 100084, China
². Institute of Biopharmaceutical and Health Engineering, Tsinghua Shenzhen International Graduate School, Shenzhen 518055, China

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Abstract

Enzyme–metal hybrid catalysts bridge the gap between enzymatic and heterogeneous catalysis, which is significant for expanding biocatalysis to a broader scope. Previous studies have demonstrated that the enzyme–metal hybrid catalysts exhibited considerably higher catalytic efficiency in cascade reactions, compared with that of the combination of separated enzyme and metal catalysts. However, the precise mechanism of this phenomenon remains unclear. Here, we investigated the diffusion process in enzyme–metal hybrid catalysts using Pd/lipase-Pluronic conjugates and the combination of immobilized lipase (Novozyme 435) and Pd/C as models. With reference to experimental data in previous studies, the Weisz–Prater parameter and efficiency factor of internal diffusion were calculated to evaluate the internal diffusion limitations in these catalysts. Thereafter, a kinetic model was developed and fitted to describe the proximity effect in hybrid catalysts. Results indicated that the enhanced catalytic efficiency of hybrid catalysts may arise from the decreased internal diffusion limitation, size effect of Pd clusters and proximity of the enzyme and metal active sites, which provides a theoretical foundation for the rational design of enzyme–metal hybrid catalysts.

Keywords enzyme–metal hybrid catalyst internal diffusion proximity effect kinetic model

Corresponding Author(s): Jun Ge

Online First Date: 08 April 2022 Issue Date: 28 June 2022

Cite this article:

Shitong Cui,Jun Ge. Diffusion process in enzyme–metal hybrid catalysts[J]. Front. Chem. Sci. Eng., 2022, 16(6): 921-929.

URL:

https://academic.hep.com.cn/fcse/EN/10.1007/s11705-022-2144-4
https://academic.hep.com.cn/fcse/EN/Y2022/V16/I6/921

Fig.1 Schematics showing the process of (a) the heterogeneous catalysis and (b) the proximity channeling effect.

Symbol	Description	Unit
$C W P$	Weisz–Prater parameter	1
η	Efficiency factor of internal diffusion	1
φ	Thiele modulus	1
$D e$	Effective diffusion coefficient	cm²·s^?1
$D 12$	Molecular diffusion coefficient	cm²·s^?1
$D K$	Knudsen diffusion coefficient	cm²·s^?1
$ρ c$	Particle density	g·cm^?1
$R$	Particle size	cm
$θ$	Porosity of the catalysts	1
$τ$	Tortuosity of the catalysts	1
$r e$	Average pore size	cm
$r ′ (o b s)$	Observed reaction rate	mol·g^?1·s^?1
$C s$	Reactant concentration	mol?cm^?3
$X$	Associating coefficient of the solvent	1
$μ$	Viscosity of the solvent	P
$M$	Relative molecular weight of the solute	g?mol^?1
$V b$	Molar volume of the solute	cm^?3?mol^?1

Tab.1 Parameters used in the model

Fig.2 Schematics showing (a) the principles and (b) kinetic models of the DKR reaction catalyzed by CALB and Pd clusters.

Tab.2 Weisz–Prater parameters (C_WP) and effectiveness factors (η) of different catalysts

Fig.3 Radar maps illustrated the (a) effectiveness factor of internal diffusion η and (b) Weisz–Prater parameter C_WP of Pd/C and Novozyme 435.

Fig.4 Verification of the reaction order of (a, b) Novozyme 435 and (c, d) Pd/CALB-P to the R-substrate when assuming (a, c) first order and (b, d) second order, respectively.

Fig.5 Numerical solutions of the DKR reaction model for Pd/C + Novozyme 435 (dashed line) and Pd/CALB-P (solid line) with different fractions of the proximity channeling effect.

Catalyst	$k 1$	$k 2$	$f c$
Pd/C + Novozyme 435	0.13	0.60	0
Pd/CALB-P	0.37	13.60	1

Tab.3 Fitting values of kinetic parameters in the DKR reaction model

Fig.6 Fitting of the DKR reaction model to the experimental data reported for the Pd/C + Novozyme 435 and Pd/CALB-P.

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