Lab Report On Starch

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Polysaccharides are polymers of carbohydrates formed by linking monosaccharides through condensation reaction and forming glycosidic bonds. In this lab we will be examining starch. Starch is most commonly used for short term energy storage in humans and in plants. Starch that is present in humans and is stored in the form of glycogen as it is more compact. However, both humans and plants convert the polysaccharides into smaller subunits in order to obtain the energy from them. Starch is a polysaccharide which is formed by linking alpha-glucose molecules through 1-4 glycosidic bonds. Starch is made up of two polymers of glucose, amylose (straight chain of glucose molecules) and amylopectin (branched chain of glucose molecules). However when…show more content…
If the concentration of hydrogen ions is high that means that the pH will be lower and vice versa, a low concentration would mean a high pH. All enzymes are not equally as functional across the spectrum of pH concentration, however each enzyme has it’s own optimum pH at which it is capable of performing its' designated function at the maximum rate. Enzymes sensitivity to pH is determined by the tertiary structure as it determines the shape and charge of the active site. The tertiary structure is formed by the ionic bonds between the amine group, carboxyl group, and the “R” group. (Ms Cooper's A Level Biology). “A change in pH will result in a change of charge on the groups which will untimely result in the bonds breaking and changing the shape of the active site” (Ms Cooper's A Level Biology).

Depending on the form of amylase the optimum pH will vary, for α-Amylase (both pancreatic and salivary) the optimum pH is around pH 6.7 to pH 7. β-amylase is present in plants and its optimum pH is around pH 4.0-pH 5.0. And lastly γ-amylase likes the most acidic environment as its optimum pH is about pH 3 ("Amylase." Wikipedia). As we will be using only α-Amylase, we will place it into a pH 7 buffer to see its’ activity at its’ optimum pH ("Amylase." Wikipedia). Using a pH buffer that is higher or lower will most likely denature of enzyme or cause it to function slower (Ms Cooper's A
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A spectrometer could be used to measure these wavelengths. Spectrometry could be used to indicate a solutions concentration if we have a known its absorbance. Spectrometry measures the interaction of a sample on the light. A spectrophotometer works by having a lamp that diverts a beam of light at the diffraction grating. The diffraction grating functions as a prism and separates the light into its component wavelengths. For a specific wavelength to reach the exit slit the diffraction grating could be rotated (BioNetwork). The light that is reflected by the grating is shined through the exit slip which then allows for that wavelength to interact with the sample. The detector that is located infant of the sample measures the transmittance and absorbance of the sample. Absorption measures the light that is absorbed by the sample, or taken in. Transmittance is the opposite, it measures the amount of light that passes through the sample
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