Amylase and Its Functionality at Various Ph Level

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Amylase And Its Functionality
At
Various Ph Level
Abstract

Enzymes can be denatured at various ph levels in which then affects the shape of the enzymes structure and reactivity. The altering of shape causes substrates to not bind in the active site (Scott Freeman, Micheal Harrington, Joan. C Sharp, 2009). Amylase is used as a catalytic enzyme to determine the time period to convert starch into glucose monomers and transport into the bloodstream at different ph levels. Methods involved are obtaining six test tubes (different ph levels) with mixture of dilute starch solution and amylase. Starch indicator solution is used to determine if the starch have been converted to glucose using the catalytic substance amylase. Under the chemical conditions of ph 4, 8 and 10, the amylase has been denatured and the reaction has occurred slowly throughout the time frames. Ph of 6 and 7 worked as the dominant level of ph for the enzyme to catalyze the reactants to produce glucose monomers in a period of sixty minutes. The enzyme (amylase) is only favourable to certain ph levels, in which are 6 and 7. Ph levels other then the favourable ones denature the protein by changing its shape which results into a slow activity of the reactants binding to the active site on the enzyme being a critical danger to human cells.

Introduction

Enzymes play significant role in reactions as they minimize the activation energy for the reaction to proceed to create products. Amylase is a type of enzyme found in human saliva and pancreas secretions which catalyze the complex carbohydrates (starch, glycogen) to glucose (Laursen, A. E., de Jong, M., Victorio- Walz, L., McCarthy, L., & Bostan, V., Gilbride, K. , 2010). A change in either of the enzymes structures will denature overall causing the enzyme to function inactively. Under specific chemical and physical conditions, the bonds in enzymes can be broken apart. At certain ph levels, the structures of enzymes...
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