Determination of calcium in milk and water samples by using catalase enzyme electrode

Akyılmaz, Erol; Kozgus, Ozge

doi:10.1016/j.foodchem.2008.11.075

Cited by 42 publications

(17 citation statements)

References 35 publications

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“…Industrial applications for catalase include removal of hydrogen peroxide after cold sterilization steps in food processing (Farkye, 2004;Lee, 2004;Tarhan, 1995). Catalase has also been used in the manufacturing of semi-conductors (Akyilmaz and Kozgus, 2009;Liu et al 2016) and in the textile industry (Arabaci and Usluoglu, 2013;Costa et al 2002). Moreover, catalase is indispensable for carrying out biotransformation processes with the use of oxidases to cause decomposition of hydrogen…”

Section: Introductionmentioning

confidence: 99%

Estimation of the Kinetic Parameters for H2o2 Enzymatic Decomposition and for Catalase Deactivation

Miłek

2018

Braz. J. Chem. Eng.

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Catalase is a potentially useful biocatalyst in various industrial bioprocesses (textile industry, food processing, and pulp and paper) that require removal of hydrogen peroxide. This process can be achieved in such reactors even under isothermal conditions. However, it is usually connected with a long duration of the process or with spending a considerable amount of biocatalyst for a unit mass of the transformed substrate, which in turn leads to an increase in operating costs. They can be limited by applying the optimal temperature control, which requires the values of the thermodynamic parameters-the activation energy for reaction and the activation energy for deactivation must be known. This work reports these parameters for hydrogen peroxide decomposition and Aspergillus niger catalase deactivation at temperatures ranging from 35°C to 50°C.

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Section: Introductionmentioning

confidence: 99%

Estimation of the Kinetic Parameters for H2o2 Enzymatic Decomposition and for Catalase Deactivation

Miłek

2018

Braz. J. Chem. Eng.

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“…Today, monofuctional catalase have been applied in various industrial fields, such as food and textile [2], [5], [6], analytical fields as a component of different biosensor systems [6], [7], [9], medical [10] and also in energy [11]. Several researches reported that fungi could produce catalase effectively [12], such as: Paracoccidioides brasiliensis has been isolated from yeast cells grown in the presence of 15 mM of hydrogen peroxide and resulted the catalase yield and purity were 79% and 1.3-fold (aceton precipitation), respectively.…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of Catalase from Indigenous Fungi of Neurospora crassa InaCC F226

Santoso¹,

Ambarsari²,

Suryani³

et al. 2016

International Journal on Advanced Science, Engineering and Information Technology

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Microbial catalase is an important industrial enzyme that catalyzes the decomposition of hydrogen peroxide into water and oxygen. This enzyme posseses great potential of application in food, textile and pharmaceutical industries. In this paper, Neurospora crassa InaCC F226 was used to produce catalase. The aim of this research was to purify the catalase producing by Neurospora crassa InaCC F226 using gel filtration column chromatography and characterization of temperature, pH, Vmax, Km and molecular weight. In this study, the Neurospora crassa was cultured on Vogel's medium for 5 days. The cells were harvested in the 50 mM buffer sodium phosphate (pH 7) containing 3% hydrogen peroxide. Supernatant containing crude enzymes of Catalase was separated from cells by centrifugation at 15 minutes on 13000 x g and 4 o C. The purification result using gel filtration was specific activity 1464.9 U/mg, 10.7 fold and 21.7% yield. Characterization of the purified enzyme toward pH and temperature optimum was 7.0 (271.6 U/mL) and 40 o C (286.1 U/mL). The K m and V max found to be 8.8 mM and 5.7 s.mM-1. The catalase activity increased by additiom of Fe +2 , Ca +2 and inhibited by EDTA, Cu +2 and Mn +2. The molecular weight of the catalase was 59.4 kDa.

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“…As is well known, the activities of catalases and catalase mimics can be affected by some metal ions, based on the interaction between catalysts and the metal ions . As shown in Figure a,b, the activities of Co 3 O 4 NPs were also influenced by metal ions.…”

Section: Resultsmentioning

confidence: 73%

“…Since pH can affect the hydroxyl radicals, the catalytic mechanism of electron transfer would reduce the pH‐dependency on activity. In general, catalases only work in neutral pH because of their low pH‐stability . By contrast, as inorganic material, Co 3 O 4 NPs had better stability than catalases (Figure S6, Supporting Information), which is the precondition of pH‐independent activity.…”

Section: Resultsmentioning

confidence: 99%

Bioinspired Nanozymes with pH‐Independent and Metal Ions‐Controllable Activity: Field‐Programmable Logic Conversion of Sole Logic Gate System

Han

Zhang

2018

Part & Part Syst Charact

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gate functions, alternative logic systems based on other logic elements and input molecules generally need to be constructed to generate other logic functions, making logic conversion quite tedious and expensive. [11][12][13] However, in nature, different environmental factors usually make organisms to be programmed into different forms. Therefore, it is interesting and significant to develop the simple logic conversion strategy for the next generation of unconventional processors by learning from nature.Recently, inorganic nanomaterials with enzyme-like characteristics have attracted growing attentions as enzyme mimics (i.e., nanozymes). [14][15][16][17] Decades of researches have shown that unique properties and activities of nanozymes can bring about the diversity of application, [18,19] such as electrochemical sensor, [20,21] fluorescence assay, [22,23] colorimetric assay, [24] surfaceenhanced raman scattering, [25] and therapeutic medicine. [26,27] Therefore, it is expected that the peculiar characters of nanozymes will bring about novel applications, such as logic conversion.In nature, transition metal ions are associated closely with living organisms, which can positively or negatively influence the activities of enzymes. [28,29] On the other hand, some enzymes can maintain high activity in wide pH range by stabilizing their surface charge, space structure, and electron transfer rate in order to adapt well to different environments. [30] Inspired by these above phenomena, taking advantage of the biotemplates, nanostructure, and Co 3 O 4 , we synthesized Co 3 O 4 nanoparticles (NPs) with unique catalase-like activity: the influence of pH on activity is negligible in wide range of pH; the influence of the same metal ions on activity is variable under the different pH; the influence of the different metal ions on activity is versatile at the same pH. Given the peculiar characters of as-synthesized Co 3 O 4 nanozymes, we present the pHprogrammable logic conversion based on sole logic system. The metal ion-triggered logic gates based on nanozymes are constructed and the transformation of logic functions can be facilely realized by change pH of the same logic systems. This contribution would not only broaden the species and application area of nanozymes, but also open novel avenues for logic conversion on the untraditional processors and the pH-switchable sensing of multiple metal ions.In nature, different environmental factors make organisms to be programmed into different forms. However, it is difficult and significant to realize the fieldprogrammable logic conversion of sole logic system for molecular logic gates. Here, the concept of pH-programmable "logic conversion" on the single logic gate based on the peculiar enzyme-mimicking activity is presented. Inspired by natural enzymes with high pH-stability and metal ions-stimulated activity, pH-independent and metal ions-controllable catalase mimics (Co3 O 4 nanozymes) are designed by protein-directed method. Although pH cannot directly change the activity of n...

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Determination of calcium in milk and water samples by using catalase enzyme electrode

Cited by 42 publications

References 35 publications

Estimation of the Kinetic Parameters for H2o2 Enzymatic Decomposition and for Catalase Deactivation

Estimation of the Kinetic Parameters for H2o2 Enzymatic Decomposition and for Catalase Deactivation

Purification and Characterization of Catalase from Indigenous Fungi of Neurospora crassa InaCC F226

Bioinspired Nanozymes with pH‐Independent and Metal Ions‐Controllable Activity: Field‐Programmable Logic Conversion of Sole Logic Gate System

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