GEL MATRIX INFLUENCE ON HYDROLYSIS OF TRIGLYCERIDES BY IMMOBILIZED LIPASES

The hydrolytic activities and specificities of gel-entrapped C. cylind racae lipase (CCL) and R. arrhizus lipase (RAL) toward olive oil and t ributyrin were investigated. Lipases in hydrophobic gels with the long est chain lengths generally displayed highest activity. The optimal te mperature was 30-35 degrees C for free and 37-40 degrees C for gel-ent rapped lipases. The ratio of the activity on tributyrin to that of oli ve oil (expressed as T/O ratio), an indicator of substrate specificity , increased from 0.3 for free lipases to 12.3 +/- 2.3 for CCL lipase i n ENTP-2000-formed gel and 16.2 +/- 0.3 for RAL lipase in ENTP4000-for med gel.