Enzymatic synthesis of structured lipids using a novel cold-active lipase from Pichia lynferdii NRRL Y-7723 |
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| Authors: | Hak-Ryul Kim Ching T Hou Ki-Teak Lee Byung Hee Kim In-Hwan Kim |
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| Affiliation: | 1. Department of Animal Science and Biotechnology, Kyungpook National University, 702-701 Daegu, Republic of Korea;2. Microbial Genomic and Bioprocessing Research Unit, National Center for Agricultural Utilization Research, ARS, USDA, Peoria, IL 61604, USA;3. Department of Food Science and Technology, College of Agriculture, Chungnam National University, Daejon, Republic of Korea;4. Department of Food Science and Technology, Chung-Ang University, Ansung, Kyunggido 456-756, Republic of Korea;5. Department of Food and Nutrition, College of Health Science, Korea University, Chungneung-Dong, Sungbuk-Gu, Seoul 136-703, Republic of Korea |
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| 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. |
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| Keywords: | Acidolysis Borage oil Caprylic acid Enzyme loading Novel lipase Regiospecifity Structured lipids Temperature |
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