Abstract
Chemical modification of soybean lipoxygenase (LG) by N-acyloxysuccinimides (1) and the enzyme reaction of free linolic acid in a hexane-water biphasic system were studied.
Non-modified LG showed no enzyme activity in the Biphasic system due to denaturation of the enzyme. However, modified LG gave enzyme activity in the order of CN=8>6>4>2 [CN : carbon number of the acyl group in (1)]. That is, activity in the biphasic system increased with increasing the additional hydrophobicity of LG by modification. The stability of modified LG in the biphasic system was in the order of CN=2>4>6>8. This may possible be due to conformational change in the enzyme by modification. The products were determined by HPLC and GC-MS.
