Efficient stabilization of Saccharomyces cerevisiae external invertase by immobilisation on modified beidellite nanoclays

Andjelković, Uroš; Milutinović-Nikolić, A.; Jović-Jovičić, Nataša; Banković, Predrag; Bajt, Teja; Mojović, Zorica; Vujčić, Zoran; Jovanović, D.

doi:10.1016/j.foodchem.2014.07.055

Cited by 44 publications

(29 citation statements)

References 29 publications

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“…The free and immobilized invertase (EC 3.2.1.26) produces high quality invert sugar with low concentrations of 5-hydroxymethyl-2-furfural (HMF – a carcinogenic byproduct) and without color development compared to the colored version obtained through acid hydrolysis [3], [4]. Invertase is one of the most studied enzymes and it has been immobilized by different methods and supports [5], [6], [7], [8].…”

Section: Introductionmentioning

confidence: 99%

High sucrolytic activity by invertase immobilized onto magnetic diatomaceous earth nanoparticles

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Neri

et al. 2017

Biotechnology Reports

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Section: Introductionmentioning

confidence: 99%

High sucrolytic activity by invertase immobilized onto magnetic diatomaceous earth nanoparticles

Cabrera

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Neri

et al. 2017

Biotechnology Reports

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“…The results show that although the efficiency of removal of tetracycline declined slightly with repeated use, even in the 10th batch removal cycle over 90% of the antibiotic was removed. The exceptional reusability of these biocatalytic systems is related to the stability and durability of the chitinous scaffolds [26] as well as the ability of this material to protect the immobilized enzyme against inactivation as a result of process conditions [85]. Furthermore, the enzyme-support interactions protect the enzyme against elution from the matrix, as tetracycline is washed out from the scaffolds between repeated uses [86].…”

Section: Removal Of Tetracyclinementioning

confidence: 99%

3D Chitin Scaffolds from the Marine Demosponge Aplysina archeri as a Support for Laccase Immobilization and Its Use in the Removal of Pharmaceuticals

et al. 2020

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For the first time, 3D chitin scaffolds from the marine demosponge Aplysina archeri were used for adsorption and immobilization of laccase from Trametes versicolor. The resulting chitin–enzyme biocatalytic systems were applied in the removal of tetracycline. Effective enzyme immobilization was confirmed by scanning electron microscopy. Immobilization yield and kinetic parameters were investigated in detail, in addition to the activity of the enzyme after immobilization. The designed systems were further used for the removal of tetracycline under various process conditions. Optimum process conditions, enabling total removal of tetracycline from solutions at concentrations up to 1 mg/L, were found to be pH 5, temperature between 25 and 35 °C, and 1 h process duration. Due to the protective effect of the chitinous scaffolds and stabilization of the enzyme by multipoint attachment, the storage stability and thermal stability of the immobilized biomolecules were significantly improved as compared to the free enzyme. The produced biocatalytic systems also exhibited good reusability, as after 10 repeated uses they removed over 90% of tetracycline from solution. Finally, the immobilized laccase was used in a packed bed reactor for continuous removal of tetracycline, and enabled the removal of over 80% of the antibiotic after 24 h of continuous use.

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“…Posterior a la extracción, la enzima se encuentra libre pero glicosilada, y dependiendo de su aplicación, se necesitan operaciones de purificación antes del estudio de su cinética completa ya sea en la forma libre o inmovilizada. Las técnicas de precipitación con solvente seguido de separación en columnas cromatográficas son bastante citadas para preparar la enzima principalmente para caracterizar las isoenzimas de invertasa y su inmovilización (GUIMARÃES et al 2007;VEANA et al, 2011;ANDJELKOVIĆ, et al, 2015).…”

Section: Introductionunclassified

Extracción optimizada y purificación parcial de invertasa aislada de S. Cerevisiae en puré de durazno

et al. 2018

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Resumen -La extracción fue realizada a través de un proceso de autolisis, donde las enzimas degradan las estructuras celulares y liberan el contenido citoplasmático al medio extracelular. El proceso de autolisis fue realizado en shaker con diferentes velocidades de agitación (50 -350 rpm) y concentraciones de bicarbonato de sodio (50 -350 mM NaHCO 3 ) a 40 °C por 24 horas, usando un diseño experimental compuesto central adaptado para dos variables y cinco niveles, así como una metodología de superficie de r e s p u e s t a (MSR) y análisis canónico para definir las condiciones óptimas de extracción de invertasa de S. cerevisiae aislada de puré de durazno (ISc). En la condición optima de extracción, se estudió el efecto de la liofilización y purificación en la actividad de la invertasa, usando el método colorimétrico del ácido 3,5-dinitrosalicílico (DNS) a 490 nm para acompañar su actividad expresada en unidades. Una unidad (U) es definida como 1 mg glucosa.min -1 . El valor de proteínas fue cuantificado por el método Lowry y la invertasa de levadura comercial (ILC) como testigo. La influencia de la concentración de NaHCO 3 y de la velocidad de agitación en la extracción de la enzima invertasa indicó efecto lineal, cuadrático e interactivo. El modelo de forma polinómica de segundo orden explicó el fenómeno de extracción de la invertasa con un R 2 de 0,80, y con actividad significativamente dependiente de ambas variables. La máxima extracción fue observada en el punto central experimental (200 mM NaHCO 3 y 200 rpm) con una actividad de 14,7 U.mg -1 . El punto estacionario es un punto de máxima extracción, el cual difiere en menos de 10% del punto central experimental. De acuerdo a estas características, las óptimas condiciones para extracción de la invertasa de S. cerevisiae aislada de puré de durazno son 200 mM NaHCO 3 como agente de autolisis, 200 rpm de agitación orbital a 40 o C durante 24 horas y usando una biomasa de levaduras liofilizadas. El etanol es más efectivo que la acetona para la recuperación de la actividad específica. Términos para indexación: levadura; autolisis; MSR; análisis canónico. Optimized extraction and partial purification of S. Cerevisiae invertase from peach pureeAbstract -The extraction was performed using an autolysis process where enzymes degrade cell structures and release the cytoplasmic contents to the extracellular medium. The autolysis process was carried out in shake flasks with different agitation speeds (50 -350 rpm) and the concentration of sodium bicarbonate (50 -350 mM NaHCO 3 ) at 40 ° C for 24 hours, using a central composite design adapted for two variables and five levels and response surface methodology (RSM) and canonical analysis to define the optimal conditions of extraction of invertase S. cerevisiae from peach puree (ISc). In great condition extraction, we studied the effect of the liofilization and purified in the invertase activity using colorimetric method of 3,5-dinitrosalicílico (DNS) at 490 nm to monitor their activity. One unit (U) defined as 1 mg glicose....

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Efficient stabilization of Saccharomyces cerevisiae external invertase by immobilisation on modified beidellite nanoclays

Cited by 44 publications

References 29 publications

High sucrolytic activity by invertase immobilized onto magnetic diatomaceous earth nanoparticles

High sucrolytic activity by invertase immobilized onto magnetic diatomaceous earth nanoparticles

3D Chitin Scaffolds from the Marine Demosponge Aplysina archeri as a Support for Laccase Immobilization and Its Use in the Removal of Pharmaceuticals

Extracción optimizada y purificación parcial de invertasa aislada de S. Cerevisiae en puré de durazno

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