Enzymatic synthesis of structured lipids using a novel cold-active lipase from Pichia lynferdii NRRL Y-7723
- Authors
- 김학렬; Ching T. H; 이기택; 김병희; 김인환
- Issue Date
- Oct-2010
- Publisher
- ELSEVIER SCI LTD, THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD, ENGLAND, OXON, OX5 1GB
- Citation
- FOOD CHEMISTRY, v.122, no.3, pp 846 - 849
- Pages
- 4
- Journal Title
- FOOD CHEMISTRY
- Volume
- 122
- Number
- 3
- Start Page
- 846
- End Page
- 849
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/147875
- DOI
- 10.1016/j.foodchem.2010.03.067
- ISSN
- 0308-8146
1873-7072
- 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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