WO2006064488A1 - Trousse pour dosages colorimetriques d'analytes d'aliments et de boissons - Google Patents

Trousse pour dosages colorimetriques d'analytes d'aliments et de boissons Download PDF

Info

Publication number
WO2006064488A1
WO2006064488A1 PCT/IE2004/000171 IE2004000171W WO2006064488A1 WO 2006064488 A1 WO2006064488 A1 WO 2006064488A1 IE 2004000171 W IE2004000171 W IE 2004000171W WO 2006064488 A1 WO2006064488 A1 WO 2006064488A1
Authority
WO
WIPO (PCT)
Prior art keywords
tablet
dehydrogenase
kit according
analyte
kit
Prior art date
Application number
PCT/IE2004/000171
Other languages
English (en)
Inventor
Barry V. Mccleary
Simon Charnock
Original Assignee
Megazyme Ip Limited
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Megazyme Ip Limited filed Critical Megazyme Ip Limited
Priority to PCT/IE2004/000171 priority Critical patent/WO2006064488A1/fr
Publication of WO2006064488A1 publication Critical patent/WO2006064488A1/fr

Links

Classifications

    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N31/00—Investigating or analysing non-biological materials by the use of the chemical methods specified in the subgroup; Apparatus specially adapted for such methods
    • G01N31/22—Investigating or analysing non-biological materials by the use of the chemical methods specified in the subgroup; Apparatus specially adapted for such methods using chemical indicators

Definitions

  • the present invention relates to a kit for the colorimetric assay of analytes in food and beverages.
  • the invention also relates to a reagent composition in tablet form for colorimetric assays for use in the wine industry.
  • the assay is any assay in which NADH is formed.
  • samples have to be taken periodically during production to ensure optimum quality of the end products.
  • samples have to be taken periodically to assess the quality of the wine.
  • samples are tested at several stages during the alcoholic fermentation process to test for the presence of key analytes such as reducing sugars (D-glucose plus D-fructose) and ethanol, and during the malolactic fermentation process to test for the presence of key analytes such as L-malic acid and L-lactic acid.
  • the amount of NADH or NADPH formed in these coupled reactions is stoichoimetric with the amount of L-malic acid, D-glucose, D-fructose, L- lactic acid etc. present in the test sample.
  • the equilibrium of coupled reactions lies in favour of the NAD + or NADP + , so a further reaction must be included to "pull" the reaction towards formation of NADH or NADPH.
  • One such reaction is the conversion of L-glutamic acid to 2-oxoglutarate by glutamate dehydrogenase (GlDH), shown below:
  • NADH reduces iodonitrotetrazolium chloride (INT) to yield an INT-formazan product (2), leading to a rapid and quantitiative conversion of L-glutamic acid to 2-oxoglutarate.
  • INT iodonitrotetrazolium chloride
  • the amount of INT-formazan formed in this reaction is stoichiometric with the amount of L-glutamic acid. It is the INT-formazan which is measured by this increase in absorbance at 492 nm.
  • This diaphorase/INT reaction is well known. However it has not been widely used for several reasons. For example, in cases where an Ultraviolet (UV) spectrophotometer is readily available, there is no need to incorporate these extra reagents and analytical steps. In addition, some sample mixtures contain reducing substances, such as L- ascorbic acid in fruit juices, or sulphur dioxide in jam, which interfere with the assay as they react with INT causing a "creep" reaction. Such samples require pre-treatment with alkaline hydrogen peroxide before assay. A major disadvantage of adding the diaphorase/INT reaction to assay formulations is the need for the extra steps to be carried out in the assay. In addition the light sensitivity/instability of INT in solution is disadvantageous.
  • the production of a colored end product is clearly desirable and advantageous. This allows measurement of reaction products with a cheap colorimeter rather than an expensive UV spectrophotometer. Furthermore, in such situations, it is essential that the assay reagents are compact, robust and simple to employ. Moreover it is desirable that the assay format employs ready-to-use reagents in the simplest possible format.
  • a further object is to provide an assay which does not require expensive equipment for determination of a result.
  • a still further object is to provide an assay which can be conducted "in-house” without the need to send samples to a laboratory for determination.
  • the invention provides a kit for measuring the amount of analyte in a sample, comprising a tablet comprising (i) a tetrazolium salt (ii) diaphorase and (iii) NAD + , and at least one enzyme active on the analyte to be measured.
  • the kit enables the convenient and accurate determination of the amount of analytes affecting food or beverage quality present in a sample to be carried out on the production floor without the need for expensive analytical equipment, such as for example, a UV spectrophotometer.
  • the tablet of the kit further comprises ATP.
  • ATP is required for the determination of the presence of certain analytes, for example D-glucose and D-fructose.
  • the tablet further comprises a flow agent, which may be water soluble.
  • a flow agent which may be water soluble.
  • the flow agent comprises sodium benzoate.
  • other flow agents may be used.
  • the tablet may comprise a bulking agent.
  • the bulking agent may be selected from the group consisting of lactose, mannitol, maltose or sorbitol.
  • the tablet may comprise a disintegration agent.
  • the disintegration agent may comprise a mixture of sodium bicarbonate and an organic acid such as citric acid, L-malic acid, D-malic acid, succinic acid, for example.
  • the kit further comprises a buffer solution.
  • the pH and composition of the buffer solution are selected to facilitate optimum activity of the included enzyme(s), as would be well known to those of skill in the art.
  • the buffer comprises surfactant selected from the group consisting of Triton X-IOO, polyoxyethylene ether, polyoxyethylene sorbitan or other non-ionic detergent at a concentration of approximately 0.5% (v/v).
  • the buffer provides and maintains the correct pH for the assay.
  • the pH will be selected depending on the active enzymes being used. It will be appreciated by those skilled in the art that if the pH changes the enzyme(s) will be less active or unstable, either of which will impair the test method. Likewise different enzymes are most active at different optimum pHs, and accordingly the pH should be adjusted to achieve optimum activity for the enzyme used.
  • the analyte is selected from the group consisting of D-glucose, D-fructose, D- galactose, L-malic acid, D-malic acid, L-lactic acid, hydroxybutyric acid, D-mannitol, D-sorbitol, L-arabitol, xylitol, acetaldehyde , ethanol or L-glutamate.
  • Other analytes wherein prior coupled reactions produce NADH may also be assayed using the kit according to the invention.
  • the enzyme(s) may be selected from the group consisting of hexokinase, glucose 6- phosphate dehydrogenase, phosphoglucose isomerase, L-malate dehydrogenase, D- malate dehydrogenase, L-lactate dehydrogenase, alcohol dehydrogenase, aldehyde dehydrogenase, D-mannitol dehydrogenase, D-sorbitol dehydrogenase, 3- hydroxybutyrate dehydrogenase, galactose dehydrogenase and glutamate dehydrogenase. It will be appreciated by those skilled in the art that other enzymes could also be used whereby the enzyme is selected according to the analyte to be assayed.
  • the enzymes are supplied as a suspension in ammonium sulphate or another salt solution such as lithium sulphate or dipotassium phosphate, as a solution in glycerol at approximately 50% (v/v) or as a freeze-dried (lyophilised) powder.
  • the tablet of the kit is used in combination with an enzyme or enzymes that in combination with NAD + catalyse the production of NADH in a linked reaction related to the concentration of the specific analyte.
  • the tetrazolium salt is of the type to be reduced by NADH in the presence of diaphorase and is present in an amount sufficient to allow quantitative detection of specific analytes in a test sample.
  • the tetrazolium salt comprises iodonitrotetrazolium chloride, INT. It will be appreciated by the person skilled in the art that other tetrazolium salts may also be employed.
  • the diaphorase is of the correct type and has an activity level to catalyse the indicator-forming reaction involving the enzyme, NADH and a tetrazolium compound.
  • the invention also provides a tablet for the determination of an analyte in a food or beverage sample, the tablet comprising: (i) a tetrazolium salt (ii) diaphorase and (iii) NAD + .
  • the tablet further comprises ATP.
  • the tablet further comprises a buffer and/or surfactant in powder form.
  • the buffer when dissolved in water, or water containing surfactant, yields the correct pH and concentration of required components.
  • the invention also provides a method for measuring the amount of analyte in a test sample comprising the steps of
  • the method includes spectrophotometry measurement of the INT-formazan compound at about 400-5 IOnm.
  • Figure 1 shows the time course of colour formation in the determination of L-malic acid using the procedure as outlined in Example 1.
  • A Reaction mixture containing 6.5 ⁇ g of L-malic acid.
  • B Reaction mixture containing no L-malic acid.
  • the diaphorase/INT reaction used in the assay kit involves quantative utilization of NADH with stoichiometric formation of the INT-formazan complex. This reaction could potentially be applied to all assay situations where NADH is formed, offering the advantages of producing a red coloured (INT-formazan) complex which can be measured with a simple colorimeter and also, of potentially increasing the speed of the reaction by removal of NADH.
  • the invention will now be described in more detail by way of the following examples.
  • the reagent tablet was used to assay for the presence of a variety of key analytes as outlined in the following examples.
  • Step 1 A buffer stock solution was prepared by dissolving 13.2 g of glycylglycine (Sigma G- 1002), 14.7 g of L-glutamate (Sigma G- 1251) and 10 mL of Triton X-100 in 1.5 litres of distilled water. The pH was adjusted to 10.0 with 4 M NaOH and the volume to 2 litres.
  • Step 2 Tablets for the measurement of L-Malic acid were prepared by mixing 4500 Units of diaphorase, 176 mg of INT, 5 g NAD + and flow, bulking and disintegration agents to a weight of 100 grams. After thorough mixing, this was compacted into tablets of approx. 60 mg using a Manesty tablet press.
  • Step 3 Assays were performed by adding 0.1 mL of test sample to 3.0 mL of buffer solution in a special test tube designed to fit directly into a colorimeter. A test tablet was added, allowed to disintegrate over 1-2 min in the dark with occasional agitation. An initial absorbance reading (Ai) was taken and recorded. An aliquot (20 ⁇ L) of L-malate dehydrogenase (7500 U/mL) was added and the reaction allowed to proceed at room temperature (preferably above 22 0 C) for approx 5 min (until there was no significant increase in absorbance over a 1 min period). This absorbance reading (A 2 ) was recorded. From these absorbance values, the concentration of L-malic acid was calculated.
  • Figure 1 shows the time course of colour formation in the determination of L-malic acid using the procedure outlined above.
  • a test tablet as described in example 1 was added to 3.0 mL of buffer solution as described in example 1 and allowed to dissolve completely.
  • An aliquot (0.1 mL) of sample solution containing 6.5 ⁇ g of L-malic acid was added and the initial absorbance reading was taken.
  • An aliquot (20 ⁇ L) of L-malate dehydrogenase (7500 Units/mL) in 3.2 M ammonium sulphate was then added and the increase in colour was monitored in a recording spectrophotometer.
  • a Unit as mentioned here and throughout the patent specification, refers to an International Unit of enzyme activity.
  • Step 1 A buffer stock solution was prepared by dissolving 34 g of imidazole (Sigma 1-1025), 2.4 g anhydrous magnesium chloride and 25 mL of Triton X-IOO in 4 litres of distilled water. The pH was adjusted to 7.6 and the volume to 5 litres.
  • Step 2 Tablets for the measurement of D-glucose and D-fructose were prepared by mixing 4500 Units of diaphorase, 176 mg of INT, 5 g NAD + , 6 g ATP and flow, bulking and disintegration agents such as sodium benzoate, lactose or mannitol, sodium bicarbonate and citric acid to a weight of 100 grams. After thorough mixing, this was compacted into tablets of approx. 60 mg using a Manesty tablet press.
  • Step 3 Assays were performed by adding 0.1 mL of test sample to 3.0 mL of buffer solution in a special test tube designed to fit directly into a colorimeter. A test tablet was added and allowed to disintegrate over 1-2 min in the dark with occasional agitation. An initial absorbance reading (Ai) was taken and recorded. An aliquot (20 ⁇ L) of a mixture of hexokinase (425 Units/mL), glucose 6-phosphate dehydrogenase (212 Units/mL) and phosphoglucose isomerase (1000 Units/mL) was added and the reaction allowed to proceed at room temperature (preferably above 22 0 C) for approx 10 min (until there was no significant increase in absorbance over a 1 min period). This absorbance reading (A 2 ) was recorded. From these absorbance values, the concentration of D-glucose + D- fructose was calculated.
  • Step 1 A buffer stock solution was prepared by dissolving 13.2 g of glycylglycine (Sigma G-1002), 7.5 g potassium chloride, 20 g of magnesium chloride.6 H 2 O and 1OmL of Triton X-IOO in 1.5 litres of distilled water. The pH was adjusted to 8.0 with 4 M NaOH and the volume to 2 litres.
  • Step 2 Tablets for the measurement of D-Malic acid were prepared by mixing 4500 Units of diaphorase, 176 mg of INT, 5 g NAD + and flow, bulking and disintegration agents to a weight of 100 grams. After thorough mixing, this was compacted into tablets of approx. 60 mg using a Manesty tablet press.
  • Step 3 Assays were performed by adding 0.1 mL of test sample to 3.0 mL of buffer solution in a special test tube designed to fit directly into a colorimeter. A test tablet was added, allowed to disintegrate over 1-2 min in the dark with occasional agitation. An initial absorbance reading (Aj) was taken and recorded. An aliquot (20 ⁇ L) of D-malate dehydrogenase (220 Units/mL) was added and the reaction allowed to proceed at room temperature (preferably above 22 0 C) for approx 30 min (until there was no significant increase in absorbance over a 1 min period). This absorbance reading (A 2 ) was recorded. From these absorbance values, the concentration of D-malic acid was calculated.
  • Step 1 A buffer stock solution was prepared by dissolving 26.4 g of glycylglycine, 29.4 g of D-glutamate and 10 mL of Triton X-100 in 1.5 litres of distilled water. The pH was adjusted to 10.0 with 4 M NaOH and the volume to 2 litres.
  • Step 2 Tablets for the measurement of L-Lactic acid were prepared by mixing 4500 Units of diaphorase, 176 mg of INT, 5 g NAD + and flow, bulking and disintegration agents to a weight of 100 grams. After thorough mixing, this was compacted into tablets of approx. 60 mg using a Manesty tablet press.
  • Step 3 Assays were performed by adding 0.1 mL of test sample to 3.0 mL of buffer solution in a special test tube designed to fit directly into a colorimeter. A test tablet was added, allowed to disintegrate over 1-2 min in the dark with occasional agitation. An initial absorbance reading (A
  • Step 1 A buffer stock solution was prepared by dissolving 79 g of tetrapotassium pyrophosphate (anhydrous Sigma p-8260) and 10 mL of Triton X-100 in 1.2L of distilled water. The pH was adjusted to 9.0 with 8 M HCl and the volume to 2 litres.
  • Step 2 Tablets for the measurement of ethanol were prepared by mixing 4500 Units of diaphorase, 176 mg of INT, 5 g NAD + and flow, bulking and disintegration agents to a weight of 100 grams. After thorough mixing, this was compacted into tablets of approx. 60 mg using a Manesty tablet press.
  • Step 3 Assays were performed by adding 0.1 mL of test sample to 3.0 mL of buffer solution in a special test tube designed to fit directly into a colorimeter. A test tablet was added and allowed to disintegrate over 1-2 min in the dark with occasional agitation. An initial absorbance reading (Ai) was taken and recorded. An aliquot (20 ⁇ L) of alcohol dehydrogenase (167 Units/mL) was added and the reaction allowed to proceed at room temperature (preferably above 22 0 C) for approx 5 min (until there was no significant increase in absorbance over a 1 min period). This absorbance reading (A 2 ) was recorded. From these absorbance values, the concentration of ethanol was calculated.
  • Example 6 Acetaldehyde Determination Reagent Step 1.
  • a buffer stock solution was prepared by dissolving 79 g of tetrapotassium pyrophosphate (anhydrous Sigma p-8260) and 10 mL of Triton X-IOO in 1.2L of distilled water. The pH was adjusted to 9.0 with 8 M HCl and the volume to 2 litres.
  • Step 2 Tablets for the measurement of acetaldehyde were prepared by mixing 4500 Units of diaphorase, 176 mg of INT, 5 g NAD + and flow, bulking and disintegration agents to a weight of 100 grams. After thorough mixing, this was compacted into tablets of approx. 60 mg using a Manesty tablet press.
  • Step 3 Assays were performed by adding 0.1 mL of test sample to 3.0 mL of buffer solution in a special test tube designed to fit directly into a colorimeter. A test tablet was added and allowed to disintegrate over 1-2 min in the dark with occasional agitation. An initial absorbance reading (Ai) was taken and recorded. An aliquot (20 ⁇ L) of aldehyde dehydrogenase (7.9 Units/mL) was then added and the reaction allowed to proceed at room temperature (preferably above 22 0 C) for approx 5 min (until there was no significant increase in absorbance over a 1 min period). This absorbance reading (A 2 ) was recorded. From these absorbance values, the concentration of acetaldehyde was calculated.
  • Step 1 A buffer stock solution was prepared by dissolving 24.2 g of Trizma base, 1 ,5 g of bovine serum albumin and 10 mL of Triton X-100 in 1.5 litres distilled water. The pH was adjusted to 9.0 with 8 M HCl and the volume to 2 L.
  • Step 2 Tablets for the measurement of D-mannitol were prepared by mixing 4500 Units of diaphorase, 176 mg of INT, 5 g NAD + and flow, bulking and disintegration agents to a weight of 100 grams. After thorough mixing, this was compacted into tablets of approx. 60 mg using a Manesty tablet press.
  • Step 3 Assays were performed by adding 0.1 mL of test sample to 3.0 mL of buffer solution in a special test tube designed to fit directly into a colorimeter. A test tablet was added and allowed to disintegrate over 1-2 min in the dark with occasional agitation. An initial absorbance reading (Ai) was taken and recorded. An aliquot (20 ⁇ L) of D- mannitol dehydrogenase (300 Units/mL) was then added and the reaction allowed to proceed at room temperature (preferably above 22 0 C) for approx. 4 min (until there was no significant increase in absorbance over a 1 min period). This absorbance reading (A 2 ) was recorded. From these absorbance values, the concentration of D-mannitol was calculated.
  • Step 1 A buffer stock solution was prepared by dissolving 17.8 g of TEA, 1.8 g KCl and 10 mL of Triton X-100 in 1.5 litres of water. The pH was adjusted to 8.6 and the volume to 2 litres.
  • Step 2 Tablets for the measurement of D-sorbitol were prepared by mixing 4500 Units of diaphorase, 176 mg of INT, 5 g NAD + and flow, bulking and disintegration agents to a weight of 100 grams. After thorough mixing, this was compacted into tablets of approx. 60 mg using a Manesty tablet press.
  • Step 3 Assays were performed by adding 0.1 mL of test sample to 3.0 mL of buffer solution in a special test tube designed to fit directly into a colorimeter. A test tablet was added, allowed to disintegrate over 1-2 min in the dark with occasional agitation. An initial absorbance reading (Ai) was taken and recorded. An aliquot (50 ⁇ L) of D- sorbitol dehydrogenase (40 Units/mL) was then added and the reaction allowed to proceed at room temperature (preferably above 22 0 C) for approx. 15 min (until there was no significant increase in absorbance over a 2 min period). This absorbance reading (A 2 ) was recorded. From these absorbance values, the concentration of D-sorbitol was calculated.
  • a buffer stock solution was prepared by dissolving 74.2 g of TEA, 8.7 g dipotassium hydrogen phosphate and 25 mL of Triton X-IOO in 4 litres of water. The pH was adjusted to 8.6 and the volume to 5 litres.
  • Step 2 Tablets for the measurement of hydroxybutyric acid were prepared by mixing 4500 Units of diaphorase, 176 mg of INT, 5 g NAD + and flow, bulking and disintegration agents to a weight of 100 grams. After thorough mixing, this was compacted into tablets of approx. 60 mg using a Manesty tablet press.
  • Step 3 Assays were performed by adding 0.1 mL of test sample to 3.5 mL of buffer solution in a special test tube designed to fit directly into a colorimeter. A test tablet was added and allowed to disintegrate over 1-2 min in the dark with occasional agitation. An initial absorbance reading (Ai) was taken and recorded. An aliquot (20 ⁇ L) of 3- hydroxybutyrate dehydrogenase (270 Units/mL) was then added and the reaction allowed to proceed at room temperature (preferably above 22 0 C) for approx. 6 min (until there was no significant increase in absorbance over a 1 min period). This absorbance reading (A 2 ) was recorded. From these absorbance values, the concentration of hydroxybutyric acid was calculated.
  • Step 1 A buffer stock solution was prepared by dissolving 121.4 g of Trizma base (BDH cat. no. 271195Y), plus 7.4 g of EDTA (Sigma cat. no. ED2SS) in 4.0 litres of distilled water. The pH was adjusted to 8.6 and the volume to 5 litres.
  • Step 2 Tablets for the measurement of D-galactose were prepared by mixing 4500 Units of diaphorase, 176 mg of INT, 5 g NAD + and flow, bulking and disintegration agents to a weight of 100 grams. After thorough mixing, this was compacted into tablets of approx. 60 mg using a Manesty tablet press.
  • Step 3 Assays were performed by adding 0.1 mL of test sample to 3.0 mL of buffer solution in a special test tube designed to fit directly into a colorimeter. A test tablet was added and allowed to disintegrate over 1-2 min in the dark with occasional agitation. An initial absorbance reading (Ai) was taken and recorded. An aliquot (20 ⁇ L) of galactose dehydrogenase (100 Units/mL) was then added and the reaction allowed to proceed at room temperature (preferably above 22 0 C) for approx. 30 min (until there was no significant increase in absorbance over a 1 min period). This absorbance reading (A 2 ) was recorded. From these absorbance values, the concentration of galactose was calculated.
  • Step 1 A buffer stock solution was prepared by dissolving 74.2 g of TEA, 8.7 g dipotassium hydrogen phosphate and 25 mL of Triton X-100 in 4 litres of distilled water. The pH was adjusted to 8.6 and the volume to 5 litres.
  • Step 2 Tablets for the measurement of D-galactose were prepared by mixing 4500 Units of diaphorase, 176 mg of INT, 5 g NAD + and flow, bulking and disintegration agents to a weight of 100 grams. After thorough mixing, this was compacted into tablets of approx. 60 mg using a Manesty tablet press.
  • Step 3 Assays were performed by adding 0.1 mL of test sample to 3.0 mL of buffer solution in a special test tube designed to fit directly into a colorimeter. A test tablet was added, allowed to disintegrate over 1-2 min in the dark with occasional agitation. An initial absorbance reading (Ai) was taken and recorded. An aliquot (50 ⁇ L) of glutamate dehydrogenase (200 Units/mL) was then added and the reaction allowed to proceed at room temperature (preferably above 22 0 C) for approx. 10 min (until there was no significant increase in absorbance over a 1 min period). This absorbance reading (A 2 ) was recorded. From these absorbance values, the concentration of L-glutamate was calculated.

Landscapes

  • Life Sciences & Earth Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Analytical Chemistry (AREA)
  • Molecular Biology (AREA)
  • Physics & Mathematics (AREA)
  • Chemical & Material Sciences (AREA)
  • Biophysics (AREA)
  • Biochemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • General Physics & Mathematics (AREA)
  • Immunology (AREA)
  • Pathology (AREA)
  • Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)

Abstract

L'invention se rapporte à une trousse permettant de mesurer la quantité d'un analyte dans un échantillon et comportant un comprimé contenant un sel de tétrazolium, de la diaphorase et NAD+, et au moins un enzyme actif sur l'analyte à mesurer. La trousse conforme à la présente invention peut être utilisée pour effectuer des dosages colorimétriques, notamment dans l'industrie du vin. L'invention se rapporte également à un comprimé pouvant être utilisé dans une trousse de diagnostic et comportant un sel de tétrazolium, de la diaphorase et NAD+
PCT/IE2004/000171 2004-12-17 2004-12-17 Trousse pour dosages colorimetriques d'analytes d'aliments et de boissons WO2006064488A1 (fr)

Priority Applications (1)

Application Number Priority Date Filing Date Title
PCT/IE2004/000171 WO2006064488A1 (fr) 2004-12-17 2004-12-17 Trousse pour dosages colorimetriques d'analytes d'aliments et de boissons

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
PCT/IE2004/000171 WO2006064488A1 (fr) 2004-12-17 2004-12-17 Trousse pour dosages colorimetriques d'analytes d'aliments et de boissons

Publications (1)

Publication Number Publication Date
WO2006064488A1 true WO2006064488A1 (fr) 2006-06-22

Family

ID=34959575

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/IE2004/000171 WO2006064488A1 (fr) 2004-12-17 2004-12-17 Trousse pour dosages colorimetriques d'analytes d'aliments et de boissons

Country Status (1)

Country Link
WO (1) WO2006064488A1 (fr)

Cited By (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN104237147A (zh) * 2014-09-26 2014-12-24 天津市宝坻区人民医院 体液中乳糖测定方法
CN106198531A (zh) * 2016-08-30 2016-12-07 内蒙古蒙牛乳业（集团）股份有限公司 检测左旋肉碱含量的方法
CN106248952A (zh) * 2016-07-11 2016-12-21 华测检测认证集团股份有限公司 一种快速测定食品中l‑谷氨酸的方法
CN110923129A (zh) * 2019-04-25 2020-03-27 苏州格锐思生物科技有限公司 一种Fd-谷氨酸合成酶活性测定试剂盒及其检测方法

Citations (9)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4142938A (en) * 1974-03-20 1979-03-06 The Dow Chemical Company Determination of triglycerides and glycerol
US4215197A (en) * 1978-08-04 1980-07-29 Miles Laboratories, Inc. Test means and method for creatinine determination
US4247633A (en) * 1979-04-05 1981-01-27 Pabst Brewing Company Reagent for colorimetric determination of creative phosphokinase
US4613569A (en) * 1980-12-23 1986-09-23 Boehringer Mannheim Gmbh Stabilized composition of tetrazolium salts
JPS61268199A (ja) * 1985-05-22 1986-11-27 Sekisui Chem Co Ltd 胆汁酸測定用試験紙およびその製造方法
EP0279988A1 (fr) * 1986-12-16 1988-08-31 Enzymatics, Inc. Système numérique de contrôle colorimétrique
US5278047A (en) * 1989-04-25 1994-01-11 Lilja Jan E Method of analysis, reagent composition and use thereof for glucose determination
EP0806482A2 (fr) * 1992-03-17 1997-11-12 Unitika Ltd. Méthode pour l'analyse enzymatique et réactif pour cette méthode
EP0990706A1 (fr) * 1998-09-28 2000-04-05 Lifescan, Inc. Dispositifs de diagnostic à base des composés tétrazolium

Patent Citations (9)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4142938A (en) * 1974-03-20 1979-03-06 The Dow Chemical Company Determination of triglycerides and glycerol
US4215197A (en) * 1978-08-04 1980-07-29 Miles Laboratories, Inc. Test means and method for creatinine determination
US4247633A (en) * 1979-04-05 1981-01-27 Pabst Brewing Company Reagent for colorimetric determination of creative phosphokinase
US4613569A (en) * 1980-12-23 1986-09-23 Boehringer Mannheim Gmbh Stabilized composition of tetrazolium salts
JPS61268199A (ja) * 1985-05-22 1986-11-27 Sekisui Chem Co Ltd 胆汁酸測定用試験紙およびその製造方法
EP0279988A1 (fr) * 1986-12-16 1988-08-31 Enzymatics, Inc. Système numérique de contrôle colorimétrique
US5278047A (en) * 1989-04-25 1994-01-11 Lilja Jan E Method of analysis, reagent composition and use thereof for glucose determination
EP0806482A2 (fr) * 1992-03-17 1997-11-12 Unitika Ltd. Méthode pour l'analyse enzymatique et réactif pour cette méthode
EP0990706A1 (fr) * 1998-09-28 2000-04-05 Lifescan, Inc. Dispositifs de diagnostic à base des composés tétrazolium

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
PATENT ABSTRACTS OF JAPAN vol. 011, no. 132 (C - 417) 24 April 1987 (1987-04-24) *

Cited By (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN104237147A (zh) * 2014-09-26 2014-12-24 天津市宝坻区人民医院 体液中乳糖测定方法
CN106248952A (zh) * 2016-07-11 2016-12-21 华测检测认证集团股份有限公司 一种快速测定食品中l‑谷氨酸的方法
CN106198531A (zh) * 2016-08-30 2016-12-07 内蒙古蒙牛乳业（集团）股份有限公司 检测左旋肉碱含量的方法
CN110923129A (zh) * 2019-04-25 2020-03-27 苏州格锐思生物科技有限公司 一种Fd-谷氨酸合成酶活性测定试剂盒及其检测方法

Similar Documents

Publication Publication Date Title
US4378429A (en) Enzymatic method and stabilized solutions for determining total cholesterol in human serum
DK145234B (da) Fremgangsmaade og reagens til kvantitativ bestemmelse af cholesterol
JPS6225040B2 (fr)
US5525481A (en) Enzymatic Reagents for ethanol assay containing diamino compounds
JP3468517B2 (ja) フェナジン含有指示薬を含む試薬および検定法
WO2006064488A1 (fr) Trousse pour dosages colorimetriques d'analytes d'aliments et de boissons
JP3036708B2 (ja) Ｄ−グルコース−６−リン酸の高感度定量法および定量用組成物
US4834918A (en) Process and reagent for increasing the quantum yield in chemiluminescent reactions
CN112255219A (zh) 一种1,5-脱水山梨醇的测定试剂盒及其制备方法和应用
JP2528457B2 (ja) 過酸化水素の定量法
US4409326A (en) Stabilized enzymatic solutions and method for determining total cholesterol in human serum
JP3170377B2 (ja) 物質の測定法
IES20040847A2 (en) A kit for colorimetric assays of food and beverage analytes
US5286627A (en) Method of high-sensitive analysis of bile acid and reagent composition for the analysis
Curey et al. Enzyme-based sensor arrays for rapid characterization of complex disaccharide solutions
EP0727495A2 (fr) Quantification de phosphate inorganique et tréhalose
IE20050815U1 (en) A kit for colorimetric assays of food and beverage analytes
IES84414Y1 (en) A kit for colorimetric assays of food and beverage analytes
Cheng et al. A coupled enzymatic method to measure blood lactate by amperometric monitoring of the rate of oxygen depletion with a Clark oxygen electrode
IES20050815A2 (en) A kit for colorimetric assays of food and beverage analytes
Taniguchi et al. Determination of cholesterol with a laboratory-built chemiluminescence system
JPH02234698A (ja) 細菌ルシフェラーゼ系によるｄｎａプローブの検出法
JP2818696B2 (ja) Ｎａｄｈキナーゼを用いる高感度定量法
JP2002142798A (ja) イヌリン測定方法
JP3034984B2 (ja) Ｄ−ガラクトースの高感度定量法および定量用組成物

Legal Events

Date Code Title Description
AK Designated states

Kind code of ref document: A1

Designated state(s): AE AG AL AM AT AU AZ BA BB BG BR BW BY BZ CA CH CN CO CR CU CZ DE DK DM DZ EC EE EG ES FI GB GD GE GH GM HR HU ID IL IN IS JP KE KG KP KR KZ LC LK LR LS LT LU LV MA MD MG MK MN MW MX MZ NA NI NO NZ OM PG PH PL PT RO RU SC SD SE SG SK SL SM SY TJ TM TN TR TT TZ UA UG US UZ VC VN YU ZA ZM ZW

AL Designated countries for regional patents

Kind code of ref document: A1

Designated state(s): GM KE LS MW MZ NA SD SL SZ TZ UG ZM ZW AM AZ BY KG KZ MD RU TJ TM AT BE BG CH CY CZ DE DK EE ES FI FR GB GR HU IE IS IT LT LU MC NL PL PT RO SE SI SK TR BF BJ CF CG CI CM GA GN GQ GW ML MR NE SN TD TG

121 Ep: the epo has been informed by wipo that ep was designated in this application
NENP Non-entry into the national phase

Ref country code: DE

122 Ep: pct application non-entry in european phase

Ref document number: 04806646

Country of ref document: EP

Kind code of ref document: A1

WWW Wipo information: withdrawn in national office

Ref document number: 4806646

Country of ref document: EP