P14: A Super Lipase : The Engineering of Photobacterium Lipolyticum M37 Lipase For Efficient Production of Biodiesel

Lipases (EC 3.1.1.3) have been utilized for various biotechnological applications due to its multi-catalytic activity hydrolase and synthetase.  Because lipases have excellent esterification/trans-esterification activity and stability in non-aqueous medium, it can be also utilized to produce eco-friendly biodiesel from either triglyceride with short chain alcohols or animal fat, even from waste cooking oil, which can be an alternative to petroleum-based diesel fuels.  However, major problems in using lipases to catalyze the trans-esterification process for biodiesel production are that the lipase activity is lower than that of chemical catalysts and the lipase is easily deactivated even at low concentration of alcohol that needed for biodiesel production.  Furthermore, the relatively slower enzyme reaction rate hinder utilization of lipases for the biodiesel production in industry. For these reasons, researchers have attempted to improve a catalytic activity of lipase have relied on structure based rational design or directed evolution, and exploring a novel lipase from natural communities by the metagenomic approach.  Furthermore, The lipases were immobilized on various matrix to improve the activity, stability and substrates specificity. Despite all these efforts, increasing enzyme efficiency of lipase enzyme reactions is still hampered by intrinsic relationship between lipase and substrates.  Here, we designed a super lipase using the photobacterium lipolyticum M37 lipase as a template scaffold.  This engineered M37 lipase not only enhanced the catalytic activity but also shortened the biodiesel production time.  Therefore, our results suggest that our novel approaches can be useful platform technology for the production of biodiesel and biochemical in industry.