Separation Of Amino Acid Lab Report

College of Science, Technology & Applied Arts of Trinidad & Tobago DEPARTMENT OF INFORMATION SCIENCE AND TECHNOLOGY INDIVIDUAL ASSIGNMENT COVER PAGE
ASSIGNMENT TITLE: Laboratory four (8): Separation of Amino acids

COURSE CODE: CHEM 134

COURSE TITLE: Survey of Organic and Biochemistry

CRN: 18141 SEMESTER: 1

STUDENT NAME: Rebekah Deepan

STUDENT ID: 00037503

PROGRAMME: Medical Laboratory Technology

DATE OF SUBMISSION: 18th November, 2014

LECTURER’S NAME: Miss Sandra Ashiboe-Mensah
Experiment Number: Title of Experiment:
Experiment four (8): Separation of amino acids
Objectives:
1. To demonstrate

The unit used to compare the movement of the amino acids in this experiment is the retention factor; this is the amount of which the amino acid moved divided by the amount in which the solvent moved. In the experiment isoleucine had an Rf of 0.84 and moved 7cm and phenylalanine had and Rf of 0.81 and moved 6.7cm both of which are hydrophobic and were close to the solvent front. Cysteine which is polar hydrophobic neutral and has a sulfhydryl group had an Rf of 0.54 and moved 4.5cm. Lysine, however, has a polar hydrophilic charge had an Rf of 0.27 and moved 2.2 cm. Therefore the results show that the hydrophobic amino acids were closer to the solvent front than the hydrophilic amino acids. This means that the hydrophobic amino acids have a higher affinity to the mobile phase and moves with the solvent through the paper. The hydrophilic amino acid had a greater affinity to the stationary phase which allows it to somewhat stick to the paper at the spot it was placed. One would think that since the solvent contained water the hydrophobic amino acids would move less, but because the paper is made up of cellulose and cellulose have the ability to absorb water it forms a stationary hydrophilic phase allowing for the hydrophobic amino acids to have a high affinity to the mobile phase and causing the hydrophilic amino acids to have a greater attraction to the

If the amino acid is hydrophobic it would have a greater affinity to the solvent, even though the solvent contains water. This is because the stationary phase is made up of cellulose which absorbs the water thus causing the hydrophobic amino acids to have a greater affinity to the mobile phase. Hydrophilic amino acids would have a greater affinity to the stationary phase causing it to “stick” to the starting point. The amino acids are carried upward by the mobile phase in what is called capillary action. Since amino acids are colorless ninhydrin is sprayed to give the amino acids a purplish color making it more visible to measure the distance traveled. The distance in which each amino acid travels allows for identification of the amino