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Immobilized Phospholipase A1-Catalyzed Preparation of l -α-Glycerylphosphorylcholine from Phosphatidylcholine

Authors
Song, Y.Roh, S.Hwang, J.Chung, M.-Y.Kim, I.-H.Kim, B.H.
Issue Date
2020
Publisher
American Chemical Society
Keywords
cognitive enhancer; immobilization; interfacial activation; l -α-glycerylphosphorylcholine; phospholipase A1
Citation
Journal of Agricultural and Food Chemistry, v.68, no.44, pp.12375 - 12383
Indexed
SCIE
SCOPUS
Journal Title
Journal of Agricultural and Food Chemistry
Volume
68
Number
44
Start Page
12375
End Page
12383
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/130776
DOI
10.1021/acs.jafc.0c06381
ISSN
0021-8561
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.
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Kim, In Hwan
보건과학대학 (바이오시스템의과학부)
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