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Competitive substrate inhibition of amyloglucosidase from Rhizopus sp. by vanillin and curcumin

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Bio_01_06
 
Title Competitive substrate inhibition of amyloglucosidase from Rhizopus sp. by vanillin and curcumin
 
Creator Ramaiah, Sivakumar
Giriyapura, R. Vijayakumar
Balaraman, Manohar
Soundar, Divakar
 
Subject 04 Fermentation Technology
16 Enzyme Chemistry
 
Description Kinetic studies of two glucosylation reactions catalyzed by an amyloglucosidase from Rhizopus sp. leading to the synthesis of vanillin-a/b-D-glucoside from D-glucose and vanillin and curcumin-bis-a-D-glucoside from D-glucose and curcumin were investigated in detail. Initial reaction rates were determined from kinetic runs involving different concentrations of Dglucose and vanillin (5 mM to 0.1 M) or D-glucose and curcumin (5 mM to 0.1 M). Graphical double reciprocal plots showed that the kinetics of the two enzyme catalyzed reactions exhibited Ping-Pong Bi-Bi mechanism where competitive substrate inhibition by vanillin/curcumin led to dead-end amyloglucosidasevanillin/curcumin complexes at higher concentrations of vanillin/curcumin. An attempt to obtain the best fit of this kinetic model through computer simulation yielded in good approximation, the values of four important kinetic parameters, vanillin-a/b-D-glucoside: kcat/35.09/3.2105Mh1/mg, Ki/10.59/1.1 mM, Km D-glucose/60.09/6.2 mM, Km vanillin/50.09/4.8 mM; curcumin-bis-a-D-glucoside:kcat/6.079/0.58 105Mh1/mg, Ki/3.09/0.28 mM, Km D-glucose/10.09/0.9 mM, Km curcumin/4.69/0.5 mM.
 
Date 2006-01
 
Type Article
PeerReviewed
 
Format application/pdf
 
Language en
 
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Identifier http://ir.cftri.com/573/1/Biocatalysis_and_Biotransformation%2C_July-August_2006_24%284%29_299-305.pdf
Ramaiah, Sivakumar and Giriyapura, R. Vijayakumar and Balaraman, Manohar and Soundar, Divakar (2006) Competitive substrate inhibition of amyloglucosidase from Rhizopus sp. by vanillin and curcumin. Biocatalysis and Biotransformation, 24 (4). pp. 299-305. (Submitted)