Immobilized phospholipase A1-catalyzed preparation of L-αglycerylphosphorylcholine from phosphatidylcholine
DC Field | Value | Language |
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dc.contributor.author | Song, Yejin | - |
dc.contributor.author | Roh, Seoye | - |
dc.contributor.author | Hwang, Jihyun | - |
dc.contributor.author | Chung, Min-Yu | - |
dc.contributor.author | Kim, In-Hwan | - |
dc.contributor.author | Kim, Byung Hee | - |
dc.date.available | 2021-02-22T05:21:14Z | - |
dc.date.issued | 2020-11 | - |
dc.identifier.issn | 0021-8561 | - |
dc.identifier.uri | https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/1056 | - |
dc.description.abstract | This 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.format.extent | 9 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | American Chemical Society | - |
dc.title | Immobilized phospholipase A1-catalyzed preparation of L-αglycerylphosphorylcholine from phosphatidylcholine | - |
dc.type | Article | - |
dc.publisher.location | United States | - |
dc.identifier.doi | 10.1021/acs.jafc.0c06381 | - |
dc.identifier.scopusid | 2-s2.0-85095674379 | - |
dc.identifier.wosid | 000589379300019 | - |
dc.identifier.bibliographicCitation | Journal of Agricultural and Food Chemistry, v.68, no.44, pp 12375 - 12383 | - |
dc.citation.title | Journal of Agricultural and Food Chemistry | - |
dc.citation.volume | 68 | - |
dc.citation.number | 44 | - |
dc.citation.startPage | 12375 | - |
dc.citation.endPage | 12383 | - |
dc.type.docType | Article | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Agriculture | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.relation.journalResearchArea | Food Science & Technology | - |
dc.relation.journalWebOfScienceCategory | Agriculture, Multidisciplinary | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Applied | - |
dc.relation.journalWebOfScienceCategory | Food Science & Technology | - |
dc.subject.keywordPlus | Biocatalysts | - |
dc.subject.keywordPlus | Catalyst activity | - |
dc.subject.keywordPlus | Hydrolysis | - |
dc.subject.keywordPlus | Phase separation | - |
dc.subject.keywordPlus | Biocatalysis | - |
dc.subject.keywordPlus | Lewatit vp oc 1600 | - |
dc.subject.keywordPlus | Optimal conditions | - |
dc.subject.keywordPlus | Phosphatidylcholine | - |
dc.subject.keywordPlus | Phosphocholine | - |
dc.subject.keywordPlus | Phospholipases | - |
dc.subject.keywordPlus | Positional specificity | - |
dc.subject.keywordPlus | Response surface methodology | - |
dc.subject.keywordPlus | Catalysis | - |
dc.subject.keywordAuthor | Cognitive enhancer | - |
dc.subject.keywordAuthor | Immobilization | - |
dc.subject.keywordAuthor | Interfacial activation | - |
dc.subject.keywordAuthor | L-α-glycerylphosphorylcholine | - |
dc.subject.keywordAuthor | Phospholipase A1 | - |
dc.identifier.url | https://pubs.acs.org/doi/10.1021/acs.jafc.0c06381 | - |
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