Immobilization of Purified Phytase Enzyme from Tirmit (Lactarius volemus) on Coated Chitosan with Iron Nanoparticles and Investigation of Its Usability in Cereal Industry

Önem, Hicran; Nadaroğlu, Hayrünnisa

doi:10.1007/s40995-016-0111-y

Cited by 10 publications

(13 citation statements)

References 22 publications

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“…The conventional chromatography techniques such as CM-Cellulose and Sephadex G-100 column chromatographies, DEAE-Sepharose ion exchange, have been efficiently used to purify these enzymes [7]. Since these methods are usually multi-stage and cause depolymerization, the triple phase precipitation technique (TPP) is also often preferred in recent years [5,11,12]. The stability of these enzymes depends on the medium, otherwise the enzymes cannot function appropriately and can be easily disrupted.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Purified Pectin Lyase from Pseudomonas putida onto Magnetic Lily Flowers (Lilium candidum L.) Nanoparticles and Applicability in Industrial Processes

et al. 2020

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Pectinases are an important class of enzymes distributed in many higher plants and microorganisms. One of these enzymes is pectin lyase which has an important role in industrial applications such as clarification of fruit juices. Pectin lyase was purified with 73% yield from Pseudomonas putida bacteria and was 220.7-fold using three phase precipitation technique. Molecular weight of purified pectin lyase was determined as 32.88 kDa with SDS-polyacrylamide gel electrophoresis. The pectin lyase was immobilized covalently via the L-glutaraldehyde spacer to the cellulosic structures of lily flowers (Lilium candidum L.). The immobilized enzyme was then magnetized by modifying with γ-Fe3O4 nanoparticles and determined the most appropriate immobilization conditions as pH 6 and 30 °C. Purified pectin lyase was connected to magnetized support material after 60 min at the rate of 86.4%. The optimum pH and temperatures for the free and immobilized pectin lyase was found to be 6.0 and 40 °C. pH and thermal stabilities of the free and immobilized pectin lyase enzyme have been preserved at high-low temperatures and pH. The structural characterization of the immobilized pectin lyase was performed by SEM, FT-IR, and XRD chromatographic analyses and it was observed that the support materials structure was appropriated to immobilization with pectin lyase and to modify with Fe3O4 nanoparticles.

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Section: Introductionmentioning

confidence: 99%

Immobilization of Purified Pectin Lyase from Pseudomonas putida onto Magnetic Lily Flowers (Lilium candidum L.) Nanoparticles and Applicability in Industrial Processes

et al. 2020

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“…Using the TPP Method. PNL enzyme, which was produced extracellularly from Acinetobacter calcoaceticus bacterium, was purified by triple phase separation (TPP) method [6,7]. For the optimization of ammonium sulfate, PNL was precipitated by adding different ammonium sulfate ratios (20%, 40%, 60%, and 80% ammonium sulfate) to the homogenate medium at the optimum n-butanol ratio (1.0 : 0.5%).…”

Section: Purification Of Pnl From Acinetobacter Calcoaceticusmentioning

confidence: 99%

“…e TPP method, previously used in the purification of mannanase [6] and phytase [7] enzymes, has also been used to purify the pectin lyase enzyme. e purification coefficient for PNL purified by TPP method from Pseudomonas putida for the first time was determined as 192.58 [24].…”

Section: Characterization Of Purified Pectinmentioning

confidence: 99%

“…e purified PNL enzyme was found to bind to the magnetized CMC NPs support material after 90 minutes at 80% rate (Figure 2(c)). Maximum binding rates of the pectin lyase to support materials were determined as 85% [16] and 87.2 [7] in previous studies.…”

Section: Effect Of Incubation Time Ph and Temperature On Immobilization Of Pnl Enzyme On Magnetic Cmcmentioning

confidence: 99%

“…Although some chromatography techniques such as CM-Cellulose, Sephadex G-100 column chromatographies, and DEAE-Sepharose ion exchange are used for purification of enzymes [4]; the triple phase separation method has been preferred more in recent years. In this preference, it is effective that other methods take longer and cause depolymerization [5][6][7].…”

Section: Introductionmentioning

confidence: 99%

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Immobilization of Purified Pectin Lyase from Acinetobacter calcoaceticus onto Magnetic Carboxymethyl Cellulose Nanoparticles and Its Usability in Food Industry

Taşğın

Babagil

Nadaroğlu³

et al. 2020

Journal of Chemistry

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An important component of the pectinase enzyme complex is pectin lyase (polymethylgalacturonate lyase; EC 4.2.2.10). In this study, extracellular pectin lyase enzyme was produced from Acinetobacter calcoaceticus bacteria. Pectin lyase was then purified using three-phase precipitation (TPP) technique with 25.5% yield. The pectin lyase was immobilized covalently via the L-glutaraldehyde spacer to the carboxymethyl cellulose. The immobilized pectin lyase was magnetized using Fe3O4 nanoparticles. Purified pectin lyase was connected to magnetized support material after 90 min at the rate of 80%. The most appropriate immobilization conditions were determined as pH 8 and 30°C. By characterizing the free and immobilized enzyme, KM, Vmax, and optimum pH and optimum temperature values were determined. It was optimum pH 8 and temperature 50°C for both free and immobilized pectin lyase. The structural characterization of the immobilized pectin lyase modified with Fe3O4 nanoparticles was carried out by SEM, FT-IR, and XRD chromatographic analyses. At the end of the study, free and immobilized enzymes were used for purification of some fruit juices and results were compared.

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Immobilization and Application of Industrial Enzymes on Plant-Based New Generation Polymers

Nadaroğlu

2021

Exploring Plant Cells for the Production of Compounds of Interest

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Immobilization of Purified Phytase Enzyme from Tirmit (Lactarius volemus) on Coated Chitosan with Iron Nanoparticles and Investigation of Its Usability in Cereal Industry

Cited by 10 publications

References 22 publications

Immobilization of Purified Pectin Lyase from Pseudomonas putida onto Magnetic Lily Flowers (Lilium candidum L.) Nanoparticles and Applicability in Industrial Processes

Immobilization of Purified Pectin Lyase from Pseudomonas putida onto Magnetic Lily Flowers (Lilium candidum L.) Nanoparticles and Applicability in Industrial Processes

Immobilization of Purified Pectin Lyase from Acinetobacter calcoaceticus onto Magnetic Carboxymethyl Cellulose Nanoparticles and Its Usability in Food Industry

Immobilization and Application of Industrial Enzymes on Plant-Based New Generation Polymers

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