Temperature And Ph Effect On The Enzymatic Activity Of A Amylase

Temperature and pH effects on the enzymatic activity of a-amylase

Introduction

Enzymes are fundamental molecules within Organisms. They are the biological catalysts of the cells; enhancing the rate of biochemical reactions, ensuring metabolic needs are met.

These molecules are identified as globular proteins with a three dimensional structure and are composed of one or more polypeptide chains. The polypeptide chain or chains within an enzyme are folded to form a specific active site. Each different structured active site and only catalyses a certain substrate that fits; this is known as the lock and key model (Cooper, 2000).

Enzymes achieve the highest reaction rate when under optimal conditions; these conditions include internal temperature and pH levels. When either of these conditions is not in optimal range the active sites of the enzyme can be denatured therefore disallowing the substrate to catalyse and reducing reaction rate (Berg, Tymoczko, Stryer, & Stryer, 2002).

The substrate being catalysed in this experiment is starch. Starch is a polysaccharide Carbohydrate consisting of many glucose molecules that are linked together in straight or branched chains using glycosidic bonds . The Enzyme being used in this experiment is a-amylase, simulating the starch catalysing salivary enzyme found in human saliva.

The purpose of this experiment was to investigate how changes in pH and temperature affect the reaction rate of enzyme activity of A-amylase in a starch substrate.

Rates of a-amylase reaction were seen using Iodine. Throughout the experiment the enzymatic reaction of the starch created a maltose product. Iodine reflects a blue colour when in contact with a starch molecule and converts to a yellowish colour when i...

... middle of paper ...

...re and pH are only some of the conditions that manipulate enzymatic activity. Enzyme concentration directly correlates to reaction rate until the point of enzyme saturation. Enzyme saturation is the point where the amount of enzymes (catalysis) and substrate are in an equilibrium, meaning all enzymes at work and maximum reaction rate has been reached. Enzyme concentration is just one of the many other factors that can manipulate enzyme activity, other factors include substrate concentration, inhibitors and viscosity effects. To get a more thorough understanding of enzyme specificity these factors should be investigated (Worthington Biochemical Corporation, 2015)

Determining the effects of changing pH and temperature on a-amylase enzymatic activity highlighted the specific nature of enzymes and how they can only complete biochemical reactions in optimal conditions.