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Cited by 284Enzyme Catalysis and ImmobilizationEnzyme Production and CharacterizationAdvanced Biosensing Techniques and Applications

The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.

Facile, high efficiency immobilization of lipase enzyme on magnetic iron oxide nanoparticles via a biomimetic coating

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Ren, Yuhong, Rivera, Jose G, He, Lihong, Kulkarni, Harsha, Lee, Dong-Keun, Messersmith, Phillip B·2011·BMC Biotechnology
DOI 10.1186/1472-6750-11-63PMC PMC3212977
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Abstract

BACKGROUND: Immobilization of lipase on appropriate solid supports is one way to improve their stability and activity, and can be reused for large scale applications. A sample, cost- effective and high loading capacity method is still challenging. RESULTS: A facile method of lipase immobilization was developed in this study, by the use of polydopamine coated magnetic nanoparticles (PD-MNPs). Under optimal conditions, 73.9% of the available lipase was immobilized on PD-MNPs, yielding a lipase loading capacity as high as 429 mg/g. Enzyme assays revealed that lipase immobilized on PD-MNPs displayed enhanced pH and thermal stability compared to free lipase. Furthermore, lipase immobilized on PD-MNPs was easily isolated from the reaction medium by magnetic separation and retained more than 70% of initial activity after 21 repeated cycles of enzyme reaction followed by magnetic separation. CONCLUSIONS: Immobilization of enzyme onto magnetic iron oxide nanoparticles via poly-dopamine film is economical, facile and efficient.

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Figures

Figure 1 Two-step synthesis of lipase immobilized PD-MNPs. Two-step synthesis of lipase immobilized PD-MNPs.
Figure 1 Two-step synthesis of lipase immobilized PD-MNPs. Two-step synthesis of lipase immobilized PD-MNPs.CC BY · PubMed Central
Figure 2 XPS spectra. XPS spectra of MNPs (A), PD-MNPs (B), and lipase immobilized PD-MNPs (C).
Figure 2 XPS spectra. XPS spectra of MNPs (A), PD-MNPs (B), and lipase immobilized PD-MNPs (C).CC BY · PubMed Central
Figure 3 SEM and TEM spectra. SEM (left column) and TEM (right column) images of MNPs (A), PD-MNPs (B), and lipase immobilized PD-MNPs (C). The PD-MNPs were prepared using 2.5 mg/ml initial dopamine and lipase immobilization performed using 5 mg/ml initial lipase and 10 mg/ml PD-MNPs concentration.
Figure 3 SEM and TEM spectra. SEM (left column) and TEM (right column) images of MNPs (A), PD-MNPs (B), and lipase immobilized PD-MNPs (C). The PD-MNPs were prepared using 2.5 mg/ml initial dopamine and lipase immobilization performed using 5 mg/ml initial lipase and 10 mg/ml PD-MNPs concentration.CC BY · PubMed Central
Figure 4 Magnetic isolation of PD-MNP. Photographs of an aqueous suspension of PD-MNPs before (right) and after (left) magnetic isolation.
Figure 4 Magnetic isolation of PD-MNP. Photographs of an aqueous suspension of PD-MNPs before (right) and after (left) magnetic isolation.CC BY · PubMed Central
Figure 5 The effect of temperature on the activity of free and immobilized lipase. Activity was measured at 37°C after treatment for 1 hour in phosphate buffer (10 mM, pH 7.0) at the temperatures indicated. The PD-MNPs were prepared using 2.5 mg/ml initial dopamine and lipase immobilization performed using 5 mg/ml initial lipase and 10 mg/ml PD-MNPs concentration.
Figure 5 The effect of temperature on the activity of free and immobilized lipase. Activity was measured at 37°C after treatment for 1 hour in phosphate buffer (10 mM, pH 7.0) at the temperatures indicated. The PD-MNPs were prepared using 2.5 mg/ml initial dopamine and lipase immobilization performed using 5 mg/ml initial lipase and 10 mg/ml PD-MNPs concentration.CC BY · PubMed Central
Figure 6 The effect of pH on the activity of free and immobilized lipase. The effect of pH on the activity of free (A) and immobilized (B) lipase. The samples were pre-incubated in phosphate buffer (10 mM) at the pH values and times indicated before determining enzyme activity at pH 7.0 and 37°C. The PD-MNPs were prepared using 2.5 mg/ml initial dopamine and lipase immobilization performed using 5 mg/ml initial lipase and 10 mg/ml PD-MNPs concentration.
Figure 6 The effect of pH on the activity of free and immobilized lipase. The effect of pH on the activity of free (A) and immobilized (B) lipase. The samples were pre-incubated in phosphate buffer (10 mM) at the pH values and times indicated before determining enzyme activity at pH 7.0 and 37°C. The PD-MNPs were prepared using 2.5 mg/ml initial dopamine and lipase immobilization performed using 5 mg/ml initial lipase and 10 mg/ml PD-MNPs concentration.CC BY · PubMed Central
Figure 7 The activity of immobilized lipase after multiple cycles of magnetic isolation and reuse. Activity of lipase immobilized PD-MNPs after multiple cycles of magnetic isolation and reuse. The PD-MNPs were prepared using 2.5 mg/ml initial dopamine and lipase immobilization performed using 5 mg/ml initial lipase and 10 mg/ml PD-MNPs concentration. The total elapsed time of the experiment was less than 10 hours.
Figure 7 The activity of immobilized lipase after multiple cycles of magnetic isolation and reuse. Activity of lipase immobilized PD-MNPs after multiple cycles of magnetic isolation and reuse. The PD-MNPs were prepared using 2.5 mg/ml initial dopamine and lipase immobilization performed using 5 mg/ml initial lipase and 10 mg/ml PD-MNPs concentration. The total elapsed time of the experiment was less than 10 hours.CC BY · PubMed Central

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Metadata

Authors
Ren, Y., Rivera, J. G., He, L., Kulkarni, H., Lee, D.-K., & Messersmith, P. B.
Affiliations
  • East China University of Science and Technology (CN)
  • Northwestern University (US)
Corresponding author
  • Ren, Yuhong
  • Messersmith, Phillip B
ORCID
Venue
BMC Biotechnology
Publisher
Springer Science and Business Media LLC
Published
2011-06-08
Volume
11
Issue
1
Pages
63-63
ISSN
1472-6750 (ISSN-L)
DOI
10.1186/1472-6750-11-63
PMC
PMC3212977
OpenAlex
W2165613512
Cited by
284
References
23
Citations by year
2026: 4 · 2025: 8 · 2024: 21 · 2023: 13 · 2022: 14 · 2021: 12 · 2020: 16 · 2019: 19 · 2018: 25 · 2017: 22 · 2016: 38 · 2015: 25 · 2014: 29 · 2013: 20 · 2012: 16
FWCI
8.71
Type
journal article
Language
en
Open access
Licence
Locations
  • BMC Biotechnology (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
  • eScholarship (California Digital Library) (submittedVersion)
  • eScholarship (California Digital Library) (submittedVersion, cc-by)
Funders
  • National Institutes of Health
  • National Institute of Dental and Craniofacial Research (R37DE014193)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Advanced Biosensing Techniques and Applications
Keywords
lipase immobilization, magnetic iron oxide nanoparticles, polydopamine coating, biomimetic coatings, enzyme loading capacity, enzyme stability, magnetic separation, enzyme reusability
MeSH terms
Dopamine, Enzymes, Immobilized, Ferric Compounds, Hydrogen-Ion Concentration, Lipase, Polymers, Temperature, Biomimetic Materials, Magnetite Nanoparticles

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