Evidence map›Paper›PMID 41182440›Full record

ArticleBioresources and bioprocessing2025

Enzymatic synthesis of phosphatidyl-EPA/DHA using Candida antarctica lipase B immobilized on mesoporous MIL-88 A.

Yuhan Li, Guowei Wu, Zeqing Liu, Lingmei Dai, Dehua Liu, Wei Du

Abstract read
In one paragraph

Article in Bioresources and bioprocessing, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Yuhan LiKey Laboratory for Industrial Biocatalysis, Ministry of Education, Department of Chemical Engineering, Tsinghua University, Beijing, 100084, China.
Guowei WuKey Laboratory for Industrial Biocatalysis, Ministry of Education, Department of Chemical Engineering, Tsinghua University, Beijing, 100084, China.
Zeqing LiuKey Laboratory for Industrial Biocatalysis, Ministry of Education, Department of Chemical Engineering, Tsinghua University, Beijing, 100084, China.
Lingmei DaiKey Laboratory for Industrial Biocatalysis, Ministry of Education, Department of Chemical Engineering, Tsinghua University, Beijing, 100084, China.
Dehua LiuKey Laboratory for Industrial Biocatalysis, Ministry of Education, Department of Chemical Engineering, Tsinghua University, Beijing, 100084, China.
Wei DuKey Laboratory for Industrial Biocatalysis, Ministry of Education, Department of Chemical Engineering, Tsinghua University, Beijing, 100084, China. duwei@tsinghua.edu.cn.ORCID http://orcid.org/0000-0003-4094-210X

Funding

National Key Research and Development Program of China 2023YFA0914400National Natural Science Foundation of China 22178198
6 · The paper itself

Abstract

Mesoporous MIL-88A (Meso-MIL-88A) shows significant potential as an effective carrier for immobilizing large molecules such as lipases. This study investigates Meso-MIL-88A immobilized lipase for the catalysis of eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) incorporation into soybean phosphatidylcholine. Phosphatidyl-EPA and phosphatidyl-DHA are known for their superior health benefits and have garnered significant global attention. Firstly, we developed a novel and green water-washing strategy to synthesize Meso-MIL-88A, demonstrating its significant potential as an effective carrier for immobilizing large molecules such as lipases. Nitrogen adsorption/desorption and XPS analyses revealed that water as the eluent yielded larger average pore diameters and lower sulfur residue content compared to ethanol. This optimized Meso-MIL-88A carrier was used to immobilize Candida antarctica lipase B (CalB@Meso-MIL-88A), which was applied to the production of phosphatidyl-EPA and phosphatidyl-DHA. The immobilized CalB@Meso-MIL-88A exhibited exceptional catalytic efficiency, achieving an unprecedented sn-1 positional incorporation rate of 86.8% (44.2% EPA, 42.7% DHA) with 90% EPA/DHA-ethyl ester (EE) donors, while 97% DHA-EE resulted in a record-high 90.1% DHA incorporation at the sn-1 position. Kinetic studies and molecular docking simulations indicated a higher substrate affinity for DHA-EE, attributed to enhanced transfer efficiency of EPA/DHA-EE in organic solvent system. This study presents the first demonstration of the potential of Meso-MIL-88A for industrial lipase immobilization via this optimized route, offering an eco-friendly and highly efficient catalytic application for nutraceutical synthesis.

Indexed as

Immobilized lipaseKinetic studyMesoporous MIL-88A (Meso-MIL-88A)Molecular docking simulationPhosphatidyl EPA/DHA

Identifiers

PMID41182440
PMCPMC12583253

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.