Immobilization of Thermostable Lipase QLM on Core-Shell Structured Polydopamine-Coated Fe3O4 Nanoparticles

Wang, Chenhui; Han, Haobo; Jiang, Wei; Ding, Xin; Li, Quanshun; Li, Han

doi:10.3390/catal7020049

Cited by 19 publications

(6 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Enzyme was first immobilized on magnetic nanoparticles surface by Matsunaga and Kamiya [17]. Immobilizing lipase on magnetite will generate a nano-biocatalyst, which will grant the edge of better activity in harsh conditions and reusability [18].…”

Section: Introductionmentioning

confidence: 99%

Fe3O4-PDA-Lipase as Surface Functionalized Nano Biocatalyst for the Production of Biodiesel Using Waste Cooking Oil as Feedstock: Characterization and Process Optimization

et al. 2019

View full text Add to dashboard Cite

Synthesis of surface modified/multi-functional nanoparticles has become a vital research area of material science. In the present work, iron oxide (Fe3O4) nanoparticles prepared by solvo-thermal method were functionalized by polydopamine. The catechol groups of polydopamine at the surface of nanoparticles provided the sites for the attachment of Aspergillus terreus AH-F2 lipase through adsorption, Schiff base and Michael addition mechanisms. The strategy was revealed to be facile and efficacious, as lipase immobilized on magnetic nanoparticles grant the edge of ease in recovery with utilizing external magnet and reusability of lipase. Maximum activity of free lipase was estimated to be 18.32 U/mg/min while activity of Fe3O4-PDA-Lipase was 17.82 U/mg/min (showing 97.27% residual activity). The lipase immobilized on polydopamine coated iron oxide (Fe3O4_PDA_Lipase) revealed better adoptability towards higher levels of temperature/pH comparative to free lipase. The synthesized (Fe3O4_PDA_Lipase) catalyst was employed for the preparation of biodiesel from waste cooking oil by enzymatic transesterification. Five factors response surface methodology was adopted for optimizing reaction conditions. The highest yield of biodiesel (92%) was achieved at 10% Fe3O4_PDA_Lipase percentage concentration, 6:1 CH3OH to oil ratio, 37 °C temperature, 0.6% water content and 30 h of reaction time. The Fe3O4-PDA-Lipase activity was not very affected after first four cycles and retained 25.79% of its initial activity after seven cycles. The nanoparticles were characterized by FTIR (Fourier transfer infrared) Spectroscopy, XRD (X-ray diffraction) and TEM (transmission electron microscopy), grafting of polydopamine on nanoparticles was confirmed by FTIR and formation of biodiesel was evaluated by FTIR and GC-MS (gas chromatography-mass spectrometry) analysis.

show abstract

Section: Introductionmentioning

confidence: 99%

Fe3O4-PDA-Lipase as Surface Functionalized Nano Biocatalyst for the Production of Biodiesel Using Waste Cooking Oil as Feedstock: Characterization and Process Optimization

et al. 2019

View full text Add to dashboard Cite

show abstract

“…PDA‐coated magnetic nanoparticles with immobilized lipase QLM from Alcaligenes sp . with a loading of 21.4±1.47 mg g −1 was applied in the hydrolysis of 4‐nitrophenyl caprylate . The immobilized enzyme showed a better tolerance to temperature but exhibited significant activity decreases during eight reuses with a remaining activity of 10 %.…”

Section: Immobilized Enzymes As Catalystsmentioning

confidence: 99%

Polydopamine – its Prolific Use as Catalyst and Support Material

Molnár

2020

ChemCatChem

View full text Add to dashboard Cite

Polydopamine is a mussel-inspired functional material with a unique ability to form surface coatings. It is a green, environmentally benign product available very easily for a multitude of varied applications. This review attempts to collect useful information with respect to polydopamine-based catalytic studies with the use of polydopamine and modified polydopamine preparations loaded with varied catalytically active species including metal ions and metal particles. Major sections are about the use of polydopamine as catalyst material, utilization of immobilized enzymes, removal of toxic materials, results in organic synthesis, and fuel cell applications. A few examples of chiral catalysis and results of recycling studies are also treated. Data collected and analyzed indicate the importance and high potential of polydopamine-based catalysts in sustainable chemistry. of subunits attacked by an immobilized cyclohexeneamine (5) was suggested to be the transition state of CÀ C bond formation.Edouard et al. prepared catalyst 0.29 % PDA/PU by depositing PDA onto polyurethane foam (PU, 180 � 20 mg, 8 cm 3 ) and used it for the reduction of methylene blue (MB) with NaBH 4 . [48] Activities decreased gradually with repeated uses from 100 % to 35 % in run 11 but partial reactivation was achieved upon keeping the sample at 67°C for 8 h (55 % dropping below 10 % in run 13). Exposure to air at room temperature for six days proved to be somewhat more beneficial (90 % conversion in run 14 decreasing to 48 % in run 18). In a recent study they fabricated two oxidized PDA/PU samples and then loaded them with NaBH 4 . [49] One made by the usual method (dopamine/Tris, rt, 12 h, in air; sample PDA O2 PU), whereas the other was made by treating PU in a mixture of dopamine, NaOAc, and NaIO 4 (pH 5, rt, 24 h). The sample was dried (67°C) and washed thoroughly with water (PDA NaIO4 PU). Both products were dipped into an aqueous solution of NaBH 4 (0.1 M, 10 min) to afford boron contents of 2.37 and 2.11 wt%. The catalysts tested in the degradation of MB showed high activities with efficiencies of 97 % and 98 %, respectively (NaBH 4 /MB molar ratio 40, 177 mg and 209 mg catalysts, 25 min). During five reuses, the pH of the reaction medium increased because of boron loss (0.78 wt% and 0.81 wt%). The activity of PDA NaIO4 PU decreased to 89 % in run five. However, dipping the used sample into a 0.1 M NaBH 4 solution restored the original efficiency of 98 %. This, however, was only a temporary remedy, since a low efficiency of 60 % was measured in run 10. PDA was suggested by the authors to act as a redox mediator to prevent the hydrolysis/oxidation of immobilized borohydride.This formula (5) should be moved up and placed before the paragraph starting with "Edouard et al…"The Zuo group used PDA particles (avg. diameter 240 nm) to induce the reduction of MB and rhodamine B (RhB) with NaBH 4 . [50] Quinone moieties of PDA were assumed to channel electrons from NaBH 4 to the dyes. Indeed, PDA oxidized with NaIO 4 exhibited increased degradatio...

show abstract

“…Remarkably, ABS materials for enzyme immobilization still face several problems, including low loading efficiency and poor catalytic performance in practice. Mussel-inspired surface chemical modifications are of great interest due to their simplicity, versatility, and wide applicability. , Polydopamine, with a unique ability to form a surface coating layer that contains catechol, amine, and quinone functional groups, can be used in numerous biological reactions. − Previous studies have also demonstrated that immobilizing enzymes through polydopamine is a practical and efficient strategy for obtaining high enzyme loads, favorable activity, stability, and reusability. − The most common strategy to polymerize dopamine into polydopamine is performing autopolymerization through oxygen oxidation under alkaline conditions. However, such a strategy tends to generate catechol dimers that cannot form covalent bonds with amino or thiol groups and are consequently detrimental to enzyme immobilization. , In contrast, performing electro-oxidation with dopamine ensures that the main product is dopaquinone.…”

Section: Introductionmentioning

confidence: 99%

Mussel-Inspired Electro-oxidation-Modified Three-Dimensional Printed Carriers for a Versatile Enzyme Immobilization Approach

Yang

Wang

Shao

et al. 2023

ACS Sustainable Chem. Eng.

View full text Add to dashboard Cite

Conventional enzyme immobilization approaches can only immobilize certain specific enzymes with poor generality. Attempts to improve the universality of enzyme types tend to impart them with more enzymatic catalysis applications. Here, inspired by mussel adhesive proteins, we present a novel eco-friendly surface carrier that was 3D printed and modified by electro-oxidation for enzyme immobilization. The carrier was fabricated through 3D printing by transforming acrylonitrile butadiene styrene (ABS) material into a suitable structure (3DABS). Then, electro-oxidative modification was performed on the surface to form a polydopamine (PDA) coating (3DABS-PDA). The desired structures for the enzyme immobilization carriers were obtained through 3D printing technology, while electro-oxidation modification of the surface provided numerous and firmly covalent binding sites. Based on these features, we have demonstrated that 3D printed and electro-oxidation-modified carriers could be applied to immobilize different types of enzymes. The loading capacity of all immobilized enzymes (galV, EG5C-1, XynLK9, and kdcA) exceeded 25 mg·g–1 (37.7 mg·g–1 for galV), and after 10 reuse cycles, the substrate conversion rate of 3DABS-PDA@galV was still over 85%. The carriers can be reused after simple processing. These results indicate that 3DABS-PDA provides an efficient, sustainable, and versatile approach for enzyme immobilization and exhibits excellent value in various enzymatic catalysis applications.

show abstract

Immobilization of Thermostable Lipase QLM on Core-Shell Structured Polydopamine-Coated Fe3O4 Nanoparticles

Cited by 19 publications

References 37 publications

Fe3O4-PDA-Lipase as Surface Functionalized Nano Biocatalyst for the Production of Biodiesel Using Waste Cooking Oil as Feedstock: Characterization and Process Optimization

Fe3O4-PDA-Lipase as Surface Functionalized Nano Biocatalyst for the Production of Biodiesel Using Waste Cooking Oil as Feedstock: Characterization and Process Optimization

Polydopamine – its Prolific Use as Catalyst and Support Material

Mussel-Inspired Electro-oxidation-Modified Three-Dimensional Printed Carriers for a Versatile Enzyme Immobilization Approach

Contact Info

Product

Resources

About