Abstract
Lipases are known for their high catalytic activity, unique substrate selectivity, and acyl chain length specificity. To investigate the acyl chain length specificity and catalytic properties of lipase, we developed a novel gas chromatography (GC) method by determining multiple substrates of saturated fatty acid ethyl esters with acyl chain lengths ranging from C4 to C18. The commercial immobilized lipase Novozym 435 (Candida antarctica lipase B) was selected as the model lipase. Acyl chain length specificity of Novozym 435 was determined with multiple substrates for three reactions (hydrolysis, esterification, and alcoholysis). Apparent Michaelis constant (Km) and Vmax for the reactions catalyzed by Novozym 435 were calculated, and the effect of organic solvent on lipase-catalyzed esterification and alcoholysis was further studied. The main advantages of this GC analytical method are using inexpensive reagents, simple detection operation, and a useful tool for simultaneously determining the acyl chain length specificity of lipase in catalytic hydrolysis, esterification, and alcoholysis reactions.
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