Natural montmorillonite as support for the immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571

Coghetto, Chaline Caren; Scherer, Robison P.; Silva, Marceli F.; Golunski, Simone Maria; Pergher, Sibele B. C.; Oliveira, Débora de; Oliveira, J. Vladimir; Treichel, Helen

doi:10.1016/j.bcab.2012.06.005

Cited by 13 publications

(9 citation statements)

References 32 publications

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“…Also immobilized inulinase from Aspergillus niger on amino-cellulofine was chosen as support material among different materials (CNBractivated Sepharose 4B, cellulose carbonate, bromoacetylcellulose and carboxy-cellulofine), for immobilization with different immobilization efficiencies depending on the supporting material (Nakamura et al 1995). Inulinase from Kluyveromycesmarxianus NRRL Y-7571 was immobilized on the inorganic support, natural montmorillonite, with efficiency 63% (Coghetto et al 2012), and sodium alginate, glutraldhde and activated coal with efficiency 60% (Richetti et al 2012). Yewale et al (2013) immobilized inulinase from A. niger on chitosan with immobilization efficiency 83%.…”

Section: Resultsmentioning

confidence: 99%

“…In comparison with their native form, immobilized enzymes offer several advantages, such as enhanced stability, easier product recovery and purification, the potential for repeated usage and continuous process technology (Shahidi et al 1999;Sobral et al 2003;Coghetto et al 2012).…”

Section: Introductionmentioning

confidence: 99%

“…Enzymes such as β-galactosidase, α-amylase, peroxidase and lipase have been immobilized on nonwoven fibers or membranes (Albayrak and Yang 2002; Meryem et al 2007;Mohamed et al 2008;Li et al 2011). Extensive studies on inulinase immobilization was chosen on different organic supports as: amino-cellulofine, CNBr-activated Sepharose 4B, cellulose carbonate, bromoacetyl-cellulose, Carboxy-Cellulofine, and on inorganic support as: natural montmorillonitesodiumalginate,glutraldhde and activated coal and on chitosan (Vandamme and Derycke 1983;Nakamura et al 1995;Ettalibi and Baratti 2001;Ricca et al 2007;de Paula et al 2008;Coghetto et al 2012;Yewale et al 2013). However, there are no reports on the immobilization of inulinase on nonwoven fabric.…”

Section: Introductionmentioning

confidence: 99%

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Immobilization and characterization of inulinase from Ulocladium atrum on nonwoven fabrics

et al. 2014

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Ulocladium atrum inulinase was immobilized on different composite membranes composed of chitosan/nonwoven fabrics. Km values of free and immobilized U. atrum inulinase on different composite membranes were calculated. The enzyme had optimum pH at 5.6 for free and immobilized U. atrum inulinase on polyester nonwoven fabric coated with 3 percent chitosan solution (PPNWF3), but optimum pH was 5 for immobilized U. atrum inulinase on polyester and polypropylene nonwoven fabrics coated with 1 percent chitosan solution. The enzyme had optimum temperature at 40 degree C for immobilized enzyme on each of polyester and polypropylene composite membranes coated with 1 percent chitosan, while it was 50 degree C for free and immobilized enzyme on polypropylene nonwoven fabric coated with 3 percent chitosan solution. Free U. atrum inulinase was stable at 40 degree C but thermal stability of the immobilized enzyme was detected up to 60 degree C. Reusability of immobilized enzyme was from 38 to 42 cycles of reuse; after this, the immobilized enzyme lost its activity completely. In conclusion, immobilized U. atrum inulinase was considerably more stable than the free enzyme, and could be stored for extended periods.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Immobilization and characterization of inulinase from Ulocladium atrum on nonwoven fabrics

et al. 2014

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“…In the immobilization process enzymes are trapped in a solid matrix, therefore, is possible the reuse and it will not be subjected to denaturation 25 . Several materials with different characteristics such as natural clay 26 , grafted alginate beads 27 , aminated non-porous silica nanoparticles 28 , chitin 29 , alginate-chitosan beads 30 , poly(EGDMA) cryogels 31 and carbon nanotubes 32 have been used as supports for inulinase immobilization by adsorption process. The immobilization process presents some advantages compared with free enzyme, which are the easily removed of the products from immobilized enzymes and possibility the continuous mode of operation 33 .…”

Section: Introductionmentioning

confidence: 99%

“…The immobilization process presents some advantages compared with free enzyme, which are the easily removed of the products from immobilized enzymes and possibility the continuous mode of operation 33 . Immobilized inulinases have been used for many processes, especially for the sugar production through inulin hydrolysis, yielding fructose and fructooligosaccharides, which could be used as functional ingredient 26 . In this work a new application for copper and cobalt aluminate oxides was proposed, i.e., as support for inulinase immobilization.…”

Section: Introductionmentioning

confidence: 99%

Production of Copper and Cobalt Aluminate Spinels and Their Application As Supports for Inulinase Immobilization

et al. 2015

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Copper and cobalt aluminates were obtained through the use of chitosan as template. In this synthesis route, chitosan is eliminated by heating, and a porous material is produced. These oxides were used as supports for inulinase immobilization by adsorption process. Physical properties of produced particles were analyzed by X-ray diffraction (XRD) and nitrogen adsorption-desorption isotherms. Both oxides presented particles containing mesoporous characteristics and high surface area, which is desirable for applications in enzyme immobilization processes. The results revealed that the copper and cobalt aluminates exhibit high inulinase immobilization efficiencies, which makes them promising supports for enzyme immobilization.

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Complete wastewater discoloration by a novel peroxidase source with promising bioxidative properties

Klanovicz

Stefanski

Camargo

et al. 2022

J of Chemical Tech & Biotech

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BACKGROUND Our study aimed to characterize and prospect immobilization strategies for a novel fungal peroxidase (POD) and insert it in pollutant remediation context. The enzymatic extract was obtained by submerged fermentation of Trichoderma koningiopsis in an alternative substrate consisting of fresh microalgal biomass. The immobilization efficiency was evaluated by monitoring the residual activity (RA) and the discoloration potential (DP) of a synthetic dye solution. Concomitantly, the POD catalytic properties were explored, and the most promising storage strategy to maintain the enzymatic activity was studied. RESULTS The novel and non‐purified guaiacol peroxidase from T. koningiopsis expressed a specific activity of up to 7801 U mg−1 in the free form, showing stability when subjected to up to 80 °C in a pH range between 4.0 and 8.0. Furthermore, the bioproduct immobilized on Fe3O4 magnetic nanoparticles, named magnetic nanozymes (MN‐POD), expressed up to 689% RA and 100% removal for the Direct Brown 27 dye. An increase in the enzymatic activity, in both free and immobilized forms, was also observed after storage for up to 8 months. The synthesized magnetic nanozymes showed good reusability, maintaining 13 546 U mg−1 after 10 cycles, and removing 94% of color in a second batch. Toxicological evaluation with Allium cepa indicated that the enzymatic discoloration process with immobilized POD was essential for eliminating genotoxic effects. CONCLUSION The T. koningiopsis peroxidase production and immobilization presented in this work are promising for the enzyme market and for wastewater treatment technologies due to their high bioxidative potential. © 2022 Society of Chemical Industry (SCI).

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Natural montmorillonite as support for the immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571

Cited by 13 publications

References 32 publications

Immobilization and characterization of inulinase from Ulocladium atrum on nonwoven fabrics

Immobilization and characterization of inulinase from Ulocladium atrum on nonwoven fabrics

Production of Copper and Cobalt Aluminate Spinels and Their Application As Supports for Inulinase Immobilization

Complete wastewater discoloration by a novel peroxidase source with promising bioxidative properties

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