Effects of Temperature, Ph, Enzyme Concentration, and Substrate Concentration on Enzymatic Activity
Effects of Temperature, pH, Enzyme Concentration, and Substrate Concentration on Enzymatic Activity
INTRODUCTION
Enzymes, proteins that act as catalysts, are the most important type of protein[1]. Catalysts speed up chemical reactions and can go without being used up or changed [3] Without enzymes, the biochemical reactions that take place will react too slowly to keep up with the metabolic needs and the life functions of organisms. Catecholase is a reaction between oxygen and catechol [2]. In the presence of oxygen, the removal of two hydrogen atoms oxidizes the compound catechol, as a result of the formation of water [2]. Oxygen is reduced by the addition of two hydrogen atoms, which also forms water, after catechol is converted to benzoquinone [2]. Long branched chains, the structural backbones of the red and brown melanoid pigments that cause darkening, are formed when the benzoquinone molecules are linked together [2].
Enzymes have a three-dimensional structure that is very complex [2]. This three-dimensional structure consists of one or more polypeptide chains. These polypeptide chains form an active site, an area into which the substrate will fit.
There are four factors that will have an effect on the structure of an enzyme’s active site, the activity of the enzyme, and the rate of the reaction in which the enzyme is involved. The four factors that can affect the activity of an enzyme include temperature, pH, enzyme concentration, and substrate concentration.
In the effects of temperature on enzyme activity, the rate of an enzyme-catalyzed reaction increases at temperature increases, up to the point at which the rate is its maximum [2]. Most enzymes active in living tissue becomes denatured, their secondary or tertiary protein structure breaks down, at the temperature above 40°C [2].
In the effects of pH on enzyme activity, the way a protein folds can be changed in the presence of various ions that can
INTRODUCTION
Enzymes, proteins that act as catalysts, are the most important type of protein[1]. Catalysts speed up chemical reactions and can go without being used up or changed [3] Without enzymes, the biochemical reactions that take place will react too slowly to keep up with the metabolic needs and the life functions of organisms. Catecholase is a reaction between oxygen and catechol [2]. In the presence of oxygen, the removal of two hydrogen atoms oxidizes the compound catechol, as a result of the formation of water [2]. Oxygen is reduced by the addition of two hydrogen atoms, which also forms water, after catechol is converted to benzoquinone [2]. Long branched chains, the structural backbones of the red and brown melanoid pigments that cause darkening, are formed when the benzoquinone molecules are linked together [2].
Enzymes have a three-dimensional structure that is very complex [2]. This three-dimensional structure consists of one or more polypeptide chains. These polypeptide chains form an active site, an area into which the substrate will fit.
There are four factors that will have an effect on the structure of an enzyme’s active site, the activity of the enzyme, and the rate of the reaction in which the enzyme is involved. The four factors that can affect the activity of an enzyme include temperature, pH, enzyme concentration, and substrate concentration.
In the effects of temperature on enzyme activity, the rate of an enzyme-catalyzed reaction increases at temperature increases, up to the point at which the rate is its maximum [2]. Most enzymes active in living tissue becomes denatured, their secondary or tertiary protein structure breaks down, at the temperature above 40°C [2].
In the effects of pH on enzyme activity, the way a protein folds can be changed in the presence of various ions that can
References: CITED [1]LCampbell, Neil., Jane Reece.2005. Biology, 7th ed. Beth Wilbur. Benjamin Cummings Publishing Menlo Park, California. pp. 150-157. [2]Helms, Doris., Carl Helms., Robert Kosinski., John Cummings. 1998. Biology in the Laboratory, 3rd ed, Judith Wilson ed. Freeman Publishing, New York, New York. pp. 10-1 – 10-18. [3]Timberlake, Karen C.2002. Chemistry: Structures of Life. Ben Robert. Benjamin Cummings Publishing, Menlo Park, California. pp. 208.