Enzymatic synthesis of structured lipids using a novel cold-active lipase from Pichia lynferdii NRRL Y-7723
- Authors
- Kim, Hak-Ryul; Hou, Ching T.; Lee, Ki-Teak; Kim, Byung Hee; Kim, In-Hwan
- Issue Date
- 1-10월-2010
- Publisher
- ELSEVIER SCI LTD
- Keywords
- Acidolysis; Borage oil; Caprylic acid; Enzyme loading; Novel lipase; Regiospecifity; Structured lipids; Temperature
- Citation
- FOOD CHEMISTRY, v.122, no.3, pp.846 - 849
- Indexed
- SCIE
SCOPUS
- Journal Title
- FOOD CHEMISTRY
- Volume
- 122
- Number
- 3
- Start Page
- 846
- End Page
- 849
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/115536
- DOI
- 10.1016/j.foodchem.2010.03.067
- ISSN
- 0308-8146
- 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 degrees C. (C) 2010 Elsevier Ltd. All rights reserved.
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