Salivary Amylase
Joanne Kathleen Saori T. Suzuki, Laurent Santos, Val Justin D.M. Tongco*
College of Science, University of Santo Tomas, Manila Philippines
Abstract
Salivary amylase, found in humans, is enzyme that catalyzes the hydrolysis of starch into simpler compounds. Its enzymatic activity is affected by several factors, such as temperature and pH. The rates of enzymatic activity of salivary amylase in different temperatures and pH were measured and resulted to be very near 50 C and 7 respectively. However, due to some errors that were committed, the expected optimum temperature was not achieved.
Introduction
Of all biomolecules found in the cells and organisms, the enzymes, because of their highly specialized characteristics and crucial roles, are among the most well known. The enzymes serve as catalysts for biochemical reactions in living organisms. In this role, they direct and regulate the thousands of reaction providing for energy transformation, synthesis, and metabolic degradation. As catalysts, the enzymes excel all other chemicals in power and specificity.
Salivary amylase is the enzyme produced by the salivary glands. Formerly known as ptyalin, It is an enzyme that catalyzes the breakdown of starches (more specifically the breakdown of amylase and amylopectin into disaccharides and trisaccharides). Amylase, like other enzymes, works as a catalyst. All catalysts are enzymes, but not all enzymes are catalysts. A catalyst is a substance that hastens a chemical reaction but does not become part of the end product. Amylase digests starch by catalyzing hydrolysis, which is splitting by the addition of a water molecule. The presence and absence of starch can be confirmed by several tests such as the iodine test, Benedict’s and Fehling’s test. In general, a blue-black color indicates the presence of starch.
The objectives of this experiment are to examine the enzymatic activity and specificity of salivary amylase depending on changes temperature and pH. This
College of Science, University of Santo Tomas, Manila Philippines
Abstract
Salivary amylase, found in humans, is enzyme that catalyzes the hydrolysis of starch into simpler compounds. Its enzymatic activity is affected by several factors, such as temperature and pH. The rates of enzymatic activity of salivary amylase in different temperatures and pH were measured and resulted to be very near 50 C and 7 respectively. However, due to some errors that were committed, the expected optimum temperature was not achieved.
Introduction
Of all biomolecules found in the cells and organisms, the enzymes, because of their highly specialized characteristics and crucial roles, are among the most well known. The enzymes serve as catalysts for biochemical reactions in living organisms. In this role, they direct and regulate the thousands of reaction providing for energy transformation, synthesis, and metabolic degradation. As catalysts, the enzymes excel all other chemicals in power and specificity.
Salivary amylase is the enzyme produced by the salivary glands. Formerly known as ptyalin, It is an enzyme that catalyzes the breakdown of starches (more specifically the breakdown of amylase and amylopectin into disaccharides and trisaccharides). Amylase, like other enzymes, works as a catalyst. All catalysts are enzymes, but not all enzymes are catalysts. A catalyst is a substance that hastens a chemical reaction but does not become part of the end product. Amylase digests starch by catalyzing hydrolysis, which is splitting by the addition of a water molecule. The presence and absence of starch can be confirmed by several tests such as the iodine test, Benedict’s and Fehling’s test. In general, a blue-black color indicates the presence of starch.
The objectives of this experiment are to examine the enzymatic activity and specificity of salivary amylase depending on changes temperature and pH. This