The present study demonstrates the effect of light irradiation on the esterification of oleic acid catalyzed by immobilized Pseudomonas cepacia lipase. The reaction rates of all the experiments under light irradiation were found to be higher than dark conditions. The kinetics of reactions supported the Ping‐Pong Bi‐Bi mechanism with dead end inhibition by both the alcohol and acid substrates. Moreover, circular dichroism (CD) spectroscopy was used to analyze the effect of light on lipase enzyme. The CD spectroscopic studies confirmed that the conformational changes in the secondary structure of the lipase enzyme increased the reaction rate of light‐illuminated experiments, which might have opened up the active sites of enzymes and thus, resulted in higher reaction rates compared to dark reactions. These results have successfully demonstrated that the light illumination positively influenced the rate of P. cepacia enzyme‐catalyzed esterification reactions.
This paper demonstrates Pseudomonas cepacia lipase catalyzed hydrolysis of p-nitrophenyl palmitate under irradiation of light with wavelengths of 250-750 nm. The reaction follows Michaelis-Menten Kinetics and the light irradiation increases the overall rate of hydrolysis. Using Lineweaver-Burk plot K M and V max values for the reaction in presence of light are found to be 39.07 and 66.67 mM/min/g, respectively; while for the same reaction under dark condition, the values are 7.08 and 10.21 mM/min/g. The linear form of enzyme dependent rate of reaction confirms that no mass-transfer limitations are present and the reaction is a kinetically controlled enzymatic reaction.
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