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ARS Home » Midwest Area » Peoria, Illinois » National Center for Agricultural Utilization Research » Renewable Product Technology Research » Research » Publications at this Location » Publication #306948
Title: Purification and characterization of a cold-active lipase from Pichia lynferdii Y-7723: pH-dependant activity deviation

Author
item BAE, JAE-HAN - Kyungpook National University
item KWON, MI-HYUN - Kyungpook National University
item KIM, IN-HWAN - Korea University
item Hou, Ching
item KIM, HAK-RYUL - Kyungpook National University

Submitted to: Journal of Biotechnology and Bioprocess Engineering
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 7/18/2014
Publication Date: 11/20/2014
Publication URL: http://handle.nal.usda.gov/10113/60472
Citation: Bae, J., Kwon, M., Kim, I., Hou, C.T., Kim, H. 2014. Purification and characterization of a cold-active lipase from Pichia lynferdii Y-7723: pH-dependant activity deviation. Journal of Biotechnology and Bioprocess Engineering. 19(5):851-857.

Interpretive Summary: Lipase is one of the most important enzymes used in a broad range of industrial applications. For application in restricted reaction conditions, lipases require special characteristics such as: thermo stability, alkaline, acidic, and cold-activity. In our previous study, we screened several mesophilic yeasts for the production of extracellular cold-active lipase and reported the identification of a novel cold-active lipase produced from Pichia lynferdii NRRL Y-7723 [J. Agric. Food Chem. 58: 1322-1326. 2010]. In addition, we achieved remarkable increase of lipase production from this strain over 10 times compared to that in normal conditions by optimization study [J. Agric. Food Chem. 61: 882-886. 2013]. In this study, we conducted purification and characterization of the cold-active lipase from Pichia lynferdii NRRL Y-7723. We purified the cold active lipase to 33 purification fold using chromatographic techniques. The purified lipase represented maximum lipolytic activity at 15oC and the maximum activity was highly dependent on pH. The results of this study may also be used in the preparation of functional/health foods and improve the health and nutrition of humankind.

Technical 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, cold-active 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 a 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. The purified lipase represented maximum lipolytic activity at 15oC and the maximum activity was highly dependent on pH.