Evidence map›Paper›PMID 37093529›Full record

ArticleApplied biochemistry and biotechnology2023

Immobilization of Bio-imprinted Phospholipase D and Its Catalytic Behavior for Transphosphatidylation in the Biphasic System.

Xia Zhao, Meijing Guo, Xian Li, Bo Liu, Binglin Li, Jiao Wang

Abstract read
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In one paragraph

Article in Applied biochemistry and biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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

3 citing papers in PubMed.

  1. Article
  2. Immobilization of Phospholipase D on FeMolecules (Basel, Switzerland) · 2025
    Article
  3. 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.

Xia ZhaoShaanxi Key Laboratory of Catalysis, School of Chemistry and Environment Science, Shaanxi University of Technology, No.1 Dongyihuan Road, Hanzhong, Shaanxi, 723001, China.
Meijing GuoCollege of Food Science and Engineering, Northwest University, Xi'an, China.
Xian LiCollege of Food Science and Engineering, Northwest University, Xi'an, China.
Bo LiuShaanxi Key Laboratory of Catalysis, School of Chemistry and Environment Science, Shaanxi University of Technology, No.1 Dongyihuan Road, Hanzhong, Shaanxi, 723001, China.
Binglin LiCollege of Food Science and Engineering, Northwest University, Xi'an, China. libinglin@nwu.edu.cn.ORCID http://orcid.org/0000-0002-6409-0784
Jiao WangCollege of Food Science and Engineering, Northwest University, Xi'an, China. jiao.wang@bioquant.uni-heidelberg.de.

Funding

Bilimsel Araştirma Projeleri Birimi, Istanbul Üniversitesi 2021JQ-750National Natural Science Foundation of China for Young Scholars 22108227Natural Science Foundation of Shaanxi Provincial Department of Education 2023-JC-YB-092Shaanxi Association for Science and Technology for Young Scholars 20220201
6 · The paper itself

Abstract

Phospholipase D (PLD) with the higher transphosphatidylation activity was screened from Streptomyces sp. LD0501 basing on the protoplast mutagenesis technology. Then, it was successfully bio-imprinted to form a hyperactivated structure and rigidified by the intramolecular cross-linking, which was immobilized on the nonporous nanoscale silica. Characterization techniques were employed to investigate the structure and physicochemical properties of the catalysts, including Fourier transform infrared (FTIR) spectra and scanning electron microscopy (SEM) analysis. Transphosphatidylation activity and selectivity were improved significantly when immobilized PLD was used. The maximum yield for the production of phosphatidylserine (PS) reached 97% and the side reaction, the hydrolysis, was minimized. These results were further confirmed by the nuclear magnetic resonance (NMR) and mass spectrometry (MS) analysis. The imprint-induced characteristics of PLD was successfully "remembered" even in the present of much water. In addition, this immobilized hyperactivated PLD showed the excellent operational stabilities and environmental tolerances.

Indexed as

Phospholipase DCatalysisMagnetic Resonance SpectroscopyPhosphatidylserinesWaterPhosphatidylserinesPhospholipase DWaterBio-imprintImmobilizationMutagenesisPhosphatidylserinePhospholipase D

Identifiers

PMID37093529

What OpenQuestion holds

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Registered trials

None linked

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.