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Purification and characterization of phosphatidylcholine-specific phospholipase C from Spinach.
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- Authors
- Advisor
- 박관화
- Issue Date
- 2004
- Publisher
- 서울대학교 대학원
- Keywords
- 시금치 ; Phosphatidylcholine-specific phospholipase c (pc-plc) ; 인지질 ; Spinach ; Phosphatidylcholine-specific phospholipase C (PC-PLC) ; Phospholipid ; Frozen storage
- Description
- Thesis (master`s)--서울대학교 대학원 :농생명공학부,2004.
- Abstract
- To investigate the influence of the phospholipid degrading enzymesfor the quality of spinach
during blanching and frozen storage, phosphatidylcholine-specific phospholipase C (PC-PLC) was
partially purified from spinach and charaterized. The extract of spinach was heated at 50℃ and
fractionated with ammonium sulfate between 10% and 60% saturation. A series of ion exchange
chromatographies and affinity chromatography such as Q-sepharose, ConA-sepharose and SPsepharose
chromatography, were applied to obtain the partially purified enzyme. Then the columns
of Superdex 200 and Superose 12 connected in tandem were used for further purification. The
apparent molecular weight of PC-PLC was determined to be about 13,000 Da by SDS-PAGE and MALDITOF
MASS. The enzyme showed higher activity toward phosphatidylcholine than phosphatidylinositol
and phosphatidylethanolamine. The optimum temperature and pH were 60℃, pH 7.0 respectively. The
specific activity of PC-PLC was about 12mU/mg. A possible model was proposed in which the
thermostable phosphatidylcholine-specific phospholipase C could influence the quality of spinach
during the frozen storage.
- Language
- English
- URI
- http://dcollection.snu.ac.kr:80/jsp/common/DcLoOrgPer.jsp?sItemId=000000055176
https://hdl.handle.net/10371/67589
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