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Laccase catalysed conjugation of catechin with poly(all...
Chemical Engineering Journal 
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Kinetics and mechanism on laccase 
catalyzed synthesis of poly(allylamine)–
catechin conjugate 
Parikshit Gogoia, 1, Swapnali Hazarikaa, 1, Narendra N. Duttaa, , ,  
and Paruchuri G. Raob, , , 
 
a
 Chemical Engineering Division, North East Institute of Science and Technology 
(Council of Scientific and Industrial Research), Jorhat 785 006, Assam, India 
b
 North East Institute of Science and Technology (Council of Scientific and 
Industrial Research), Jorhat 785 006, Assam, India 
Received 22 August 2009;  revised 7 July 2010;  accepted 9 July 2010.  Available 
online 18 July 2010.  
Chemical Engineering Journal 
Volume 163, Issues 1-2, 15 September 2010, Pages 86-92  
doi:10.1016/j.cej.2010.07.020 | How to Cite or Link Using DOI 
Copyright © 2010 Elsevier B.V. All rights reserved. 
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Abstract 
The conjugation reaction of catechin with poly(allylamine) has been studied in 
aqueous methanol using free, immobilized and cross-linked enzyme crystals 
(CLEC) of laccase from Trametes versicolor with particular emphasis on the 
effect of pertinent variables and kinetic aspects of the reaction. The stability of 
the CLEC was better than that of the free and immobilized enzymes for 
practical application. The kinetics of the conjugation reaction conformed to the 
so-called Substituted-enzyme mechanism with catechin inhibition. In case of 
immobilized laccase system marginal diffusional limitation could be inferred 
from the experimental data. The kinetic parameters Km(paa) and Km(cat) 
estimated by non-linear regression analysis were found to be 0.75, 1.8967, 
2.135 and 11.769, 15.1816, 29.489 for free, immobilized and CLEC laccase, 
respectively. 
Keywords: Catechin; Poly(allylamine); Laccase; CLEC; Substituted-enzyme 
mechanism 
Article Outline 
1. Introduction 
2. Materials and methods 
2.1. Materials  
2.2. Preparation of CLEC laccase  
2.3. Preparation of immobilized laccase  
2.4. Preparation of catechin conjugate  
2.5. Determination of laccase stability 
3. Results and discussions 
3.1. Characterisation of CLEC laccase  
3.2. Effect of enzyme concentration  
3.3. Effect of substrate concentration  
3.4. Effect of temperature on initial rate  
3.5. Reaction mechanism  
3.6. Stability of laccase 
4. Conclusion 
References 
 
 
 
 
 
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Corresponding authors. Tel.: +91 3762370012; fax: +91 3762370011.
 
1
 Tel.: +91 3762370012; fax: +91 3762370011. 
Chemical Engineering Journal 
Volume 163, Issues 1-2, 15 September 2010, Pages 86-92 
Page 3 of 3ScienceDirect - Chemical Engineering Journal : Kinetics and mechanism on laccase catal...
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