Immobilization of laccase via adsorption onto bimodal mesoporous Zr-MOF

Pang, Shilong; Wu, Yanwen; Zhang, Xiaoqiong; Li, Bingning; Ouyang, Jie; Ding, Mingyu

doi:10.1016/j.procbio.2015.11.033

Cited by 150 publications

(89 citation statements)

References 52 publications

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“…The amount of laccase adsorbed was determined via the Bradford method using BSA as a reference. The assay of laccase activity with ABTS as substrate, and the calculation of specific activity and activity recovery of immobilized laccase were according to our previous study …”

Section: Methodsmentioning

confidence: 99%

“…Cu–MOF was used for the adsorption of a non‐metal enzyme (trypsin, protease‐like activity) and showed a much higher affinity for bovine serum albumin (BSA) than that of free trypsin . We have previously synthesized a zirconium (Zr)–MOF and studied the enzymatic properties of immobilized laccase . However, the most favorable for such types of immobilization may be native copper imitates that contain MOF as well.…”

Section: Introductionmentioning

confidence: 99%

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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: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Synthesis and characterization of mesoporous Cu-MOF for laccase immobilization

Zhong

Pang

Wu³

et al. 2017

J. Chem. Technol. Biotechnol

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“…Laccases have high catalytic efficiency and are used for technical applications in various industrial and biotechnological domains (Xenakis et al 2016) which includes improving properties of fibers, bio-synthesis, energy exploitation, environmental protection, bio-detection, degradation of synthetic dyes, printing and dyeing industry, bio-pulping in paper industry, conversion of aromatic compounds (Zheng et al 2016), and removal of phenols which causes cancer and teratogenicity when present in waste water (Pang et al 2016). In addition, it is also used in fast moving consumer goods (FMCG) as tooth-paste, mouthwash, detergent, soap, and diapers in cosmetics as deodorants; in beverage and food industry for wine and juice stabilization (Piacquadio et al 1998;Alper and Acar 2004;Surwase et al 2016); in dough or baked products to increase strength of gluten structures; in pharmaceutical industries as anesthetics, anti-inflammatory drugs, antibiotics, and sedatives (Nicotra et al 2004;Surwase et al 2016); and in nanobiotechnology as nanoparticle-based bio-sensors.…”

Section: Introductionmentioning

confidence: 99%

“…In addition, it is also used in fast moving consumer goods (FMCG) as tooth-paste, mouthwash, detergent, soap, and diapers in cosmetics as deodorants; in beverage and food industry for wine and juice stabilization (Piacquadio et al 1998;Alper and Acar 2004;Surwase et al 2016); in dough or baked products to increase strength of gluten structures; in pharmaceutical industries as anesthetics, anti-inflammatory drugs, antibiotics, and sedatives (Nicotra et al 2004;Surwase et al 2016); and in nanobiotechnology as nanoparticle-based bio-sensors. However, laccases are not able to exhibit full efficiency under harsh conditions (Pang et al 2016). Therefore, novel strains which can tolerate harsh conditions and give maximum enzyme production with minimum energy consumption are in huge demand.…”

Section: Introductionmentioning

confidence: 99%

Fungal laccase discovered but yet undiscovered

Agrawal

Chaturvedi

Verma

2018

Bioresour. Bioprocess.

191

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Laccases belongs to multinuclear copper-containing oxidase and can act on a variety of aromatic and non-aromatic compounds. Due to their broad substrate specificity, they are considered as a promising candidate in various industrial and biotechnological sectors. They are regarded as a "Green Tool"/"Green Catalyst" in biotechnology. The present review focuses on structure, reaction mechanism, categories, applications, economic feasibility, limitations, and future prospects of fungal laccases. Thus, this review would help in understanding laccases along with the areas, which has not been focused and requires attention. Since past, immense work has been carried out on laccases: yet, new discoveries and application are ever increasing which includes bio-fuel, bio-sensor, fiber board synthesis, bioremediation, clinical, textile industry, food, cosmetics, and many more. Hence, it can be stated that fungal laccase is an enzyme which is "discovered but yet undiscovered".

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“…As can be seen in Figs and , activated H‐MOF(Zr) and CPO/HRP@H‐MOF(Zr) composites showed the two characteristic peaks (2θ = 7.3° and 8.5°) of UIO‐66(Zr), which indicated that H‐MOF(Zr) retained the UIO‐66(Zr) structure, and the skeleton structure of H‐MOF(Zr) was stable without collapse after enzyme immobilization. However, a significant reduction of the peaks in enzyme loaded H‐MOF(Zr) occurred as shown in Fig.…”

Section: Resultsmentioning

confidence: 98%

Design and preparation of stable CPO/HRP@H‐MOF(Zr) composites for efficient bio‐catalytic degradation of organic toxicants in wastewater

Gao

Zhai

et al. 2018

J of Chemical Tech & Biotech

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BACKGROUND Immobilization of enzyme on a solid support can improve its stability, however, this is often accompanied by a decrease of the initial catalytic activity. The design and preparation of immobilized enzyme with simultaneous high activity and stability is a challenge. RESULTS A hierarchically porous metal organic framework H‐MOF(Zr) which was prepared by ‘crystal defect’ strategy was very stable in aqueous solution and possessed well‐defined, tunable and adjacent hierarchical pores. When using the H‐MOF(Zr) as support for enzyme immobilization, a single array of enzyme in a single mesoporous channel was achieved so as to avoid aggregation of the enzyme. Meanwhile the micropores can be utilized to concentrate substrates, resulting in a decrease in the mass transfer resistance of substrate compared with that in the bulk buffer due to the enzymes and substrates closely embedded on the same support. The prepared immobilized enzyme CPO/HRP@H‐MOF(Zr) was more stable at elevated temparatures, showing 58.2% enhanced activity compared with free enzymes at 70 °C for 1 h incubation. After 12 cycles, 70.7% of activity remained. When the CPO/HRP@H‐MOF(Zr) was applied in the treatment of wastewater containing isoproturon and 2,4‐dichlorophenol, complete degradation was achieved in only 15 min. CONCLUSION Both high activity and stability under harsh reaction conditions give the CPO/HRP@H‐MOF(Zr) composites potential for practical application in wastewater treatment. © 2018 Society of Chemical Industry

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Immobilization of laccase via adsorption onto bimodal mesoporous Zr-MOF

Cited by 150 publications

References 52 publications

Synthesis and characterization of mesoporous Cu-MOF for laccase immobilization

Synthesis and characterization of mesoporous Cu-MOF for laccase immobilization

Fungal laccase discovered but yet undiscovered

Design and preparation of stable CPO/HRP@H‐MOF(Zr) composites for efficient bio‐catalytic degradation of organic toxicants in wastewater

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