Publication: Research - peer-review › Journal article – Annual report year: 2007
Kinetic study of sphingomyelin hydrolysis catalyzed by Clostridium perfringens phospholipase C was, at the first time, conducted for ceramide production. Ceramide has the major role in maintaining the water-retaining properties of the epidermis. Hence, it is of great commercial potential in cosmetic and pharmaceutical industries such as in hair and skin care products. The enzymatic hydrolysis of sphingomyelin has been proved to be a feasible method to produce ceramide. The kinetic performance of sphingomyelin hydrolysis in the optimal two-phase (water:organic solvent) reaction system was investigated to elucidate the possible reaction mechanism and also to further improve the hydrolysis performance. Enzyme in solution had less thermal stability than the enzyme powder and the immobilized enzyme. The thermal inactivation of phospholipase C in all the three forms did not follow the first order reaction at 65 °C. The reactions for both the soluble and immobilized enzymes followed Michaelis–Menten kinetics. Km's for the soluble and immobilized enzymes were 1.07 ± 0.32 and 1.26 ± 0.19 mM, respectively. The value of Vmax was markedly decreased by the immobilization without much change in Km, as if the immobilization functioned as the non-competitive inhibition. Ceramide as product activated the hydrolysis reaction, however, and its addition mainly caused the increase in the affinity of the enzyme–substrate complex.
|Citations||Web of Science® Times Cited: No match on DOI|
- Sphingomyelin, Ceramide, Phospholipase C, Kinetic, Thermal stability