Purification and characterization of a cold-active lipase from Pichia lynferdii Y-7723: pH-dependant activity deviation

Abstract

Lipases with abnormal functionalities such as high thermostability and optimal activity at extreme conditions gain special attentions because of their applicability in the restricted reaction conditions. In particular, coldactive lipases have gained special attentions in various industrial fields such as washer detergent, pharmaceutical catalyst, and production of structured lipid. However, production of cold-active lipase is mostly found from psychrophilic microorganisms. Recently we found a novel cold-active lipase from Pichia lynferdii Y-7723 which is mesophilic yeast strain. In this study, we purified the cold active lipase and the enzyme was further characterized in several parameters. The enzyme was purified with 33 purification fold using chromatographic techniques and the purified lipase represented maximum lipolytic activity at 15A degrees C and the maximum activity was highly dependent on pH.