Glucose reacts with glucose oxidase by binding to the enzyme's active site. Glucose oxidase then catalyzes the oxidation of glucose to produce gluconic acid and hydrogen peroxide. This reaction can be used to detect or quantify glucose levels in various samples.
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The molecular weight of glucose oxidase is approximately 160-190 kDa, depending on the specific source and form of the enzyme.
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Catalase may elute in a wider range of fractions than glucose oxidase due to differences in their molecular weights, hydrophobicity, and interactions with the gel filtration or chromatography resin. Catalase is a larger and more complex protein compared to glucose oxidase, which can lead to a broader elution profile. Additionally, catalase may have different binding affinities or interactions with the resin, resulting in varied elution behavior.
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Glucose oxidase that converts the carbonyl (aldehyde) carbon of glucose to a carboxylic acid.
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The Glucose Oxidase test specifically measures the presence of glucose by detecting its oxidation reaction with glucose oxidase enzyme. This enzyme only reacts with glucose, making the test highly specific for glucose detection. On the other hand, Benedict's test, which relies on the reduction of copper ions, can give false positive results with other reducing sugars present in the urine, leading to lower specificity for glucose.
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C. Oxidase is an enzyme.
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Yes, Pseudomonas luteola is oxidase-positive, meaning it contains the enzyme cytochrome C oxidase which catalyzes the oxidation of cytochrome C. This can be detected in the laboratory using an oxidase test.
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Clinistix are used to test for glucose in urine by detecting the presence of reducing sugars. When dipped in urine, the strip will change color based on the amount of glucose present. This color change is then matched to a color chart to determine the glucose level in the urine sample.
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The quantity of glucose oxidase for 1 IU can vary depending on the specific enzyme preparation and assay method used. Generally, 1 IU of glucose oxidase is defined as the amount of enzyme that catalyzes the oxidation of 1 micromole of glucose per minute under specific conditions. It is typically around 1 microgram of enzyme, but it is important to refer to the manufacturer's instructions for the specific enzyme preparation being used.
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To calculate the concentration of glucose in blood using the Beer-Lambert law principle and glucose oxidase, you would typically measure the absorbance of a glucose solution with a spectrophotometer at a specific wavelength. The formula to calculate the concentration of glucose is:
Glucose concentration (mg/dL) = (Absorbance - intercept) / slope
Where the slope and intercept are obtained from a calibration curve using known concentrations of glucose.
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A chemical called glucose oxidase is commonly used to detect glucose. This enzyme reacts with glucose in the presence of oxygen, producing hydrogen peroxide as a byproduct. The level of hydrogen peroxide produced is then typically measured as an indicator of the glucose concentration in a sample.
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Some biochemical characteristics shared by the family Enterobacteriaceae include the ability to ferment glucose, cytochrome oxidase negativity, and the presence of peritrichous flagella. They are facultative anaerobes and typically produce catalase.
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GOD (glucose oxidase) is specific to detecting glucose because it specifically catalyzes the oxidation of glucose to gluconic acid while reducing molecular oxygen to hydrogen peroxide. This reaction is unique to glucose and does not occur with other sugars, making GOD a specific enzyme for glucose detection.
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No, Corynebacterium species are typically oxidase-negative. This means they do not produce the enzyme cytochrome c oxidase, which is essential for the oxidase test.
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Enterics are typically Gram-negative bacteria that ferment glucose, produce acid, and are often found in the intestines of animals. Pseudomonads are also Gram-negative bacteria, but they do not ferment glucose. Additionally, pseudomonads are known for their ability to produce pyocyanin pigment and grow in diverse environments, such as soil and water.
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Its a reagent used to determine the glucose content of a sample. its based on 2 coupled enzyme reactions with a colorimetric end-point:
D-glucose + O2 + H2O ----- glucose oxidase ------> H2O2 + gluconate
aminophenazone + phenol + H2O2 -----peroxidase----> a red dye + H2O
(NOTE: H2O2 product of 1st reaction acts as substrate for 2nd)
this red coloured sample can then be put into a spectrophotometer and an absorbency reading can be taken, this reading can be compared to a calibration curve and the content of glucose can be ascertained.
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Satea Salem El Atrash has written:
'Characterisation in vitro of glucose oxidase-modified electrodes designed for neurochemical analysis' -- subject(s): Biosensors, Neurochemistry, Analysis, Glucose
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i ave no idea wot d answer is
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Pseudomonas and Neisseria are two genera of bacteria that are oxidase positive. This means they produce the enzyme cytochrome c oxidase, which can be detected using an oxidase test.
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The oxidase test is used to differentiate bacteria based on their ability to produce cytochrome c oxidase enzyme. It helps to differentiate between oxidase-positive bacteria, such as Pseudomonas and Neisseria, and oxidase-negative bacteria, such as E. coli and Enterococcus.
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Yes, some aerobic organisms can be oxidase negative. Oxidase positivity is not always directly related to aerobicity, as it depends on the presence of cytochrome c oxidase in the organism. Some aerobic bacteria lack this enzyme and are therefore oxidase negative.
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Yes, Alcaligenes faecalis is oxidase positive. This bacterium produces the enzyme cytochrome c oxidase, which results in a positive oxidase test.
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You can use a glucose oxidase test strip or a glucose meter to detect and measure glucose levels in the sample. Alternatively, you can perform a chemical test like the Benedict's test or Fehling's solution test to confirm the presence of glucose based on color changes.
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A clinistrip is a urine test strip to measure levels of glucose in urine for diabetics. The small plastic strip has glucose oxidase and an organic dye on one end. The enzyme oxidizes glucose to gluconic acid with the formation of hydrogen peroxide. The hydrogen peroxide reacts with dye to produce a blue color. Each color corresponds to a specific level of glucose.
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An aldehyde oxidase is an enzyme which catalyzes the oxidation of an aldehyde to a carboxylic acid.
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No, not all aerobic bacteria are oxidase positive. Oxidase positive bacteria contain cytochrome c oxidase, an enzyme that is involved in the electron transport chain to transfer electrons to oxygen. While most aerobic bacteria are oxidase positive, there are some exceptions.
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The oxidase test result for Lactococcus lactis ssp lactis is negative. This bacterium lacks the enzyme cytochrome c oxidase that is needed to produce a positive result in the oxidase test.
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The test reagent in the oxidase test contains a substrate that changes color when it is oxidized by cytochrome oxidase, an enzyme present in certain bacteria. The color change indicates the presence of the enzyme, helping to differentiate between oxidase-positive and oxidase-negative bacteria.
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Glucose biosensors work by using an enzyme called glucose oxidase to detect glucose. When glucose comes into contact with the enzyme, it reacts and produces a measurable signal, usually in the form of an electrical current. This signal is then converted into a glucose concentration measurement, providing a quick and accurate way to monitor blood glucose levels.
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The media for oxidase test is differential, not selective. It helps differentiate between bacteria that produce the enzyme cytochrome c oxidase (positive result) and those that do not (negative result).
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Strict aerobes must be oxidase positive because oxidase is an enzyme. It is critical to cellular respiration, specifically the final reduction of oxygen in the electron transport chain.
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It's advisable so that the oxidase test determines whether or not an organism has cytochrome oxidase in its electron transport chain.
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The oxidase test detects the presence of cytochrome c oxidase by utilizing a reagent that reacts with the heme group in the enzyme. Since cytochrome c oxidase is the terminal enzyme in the electron transport chain responsible for transferring electrons to oxygen, the presence of this enzyme indicates aerobic respiration. Other electron carriers like NADH and FADH2 do not contain heme groups and therefore do not react with the oxidase test reagent.
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Including an oxidase-positive control in a test of an unknown organism helps to confirm the presence of the enzyme oxidase in the test system. This control provides a baseline for comparison with the unknown organism to determine if it also produces oxidase. This is particularly important in biochemical testing to accurately identify the unknown organism based on its metabolic properties.
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The oxidase test is performed to determine if the culture contains cytochrome c oxidase enzyme, which helps in distinguishing between oxidase-positive and oxidase-negative organisms. This information is important for selecting the appropriate biochemical tests in the API 20E and Enterotube II identification systems, as these tests are designed to work best with specific types of bacteria based on their oxidative characteristics.
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No, anaerobic bacteria do not require oxidase because they do not use oxygen for their metabolism. Oxidase is an enzyme used by aerobic bacteria to catalyze the transfer of electrons to oxygen during respiration. Anaerobic bacteria have alternative pathways for energy generation in the absence of oxygen.
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Use of Enzymes in Food Industry - Food industry utilizes a variety of enzymes for processing of various foods, e.g., production of various types of syrups from starch or sucrose (a- and β-amylases, glucamylase, pullulanase, invertase, and glucose isomerase), meat/protein processing using proteases, removal of glucose and or molecular oxygen (O2) using glucose oxidase and catalase, use of lactase in dairy industry and use of enzymes in fruit juice and brewing industries. The use of g1cose oxidase and catalase is briefly described heres.
Glucose oxides are obtained from A. Niger and Penicillium. It is a highly specific enzyme, which catalyzes the formation of gluconic acid from β - D- glucose in two separate steps, the second step being nonenzymatic spontaneous hydrolysis. Glucose oxidase is used for the removal of glucose or oxygen from the food stuffs in order to enhance their storability. Hydrogen peroxide (H2O2) effectively kills bacteria; it can be eliminated by using catalase. An important application of these enzymes is in the processing of egg white for use in baking industry. The egg white is treated with a mixture of glucose oxidase and catalase; additional H2O2 (0.1 % w/w) is added to provide sufficient O2 for glucose oxidase action. The glucose present in egg white is oxidised, and the egg white is dried for use in baking. Other applications of this enzyme pair are in
(i) removal of O2 from the air present in the head space of bottled and canned drinks, and
(ii) reduction of non enzymic browning in wines and mayonnaises. Use of Enzymes in Food Industry - Food industry utilizes a variety of enzymes for processing of various foods, e.g., production of various types of syrups from starch or sucrose (a- and β-amylases, glucamylase, pullulanase, invertase, and glucose isomerase), meat/protein processing using proteases, removal of glucose and or molecular oxygen (O2) using glucose oxidase and catalase, use of lactase in dairy industry and use of enzymes in fruit juice and brewing industries. The use of g1cose oxidase and catalase is briefly described heres.
Glucose oxides are obtained from A. Niger and Penicillium. It is a highly specific enzyme, which catalyzes the formation of gluconic acid from β - D- glucose in two separate steps, the second step being nonenzymatic spontaneous hydrolysis. Glucose oxidase is used for the removal of glucose or oxygen from the food stuffs in order to enhance their storability. Hydrogen peroxide (H2O2) effectively kills bacteria; it can be eliminated by using catalase. An important application of these enzymes is in the processing of egg white for use in baking industry. The egg white is treated with a mixture of glucose oxidase and catalase; additional H2O2 (0.1 % w/w) is added to provide sufficient O2 for glucose oxidase action. The glucose present in egg white is oxidised, and the egg white is dried for use in baking. Other applications of this enzyme pair are in
(i) removal of O2 from the air present in the head space of bottled and canned drinks, and
(ii) reduction of non enzymic browning in wines and mayonnaises.
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Yes, honey naturally contains an enzyme called glucose oxidase that produces hydrogen peroxide when honey comes into contact with water. This is one reason why honey has antimicrobial properties.
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Yes, the organism contain oxidase enzymes.
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Micrococcus luteus is negative for oxidase because it lacks the cytochrome c oxidase enzyme necessary to produce a positive oxidase reaction. The absence of this enzyme prevents the organism from undergoing the oxidation-reduction reaction typically measured by an oxidase test.
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Strict aerobes must be oxidase positive because oxidase is an enzyme. It is critical to cellular respiration, specifically the final reduction of oxygen in the electron transport chain.
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The oxidase reagent needs to be fresh because it contains the enzyme cytochrome c oxidase, which can degrade over time, leading to false-negative results if it is not active. Using fresh reagent ensures the accuracy of the test results.
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The enzymatic method for determining blood glucose is highly specific for glucose and produces accurate results. It is also a rapid method that requires minimal sample volume, making it efficient for large-scale testing. Additionally, enzymatic methods are less susceptible to interference from other substances in the blood, leading to more reliable measurements.
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And serious heart problems may occur if caffeine and monoamine oxidase inhibitors (MAO) are taken together.
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It's advisable so that the oxidase test determines whether or not an organism has cytochrome oxidase in its electron transport chain.
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