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Biochemistry Lab - Enzymes

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Biochemistry Lab - Enzymes
NAME: Aleema Chelsea Chinchamee LAB PARTNERS: Karishma Ramrattan, Vishma Ramsumair and Sharona Badree
ID #: 814003081 DATE (of lab session): Tuesday 24th March, 2015

DEMONSTRATOR: Maurissa

Course Code & Title: BIOL 1362- Biochemistry I

Title of Lab: Investigating Enzymatic Activity in Sweet Potato, Irish Potato Extract and Milk.

Aims:
1. To determine the effect of ascorbic acid on Polyphenol Oxidase (Phenolase).
2. To determine the level of specificity of Phenolase using the following substrates: Caffeic Acid, Catecol, Guaicol, Pyragallol and Tyrosine.
3. To determine the effect of ascorbic acid on Peroxidase.
4. To determine the level of specificity of Peroxidase using the following substrates: Caffeic Acid, Catecol, Guaicol, Pyragallol and Tyrosine.
5. To calculate the effect of the substrate acetaldehyde concentration on a Xanthine Dehydrogenase catalyzed reaction.
6. To determine the effect of heat on a Xanthine Dehydrogenase catalyzed reaction.

Introduction: Enzymes are specialized biologically made proteins that have catalytic functions that are essential for the maintenance and activity of life (Amano 2007). All living cells have enzymes but they are different, they depend on the concentration of enzymes that are found in the organelles. A catalyst is a substance that speeds up a chemical reaction but remains unchanged itself at the end of the reaction (Taylor, D.J and Green, N.P.O 1997, 116). The structural organization of a protein is classified into: primary, secondary, tertiary and quaternary structure. Primary structure refers to the amino acid sequence of the polypeptide chain, secondary structure refers to the conformation including α-helix and β-stand and the reverse turn (Smith, John. H 2004, 2), tertiary refers to the overall folding of the protein and involves interactions of distant parts and quaternary refers to the interaction of separate polypeptide chains (Smith, John. H 2004, 2). Only in the folded state can an

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