Dataset Information

Highly efficient preparation of 1-lysophosphatidylcholine via high proportion of Novozym® 435 (lipase B from Candida antarctica)-catalyzed ethanolysis.

ABSTRACT: Efficient preparation methods for 1-lysophosphatidylcholine (1-LPC), a physiologically important compound, are lacking. Here, we established a method for 1-LPC preparation via Novozym® 435 (a lipase B from Candida antarctica)-catalyzed ethanolysis. Novozym® 435 showed sn-1 regiospecificity to phosphatidylcholine, although it does not exhibit regiospecificity to triacylglycerol. In particular, quantitative 1-LPC yields (96.5 ± 0.2 mol%) were reliably obtained in the presence of Novozym® 435 (100 wt% of PC), 97 % ethanol, in 72 h at 40 °C. During the reaction, acyl migration from 1-LPC to 2-LPC was rare. This novel synthetic method is expected to expand the practical applications of 1-LPC.

SUBMITTER: Yasuda S

PROVIDER: S-EPMC7393457 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Highly efficient preparation of 1-lysophosphatidylcholine via high proportion of Novozym® 435 (lipase B from Candida antarctica)-catalyzed ethanolysis.

Yasuda Sayumi S Yamamoto Yukihiro Y

Biotechnology reports (Amsterdam, Netherlands) 20200722

Efficient preparation methods for 1-lysophosphatidylcholine (1-LPC), a physiologically important compound, are lacking. Here, we established a method for 1-LPC preparation via Novozym® 435 (a lipase B from Candida antarctica)-catalyzed ethanolysis. Novozym® 435 showed sn-1 regiospecificity to phosphatidylcholine, although it does not exhibit regiospecificity to triacylglycerol. In particular, quantitative 1-LPC yields (96.5 ± 0.2 mol%) were reliably obtained in the presence of Novo ...[more]

PMID: 32760663

Similar Datasets

Project description:BackgroundThe Lipase Engineering Database (LED) integrates information on sequence, structure and function of lipases, esterases and related proteins with the alpha/beta hydrolase fold. A new superfamily for Candida antarctica lipase A (CALA) was introduced including the recently published crystal structure of CALA. Since CALA has a highly divergent sequence in comparison to other alpha/beta hydrolases, the Lipase Engineering Database was used to classify CALA in the frame of the already established classification system. This involved the comparison of CALA to similar structures as well as sequence-based comparisons against the content of the LED.ResultsThe new release 3.0 (December 2009) of the Lipase Engineering Database contains 24783 sequence entries for 18585 proteins as well as 656 experimentally determined protein structures, including the structure of CALA. In comparison to the previous release 1 with 4322 protein and 167 structure entries this update represents a significant increase in data volume. By comparing CALA to representative structures from all superfamilies, a structure from the deacetylase superfamily was found to be most similar to the structure of CALA. While the alpha/beta hydrolase fold is conserved in both proteins, the major difference is found in the cap region. Sequence alignments between both proteins show a sequence similarity of only 15%. A multisequence alignment of both protein families was used to create hidden Markov models for the cap region of CALA and showed that the cap region of CALA is unique among all other proteins of the alpha/beta hydrolase fold. By specifically comparing the substrate binding pocket of CALA to other binding pockets of alpha/beta hydrolases, the binding pocket of Candida rugosa lipase was identified as being highly similar. This similarity also applied to the lid of Candida rugosa lipase in comparison to the potential lid of CALA.ConclusionThe LED serves as a valuable tool for the systematic analysis of single proteins or protein families. The updated release 3.0 was used for the evaluation of alpha/beta hydrolases. The HTML version of the database with new features is available at http://www.led.uni-stuttgart.de and provides sequences, structures and a set of analysis tools including phylogenetic trees and HMM profiles.

Dataset Information

Highly efficient preparation of 1-lysophosphatidylcholine via high proportion of Novozym® 435 (lipase B from Candida antarctica)-catalyzed ethanolysis.

Publications

Highly efficient preparation of 1-lysophosphatidylcholine via high proportion of Novozym® 435 (lipase B from <i>Candida antarctica</i>)-catalyzed ethanolysis.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets