Evidence map›Paper›PMID 39601977›Full record

ArticleApplied biochemistry and biotechnology2025

A Haloalkane Dehalogenase DhaA Nanoparticle Based on Pullulan Conjugation and Polyethyleneimine Adsorption.

Lijuan Shen, Lijia Hu, Jinming Qi, Weili Yu, Aiqin Luo, Tao Hu

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

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

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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

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Lijuan ShenKey Laboratory of Molecular Medicine and Biotherapy, School of Life Science, Beijing Institute of Technology, 100081, Beijing, China.
Lijia HuSchool of International Relations, Beijing Language and Culture University, 100083, Beijing, China.
Jinming QiState Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, 100190, Beijing, China.
Weili YuState Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, 100190, Beijing, China.
Aiqin LuoKey Laboratory of Molecular Medicine and Biotherapy, School of Life Science, Beijing Institute of Technology, 100081, Beijing, China. aqluobit@163.com.
Tao HuState Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, 100190, Beijing, China. thu@home.ipe.ac.cn.ORCID http://orcid.org/0000-0002-6681-159X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Haloalkane dehalogenase DhaA is a member of the α/β-hydrolase superfamily and can degrade the halogenated compounds. However, the enzyme could not tolerate harsh and extreme environmental conditions, such as high temperature, extreme pH, and hypersaline, which limits its practical applications. Pullulan is a hydrophilic polysaccharide and acts as an additive to improve the enzyme stability. Polyethyleneimine (PEI) is a protein stabilizer and a polymer with a high density of ionizable amino groups. In the present study, DhaA was covalently conjugated with acetylated pullulan and adsorbed with PEI by electrostatic interactions to form nanoparticles (PEI-pullulan-DhaA). As compared with DhaA, PEI-pullulan-DhaA essentially maintained the enzymatic activity of DhaA, along with slight change in the kinetic parameters and enzyme conformation. The conjugated pullulan tends to form a large hydrated layer around DhaA. PEI, a cationic polymer, generated an amphiphilic microenvironment around DhaA. Pullulan conjugation and PEI adsorption could significantly improve the stability of DhaA against high temperature and low pH by structural stabilization of DhaA. PEI-pullulan-DhaA could also tolerate the hypersaline, organic solvents, and long-term storage. Thus, PEI-pullulan-DhaA has a strong environmental stability and is promising for industrial and environmental applications.

Indexed as

GlucansHydrolasesNanoparticlesPolyethyleneimineAdsorptionEnzymes, ImmobilizedEnzyme StabilityHydrogen-Ion ConcentrationKineticsEnzymes, ImmobilizedGlucanshaloalkane dehalogenaseHydrolasesPolyethyleneiminepullulanDhaAEnzyme stabilityNanoparticlesPolyethyleneiminePullulan

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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.