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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 #252228
Title: Enzymatic Synthesis of Structured Lipids using a Novel Cold-Active Lipase from Pichia lynferdii NRRL Y-7723

Author
item KIM, HAK-RYUL - Kyungpook National University
item Hou, Ching
item LEE, KI-TEAK - Chungnam National University
item KIM, BYUNG HEE - Chung-Ang University
item KIM, IN-HWAN - Chungnam National University

Submitted to: Journal of Food Chemistry
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 5/26/2010
Publication Date: 6/7/2010
Citation: Kim, H., Hou, C.T., Lee, K., Kim, B., Kim, I. 2010. Enzymatic synthesis of structured lipids using a novel cold-active lipase from Pichia lynferdii NRRL Y-7723. Journal of Food Chemistry. 122:846-849.

Interpretive Summary: Lipase is one of the most important enzymes applied to the broad range of industrial application field. Lipases with abnormal functionality such as thermo stability, alkaline, acidic, cold-activity gain special attention because of their applicability in the restricted reaction conditions. In this study, six commercial lipases from different sources and a novel lipase we discovered from Pichia lynferdii were screened for their acidolysis activities. Commercial lipase, Lipozyme RM IM and our new lipase, NRRL Y-7723 lipase were selected to synthesize symmetrical structured lipid (SL). Both lipases showed 1,3-positional specificity toward the glycerol backbone of borage oil. The effects of enzyme loading and temperature on caprylic acid incorporation into the borage oil were investigated. The activity of NRRL Y-7723 lipase was higher than that of Lipozyme RM IM in the temperature range between 10 and 20°C. Results of this study may improve the health and nutrition of humankind.

Technical Abstract: Structured lipids (SL) were synthesized by the acidolysis of borage oil with caprylic acid using lipases. Six commercial lipases from different sources and a novel lipase from Pichia lynferdii NRRL Y-7723 were screened for their acidolysis activities and Lipozyme RM IM and NRRL Y-7723 lipase were selected to synthesize symmetrical SL since recently NRRL Y-7723 lipase was identified as a novel cold-active lipase. Both lipases showed 1,3-regiospecifity toward the glycerol backbone of borage oil. The effects of enzyme loading and temperature on caprylic acid incorporation into the borage oil were investigated. For Lipozyme RM IM and NRRL Y-7723 lipase, the incorporation of caprylic acid increased as enzyme loading increased up to 4% of total weight of the substrate, but significant increases were not observed when enzyme loading was further increased. The activity of NRRL Y-7723 lipase was higher than that of Lipozyme RM IM in the temperature range between 10 and 20°C.