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  • Created by: Ivana
  • Created on: 02-12-13 17:42

Glucose oxidase

  •  Fungal enzyme that converts B-D-glucose into D-gluconate
  • Has a relative molecular mass (Mr) of 144,000 and contaids 2 Moles of FAD per mol of enzyme.
  • Dglucose + glucose oxidase FAD > D-gluconate + glucose oxidase FADH2 
    glucose oxidase FADH2 + O2 > glucose oxidase-FAD + H2O2
    H2O2 + reduced guaicum dye (brown) -> H2O + oxidised guaicum dye (blue) 
  • The increase in blue colour is measured in the spectrophotometer at 600 nm.  
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  • rapid + sensitive method
  • seperates many compounds of biological + clinical interest
  • based on differntial partition of solute between a polar liquid phase (help by a thin layer of adsorbet spread on a glass plate) and a less polar moving (mobile) phase.
  • LIPIDS: the basis of separation is liquid/liquid partition
  • some separation by a different adsoprtion also occurs as the commonly used silica gel is not completely inert. 
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Ninhydrin test

  • generaly used to detect amino acids and ammonium salts
  • upon reaction with these compounds a deep blue/purple product is produced (Ruhemanns purple) 
  • Net result = ninhydrin is in a partially reduced form of hydrindantin
    The ninhydrin condenses with the ammonia and hydrindantin to produce a purpleish colour 
    -reacts with ninhydrin in a different way as the coloour is more yellow
    -this is due to a substitution of the alpha amino group that ninhydrin reacts with
    -this has to do with the carbon rings.  
    -Purpleish colour is usually associated with primary amino acids. Where the N is free to react with ninhydrin
    -However, in proline the N is not available for reaction as it is locked in the ring structure.
    -So no ammonia is produced so now blueish colour is produced.  
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