• Join over 1.2 million students every month
  • Accelerate your learning by 29%
  • Unlimited access from just £6.99 per month


Extracts from this document...


ENZYME IMMOBILISATION Aim -The purpose of this investigation is to break down the lactose found in milk, into its disaccharide sugars; glucose and galactose. (A disaccharide is made up of two individual monomers (monosaccharide) units joined together by a condensation reaction). In a normal digestive system all the food we eat is broken down this helps the body to absorb the food. Lactose is a natural sugar found in milk, it is a disaccharide carbohydrate (sugar) made up of two single sugar units (monomers) joined by a hydrolysis reaction (adding of water). The sugar lactose is not very sweet and is insoluble. The enzyme lactase produced in our body breaks lactose into its disaccharide forms-glucose and galactose. Glucose is the only sugar that can be absorbed into the bloodstream. In people that are lactose intolerant they do not have the enzyme to this job or the enzyme does not function well and therefore it could cause indigestion problems. In this investigation I will immobilise enzymes by entrapping them in a gel. I feel there are many advantages of using the immobilised enzymes over the free ones, some advantages are: * The enzymes can easily be separated from the mixture and so enzyme loss at the end of the experiment is minimised. * Because the enzyme can easily be removed it is easier to re-cycle it, therefore it can be re-used a number of times. * The reaction can be stopped by removing the enzyme. * The immobilised enzyme has more stability than free ones and so o reaction rate is better as the enzyme is more firm. ...read more.


I will then measure 20cm of calcium chloride in to a cylinder. After the alginate solution is mixed I will collect it in a syringe filling it all up, so that I can test the maximum possible for the experiment. I will then get a clamp stand and clamp the syringe on with a boss and clamp, tightening as required. I will then place the chloride beaker under the syringe so that the solution can fall directly into it. I will then press the syringe slowly releasing about 2cm solution each time in to the beaker. I will release the same each time so that I get the same sized beads, and so the reaction is fair. This is because bigger beads may cause longer for the lactose to be broken down. I will leave the solution in the calcium chloride for about 10 minutes to allow the beads to harden. After 10 minutes are up I will strain the solution containing the beads into a tea strainer This is a better method than tilting the beaker as I can ensure all the liquid is out, so that no access calcium chloride remains. I will then wash the beads out with distilled water. After I have washed the beads out I will get another syringe and cut a small piece of nylon gauze to be attached to the bottom of this. I will use another syringe as the previous one could still have some liquid which could contaminate the syringe. I will then attach a short length of rubber tubing to the end of the syringe and screw a Hoffman clip on to it. ...read more.


Evaluation-I feel that the method used was apt, however to make the results more certain and reliable things could be changed or improved. Although the experiment gave the desired results, it was only carried out once. To obtain a more reliable results it cold have been carried out at least one more time to see if there was any variation. Therefore I cannot check the precision as I only carried it out once. During the experiment I did not wear goggles. I realise that there could have been a health risk of any of the solutions/acids coming in contact with the eyes. I did not specifically measure the amount of milk I poured over the beads and how long it stayed over. I feel that I should have as I could have then tested the effect of the production of glucose depending on the amount and time allowed for the milk to flow over the beads. When leaving the beads to harden a stop clock could have been used to give more accurate timing. And when transferring the beads instead of using my hands I could have used something such as a spoon. To obtain a far more accurate reading, a data logger would be an option to use. This would contain a sensor that detects the % of glucose present. It would be far more accurate than human interpretation. To see if my result was reliable and to see if the same result was obtained I could have tried other ways of immobilising the enzyme such as carrier binding-which binds water to insoluble carriers, or entrapping the enzyme in a matrix. ...read more.

The above preview is unformatted text

This student written piece of work is one of many that can be found in our AS and A Level Molecules & Cells section.

Found what you're looking for?

  • Start learning 29% faster today
  • 150,000+ documents available
  • Just £6.99 a month

Not the one? Search for your essay title...
  • Join over 1.2 million students every month
  • Accelerate your learning by 29%
  • Unlimited access from just £6.99 per month

See related essaysSee related essays

Related AS and A Level Molecules & Cells essays

  1. Catalyse Investigation

    acidified potassium manganate in the boiling tube rack, so that they could be compared and the end point determined. The experiment was repeated twice for each temperature reading and carried out over ten different temperatures. This ensured an adequate range of results that could be averaged to minimise the effect of any anomalies.

  2. To carry out an investigation into the denaturing of immobilised lactase enzymes in relation ...

    Once the reactants reach this point, the reaction will proceed spontaneously, as the boulder rolls down and the products are formed. Enzymes reduce free energy activation therefore speeding up reaction rates. The enzyme-substrate complex creates a new energy profile, for the reaction, with lower free energy activation.

  1. Comparison of the affect of temperature on immobilized lactase, compared with non-immobilized lactase

    The enzyme is therefore inactive so has become denatured and cannot be re-used. Once an enzyme has become denatured, as it is not able to form enzyme-substrate complexes, the rate of reaction would decrease as the activation energy has not been lowered.

  2. Production of lactase free milk.

    Immobilised enzymes: Enzymes have many industrial used, enzymes can be simply be added to a substrate mixture. but it is not east to use this enzyme again, as it would have to be separated from the product to re use it again, consequently another efficient and economical technique is to use a immobilised enzyme.

  • Over 160,000 pieces
    of student written work
  • Annotated by
    experienced teachers
  • Ideas and feedback to
    improve your own work