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

Authors
Song, YejinRoh, SeoyeHwang, JihyunChung, Min-YuKim, In-HwanKim, Byung Hee
Issue Date
Nov-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
Journal Title
Journal of Agricultural and Food Chemistry
Volume
68
Number
44
Start Page
12375
End Page
12383
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/1056
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. © XXXX American Chemical Society.
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