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Immobilized phospholipase A1-catalyzed preparation of L-αglycerylphosphorylcholine from phosphatidylcholine

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dc.contributor.authorSong, Yejin-
dc.contributor.authorRoh, Seoye-
dc.contributor.authorHwang, Jihyun-
dc.contributor.authorChung, Min-Yu-
dc.contributor.authorKim, In-Hwan-
dc.contributor.authorKim, Byung Hee-
dc.date.available2021-02-22T05:21:14Z-
dc.date.created2021-01-21-
dc.date.issued2020-11-
dc.identifier.issn0021-8561-
dc.identifier.urihttps://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/1056-
dc.description.abstractThis study sought to prepare a cognitive enhancer L-α-glycerylphosphorylcholine (L-α-GPC) using an immobilized Lecitase Ultra (LU, phospholipase A1) to catalyze the hydrolysis of soy phosphatidylcholine (PC). Immobilization of LU on Lewatit VP OC 1600 provided the highest fixation level (83.1 g/100 g) and greatest catalytic activity achieving 100 g/100 g L-α-GPC within 20 h and was therefore selected as the optimal system for biocatalysis. Immobilization of LU increased its positional specificity compared to free LU, as shown by a decrease in the production of the phosphocholine byproduct. Under the optimal conditions determined by response surface methodology, PC was completely hydrolyzed to L-α-GPC and required a simple purification via phase separation of the biphasic media to obtain a yield of ∼26.4 g L-α-GPC from 100 g PC, with a purity of 98.5 g/100 g. Our findings suggest a possibility of using the immobilized LU as a new biocatalyst for the L-α-GPC production. © XXXX American Chemical Society.-
dc.language영어-
dc.language.isoen-
dc.publisherAmerican Chemical Society-
dc.titleImmobilized phospholipase A1-catalyzed preparation of L-αglycerylphosphorylcholine from phosphatidylcholine-
dc.typeArticle-
dc.contributor.affiliatedAuthorSong, Yejin-
dc.contributor.affiliatedAuthorKim, Byung Hee-
dc.identifier.doi10.1021/acs.jafc.0c06381-
dc.identifier.scopusid2-s2.0-85095674379-
dc.identifier.wosid000589379300019-
dc.identifier.bibliographicCitationJournal of Agricultural and Food Chemistry, v.68, no.44, pp.12375 - 12383-
dc.relation.isPartOfJournal of Agricultural and Food Chemistry-
dc.citation.titleJournal of Agricultural and Food Chemistry-
dc.citation.volume68-
dc.citation.number44-
dc.citation.startPage12375-
dc.citation.endPage12383-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaAgriculture-
dc.relation.journalResearchAreaChemistry-
dc.relation.journalResearchAreaFood Science & Technology-
dc.relation.journalWebOfScienceCategoryAgriculture, Multidisciplinary-
dc.relation.journalWebOfScienceCategoryChemistry, Applied-
dc.relation.journalWebOfScienceCategoryFood Science & Technology-
dc.subject.keywordPlusBiocatalysts-
dc.subject.keywordPlusCatalyst activity-
dc.subject.keywordPlusHydrolysis-
dc.subject.keywordPlusPhase separation-
dc.subject.keywordPlusBiocatalysis-
dc.subject.keywordPlusLewatit vp oc 1600-
dc.subject.keywordPlusOptimal conditions-
dc.subject.keywordPlusPhosphatidylcholine-
dc.subject.keywordPlusPhosphocholine-
dc.subject.keywordPlusPhospholipases-
dc.subject.keywordPlusPositional specificity-
dc.subject.keywordPlusResponse surface methodology-
dc.subject.keywordPlusCatalysis-
dc.subject.keywordAuthorCognitive enhancer-
dc.subject.keywordAuthorImmobilization-
dc.subject.keywordAuthorInterfacial activation-
dc.subject.keywordAuthorL-α-glycerylphosphorylcholine-
dc.subject.keywordAuthorPhospholipase A1-
dc.identifier.urlhttps://pubs.acs.org/doi/10.1021/acs.jafc.0c06381-
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