‘Abstract book ES AND POLICES ION, STATI LE BLUE ECONOMY: PAOD USTUNAA, TOWARDS A. Comparative analysis of thermal and pH stability of Etroplus suratensis and Oreochromis mossambicus intestinal lipase Hari Sankar. H.S'., Prabhakaran, M.I !, Preetham, E.' and Babu Philip” ‘Kerala University of Fisheries and Ocean Studies, Panangad, Kerala, India “Department of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Kerala, India and survival of organisms in its natural habitat depends on their physiological and biochemical capabilities. Lipase enzyme is a naturally occurring pliable biocatalyst found in the stomach and pancreatic juice of animals and also produced by microorganisms. Lipases are able lo calalyze 4 wide range of bioconversion reactions like hydrolysis, eSterification, transesterification, alcoholysis, acidolysis and aminulysis. A vatiely of substances such a3 natural vils, synthetic triglycerides and esters of fatty acids are substrates of lipases. They have a broad spectrum of biotechnological applications. Lipase catalyzed trans esterification, hydrolysis and esterification are the important class of reactions in fats and oil industry, dairy industry, pharmaceuticals and bakery industry. Lipases are very peculiar as they hydrolyse fats into fatty acids and glycerol at the water-lipid interface and can reverse the reaction in non-aqueous media. Novel biotechnological applications, like biopolymer synthesis, biodiesel production, treatment of fat-containing waste effluents, synthesis of specific enantinmers pharmaceuticals and nutraceutical agents, have been established successfully. In the present study, the differences obtained in the thermal and pH stability profiles of lipase of Oreochromis mossambicus and Etroplus suratensis reveals that the former is able to perform lipolysis in a wide range of temperature and pH. The pH optimum for 0. mossambicus intestinal lipase has been estimated as 9.00. The intestinal lipase of E. suratensis possesses optimum activity in a range of pH from 8.5 to 9.5. The temperature optimum for O. mossambicus intestinal lipase is found to be 45°C, whereas it is 30°C for E. suratensis, The E. suratensis intestinal lipase is stable up to 35°C and beyond this temperature thermal denaturation of the enzyme starts and inactivation occurs. The thermal inactivation kinetics of O. mossambicus intestinal lipase showed that the enzyme is more stable below 50°C. In the present study, the O, mossambicus lipase is stable in the alkaline range with about 80% relative activity, The intestinal and hepatopancreatic lipase from E. suratensis showed maximum stability in the acidic to neutral pH. Thus 0. mossambicus can tolerate, adapt and survive wide fluctuations in the water temperature as well as pH. Such lipases Can be used in various industrial applications as they retain their activity fora broad physiochemical conditions. E troplus suratensis and Oreochromis mossambicus are promising species in the aquaculture. The fitness