Immobilized Phospholipase A1-Catalyzed Preparation of l -α-Glycerylphosphorylcholine from Phosphatidylcholine
DC Field | Value | Language |
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dc.contributor.author | Song, Y. | - |
dc.contributor.author | Roh, S. | - |
dc.contributor.author | Hwang, J. | - |
dc.contributor.author | Chung, M.-Y. | - |
dc.contributor.author | Kim, I.-H. | - |
dc.contributor.author | Kim, B.H. | - |
dc.date.accessioned | 2021-12-10T09:44:01Z | - |
dc.date.available | 2021-12-10T09:44:01Z | - |
dc.date.created | 2021-08-31 | - |
dc.date.issued | 2020 | - |
dc.identifier.issn | 0021-8561 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/130776 | - |
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. © 2020 American Chemical Society. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | American Chemical Society | - |
dc.subject | Biocatalysts | - |
dc.subject | Catalyst activity | - |
dc.subject | Hydrolysis | - |
dc.subject | Phase separation | - |
dc.subject | Biocatalysis | - |
dc.subject | Lewatit vp oc 1600 | - |
dc.subject | Optimal conditions | - |
dc.subject | Phosphatidylcholine | - |
dc.subject | Phosphocholine | - |
dc.subject | Phospholipases | - |
dc.subject | Positional specificity | - |
dc.subject | Response surface methodology | - |
dc.subject | Catalysis | - |
dc.subject | fungal protein | - |
dc.subject | glycerophosphorylcholine | - |
dc.subject | immobilized enzyme | - |
dc.subject | phosphatidylcholine | - |
dc.subject | phospholipase A1 | - |
dc.subject | biocatalysis | - |
dc.subject | chemistry | - |
dc.subject | enzymology | - |
dc.subject | Eurotiales | - |
dc.subject | hydrolysis | - |
dc.subject | Biocatalysis | - |
dc.subject | Enzymes, Immobilized | - |
dc.subject | Eurotiales | - |
dc.subject | Fungal Proteins | - |
dc.subject | Glycerylphosphorylcholine | - |
dc.subject | Hydrolysis | - |
dc.subject | Phosphatidylcholines | - |
dc.subject | Phospholipases A1 | - |
dc.title | Immobilized Phospholipase A1-Catalyzed Preparation of l -α-Glycerylphosphorylcholine from Phosphatidylcholine | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kim, I.-H. | - |
dc.identifier.doi | 10.1021/acs.jafc.0c06381 | - |
dc.identifier.scopusid | 2-s2.0-85095674379 | - |
dc.identifier.bibliographicCitation | Journal of Agricultural and Food Chemistry, v.68, no.44, pp.12375 - 12383 | - |
dc.relation.isPartOf | Journal of Agricultural and Food Chemistry | - |
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.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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.keywordPlus | fungal protein | - |
dc.subject.keywordPlus | glycerophosphorylcholine | - |
dc.subject.keywordPlus | immobilized enzyme | - |
dc.subject.keywordPlus | phosphatidylcholine | - |
dc.subject.keywordPlus | phospholipase A1 | - |
dc.subject.keywordPlus | biocatalysis | - |
dc.subject.keywordPlus | chemistry | - |
dc.subject.keywordPlus | enzymology | - |
dc.subject.keywordPlus | Eurotiales | - |
dc.subject.keywordPlus | hydrolysis | - |
dc.subject.keywordPlus | Biocatalysis | - |
dc.subject.keywordPlus | Enzymes, Immobilized | - |
dc.subject.keywordPlus | Eurotiales | - |
dc.subject.keywordPlus | Fungal Proteins | - |
dc.subject.keywordPlus | Glycerylphosphorylcholine | - |
dc.subject.keywordPlus | Hydrolysis | - |
dc.subject.keywordPlus | Phosphatidylcholines | - |
dc.subject.keywordPlus | Phospholipases A1 | - |
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 | - |
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