Immobilization of laccase in a sponge-like hydrogel for enhanced durability in enzymatic degradation of dye pollutants

Sun, Hongliang; Yang, Hualin; Huang, Wenguang; Zhang, Shujuan

doi:10.1016/j.jcis.2015.03.037

Cited by 90 publications

(38 citation statements)

References 38 publications

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“…The K m of laccase immobilized on Cu–MOF was similar to those of other immobilized carriers . Taken together, these results indicate that the activity of Cu–MOF immobilized laccase is similar to that of other materials‐immobilized laccase, and thus is well‐suited to industrial applications, particularly in the biodegradation of reactive textile dye pollutants …”

Section: Resultssupporting

confidence: 70%

Synthesis and characterization of mesoporous Cu-MOF for laccase immobilization

Zhong

Pang

Wu³

et al. 2017

J. Chem. Technol. Biotechnol

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BACKGROUND Mesoporous metal–organic frameworks (MOFs) have been widely researched for enzyme immobilization, however, most are unstable in the aqueous phase. This paper reports the synthesis of a Cu–MOF for the immobilization of copper contained laccase via a surfactant‐templating method with various surfactant/chelating agent mass ratios. RESULTS The Brunauer–Emmett–Teller (BET) surface area and pore diameter of the nanoscale Cu–MOF were 366–1154 m2 g−1 and 15.2–20.7 nm, respectively. The adsorption concentration and time were optimized to be 5 mg laccase mL−1 and 1 h. This immobilized system exhibited adsorption capacity up to 502 mg g−1 and activity recovery rate of 95.2%. The optimum reaction conditions for immobilizing laccase on Cu–MOF were pH 4 and 50°C. According to the Lineweaver–Burk plot, the Km of the immobilized laccase was 0.157 mmol L−1, indicating that the affinity of immobilized laccase to its substrate was higher than that of free laccase (0.290 mmol L−1). The activity of immobilized laccase after seven iterations of reuse remained approximately 50%. CONCLUSION The mesoporous Cu–MOF showed favorable adsorption capability and can be utilized in laccase immobilization. © 2017 Society of Chemical Industry

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Section: Resultssupporting

confidence: 70%

Synthesis and characterization of mesoporous Cu-MOF for laccase immobilization

Zhong

Pang

Wu³

et al. 2017

J. Chem. Technol. Biotechnol

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“…On the other hand, the V max values were decreased for both PGMA‐ and PGMA–NH 2 ‐immobilized laccases as compared to the free laccase, indicating a decrease in the substrate conversion rate . There are many reasons for the variations in these parameters after immobilization, such as conformational changes, decreased enzyme flexibility, or lower enzyme active site availability for the substrate due to the conformational rigidity caused by enzyme immobilization . The V max / K m ratio measures the catalytic efficiency of the enzyme for the substrate .…”

Section: Resultsmentioning

confidence: 99%

Immobilization of Trametes versicolor laccase on different PGMA‐based polymeric microspheres using response surface methodology: Optimization of conditions

Vera

Rivas

2017

J of Applied Polymer Sci

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Enzymatic immobilization is a versatile alternative to improve enzyme stability and enable its reuse. In this study, the change in the immobilized enzyme properties due to the type of functional group on the carrier was evaluated. For that, monodisperse polymeric microspheres with two functional groups widely used in laccase immobilization—oxirane [poly(glycidyl methacrylate) (PGMA)] and hydrazide—were synthesized by dispersion polymerization to covalently immobilize the laccase Trametes versicolor. Using a response surface methodology, laccase immobilization was optimized for each microsphere type. As a result, laccase immobilization on PGMA carriers appears to broaden the pH and temperature ranges, storage stability, and reusability compared to free and hydrazide enzymes. These aforementioned characteristics indicate that PGMA microspheres could act as an ideal support for enzyme immobilization in biotechnological applications. © 2017 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2017, 134, 45249.

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“…The decrease in Vmax might be due to generous secondary conformational perturbation, and changes on the lipase surface upon immobilization. The catalytic efficiency (Vmax/Km) of MNp-Col-IL (0.11) is lower than that of free lipase (0.37), illustrating that MNp-Col-IL has a relatively low catalytic efficiency [30,31]. The optimal activity for both free lipase and MNp-Col-IL are at 55 • C ( Figure 5A).…”

Section: The Kinetic Parametersmentioning

confidence: 99%

Immobilization of Lipases on Magnetic Collagen Fibers and Its Applications for Short-Chain Ester Synthesis

Song

Chen

et al. 2017

Catalysts

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Magnetic nanoparticles (MNp) Fe 3 O 4 were prepared by chemical coprecipitation, and introduced onto collagen fibers to form magnetic collagen support (MNp-Col) for enzyme immobilization. Candida rugosa lipase has been successfully immobilized on MNp-Col supports by a covalent bond cross-linking agent, glutaraldehyde. The characteristics of MNp-Col and the immobilized lipase were investigated. The immobilized lipase displayed sound magnetic separation abilities in both aqueous and organic media. The activity of the immobilized lipase reached 2390 U/g under optimal conditions. The MNp-Col immobilized lipase shows broadened temperature and pH ranges for hydrolysis of olive oil emulsion. For synthesis of butyrate esters in an n-hexane medium, the yield changes through use of different alcohols, among which, butyric butyrate showed the highest yield. The prepared magnetic collagen fiber provides separation support for enzyme immobilization and has the potential to be used in other biotechnology fields.

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Immobilization of laccase in a sponge-like hydrogel for enhanced durability in enzymatic degradation of dye pollutants

Cited by 90 publications

References 38 publications

Synthesis and characterization of mesoporous Cu-MOF for laccase immobilization

Synthesis and characterization of mesoporous Cu-MOF for laccase immobilization

Immobilization of Trametes versicolor laccase on different PGMA‐based polymeric microspheres using response surface methodology: Optimization of conditions

Immobilization of Lipases on Magnetic Collagen Fibers and Its Applications for Short-Chain Ester Synthesis

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