Starch, a long chain of repeating glucose subunits, is hydrolyzed first into shorter polysaccharide chains this is used as a continual mechanism to help the removal of good debris from the gingiva but has little effect on the breakdown of polysaccharides outside of the mouth. Eventually polysaccharides are converted into the disaccharide maltose, consisting of two glucose subunits, which loosens remains that occurs between the teeth. If chewing is continued for lengthy periods of time these changes will occur in the mouth under the influence of salivary amylase.
Get Full Essay Get access to this section to get all help you need with your essay and educational issues. Effects of Ph on Fungal Amylase Activity Essay Sample Introduction In recent years, the uses of microorganisms have become a huge importance to industry and sparked a large interest into the exploration of enzyme activity in microorganisms.
Amylase is one of the most widely used enzyme required for the preparation of fermented foods. Apart from food and starch industries, in which demand for them is increasing continuously, amylase is also used in various other industries such as paper and pulp, textiles, and medical labs.
Fungi belonging to the genus Aspergillus are most commonly used for the production of amylase. Traditionally, most of the production of amylase is carried out by submerged fermentation, a process which is a method for growing pure cultures of aerobic bacteria, and are incubated in a liquid medium subjected to continuous vigorous agitation.
Because of the ease of handling and a greater control of the environmental factors like temperature and pH, microorganisms like Aspergillus can also be grown on moist solid materials in the absence of free-flowing water.
This is called solid-state fermentation. Normally, the substrates fermented by solid-state include a variety of agricultural products such as rice, wheat, and soybeans. However, non-traditional substrates include an abundant supply of agricultural, forest and food-processing wastes Young et al.
A number of such substrates have been employed for the cultivation of microorganisms to produce host of enzymes and in this case, amylase. Amylases are starch-degrading enzymes that catalyze the hydrolysis of internal glycosidic bonds in polysaccharides Sivaramakrishnan et al.
To be effective, enzymes require specific environmental and chemical conditions.
For example, the slightest variation in pH levels can significantly influence the three-dimensional shape of the enzyme and its ability to be a functional enzyme. Therefore, rendering it inactive and unable to catalylse any form of a reaction.
Similarly, as pH decreases there are more hydrogen ions in a solution making it more acidic. Consequently, with the exception to human digestive enzyme, most enzymes have an optimal range. At the slightest pH change, the active site of the enzyme is altered, which prohibits a specific substrate from binding to the active site and will no longer fit.
Unlike extreme heat that causes an enzyme irreparably damage or become denatured, pH changes are reversible. Restore the pH to its original level, and the enzyme will return to its original capability Richardson et al. The structure of an enzyme has its active site on the surface and is complementary to the substrate.
Here, the substrate and the enzyme create a chemical reaction to form a product.
Most enzyme structures are a tertiary structure that is formed by weak R-group interactions that gives the enzyme its unique form, and held together by hydrogen bonds, ionic bonds, Vann der Waals interactions, and disulfide bridges to reinforce the protein structure Weslake et al.
Any change or disruption to these interactions and the enzyme will denature. The purpose of the experiment was to determine the optimum pH for the activity of fungal amylase. The fungal amylase is the enzyme, starch is the substrate, and maltose is the product.
The digestion of the starch depended on the pH levels.
For example, in a pH 5 solution, amylase digested the starch faster turning it yellow-amber quicker when compared to a pH 6.
The iodine potassium iodine a yellow-amber indicator helps determine whether a reaction occurred. The hypothesis then is the lower the pH the faster the starch would be digested. The prediction is that an acidic pH 5 will digest starch very quickly.
In comparison to another experiment different concentrations within the pH range of 3. Materials and Methods The materials and methods were obtained from the Lab Book Manual and instructor. Each tube was filled with 5 mL of their appropriate buffer the independent variable using a 5 mL graduated pipette.
The experiment was initiated with pH 4 and tube one. After the starch was added onto a test plate, one to two drops of I2KI solution was placed into several compartments, then as quick as possible a drop of the reaction mixture were added to determine if a reaction did occurr.
The reaction mixture was sampled at ten second intervals. This was continued until the I2KI solution remained yellow-amber, thus indicating the digestion of all of the starch dependent variable.
The above steps were repeated with the remaining tubes Morgan et al.Abstract: Amylase is an important enzyme in the human body as it allows for the consumption of starch by breaking the polysaccharide down into maltose units.
The enzyme amylase is mainly used as a digestive enzyme. The reaction that is being broken down in the presence of amylase is the breaking down of long chain carbohydrates (polysaccharides such as starch) into disaccharides (maltose) and then monosaccharides (glucose).
The enzyme amylase was able to work on starch solution in the well whereby it reduced the starch into glucose. Eventually, the color of resulting iodine remained brown. This indicated that there was no starch present in the solution.
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Investigate the effect of temperature on amylase activity Introduction Amylase is an enzyme that catalyses the breakdown of starch into sugars.
Amylases are found in . Effects of Ph on Fungal Amylase Activity Essay Sample. Introduction. In recent years, the uses of microorganisms have become a huge importance to industry and sparked a large interest into the exploration of enzyme activity in microorganisms.