Bacillus Linchenilormis Experiment

The purpose of this experiment was to analyze the effects of the variables: temperature, pH, and enzyme concentration, on the enzymatic reaction rate of catalase and the level at which its products are released, measuring the rate of absorption using the indicator solution guaiacol and a spectrophotometer to develop a hypothesis of the ideal conditions for these reactions. My hypothesis is that the extremes in concentration, temperature and pH will negatively affect the Au rate. This experiment used 11 solutions contained in cuvettes. Each cuvette, once mixed, is placed in spectrophotometer and then a reading taken every 20 seconds. Cuvettes 1, 8, and 10 are used as blanks to zero out the spectrophotometer.

During the cooking process, the spores of Clostridium perfringens are still survived even after the active cells are killed due to its high heat resistance . It requires boiling for five minutes and autoclaving at 121 degree celsius for 15 minutes to kill all the spores . The presence of nitrates affect the growth of spores due to its characteristics as curing agent (Thomas J. Montville , Karl R. Matthews, 2005). The infections caused by Clostridium perfringens are usually occur due to high amount of food preparation thus foods are kept warm a long period of time before being served.

The effect of pH on the speed of enzyme interaction with substrate chemicals Hypothesis: About pH: If the pH level is less than 5, then the speed of the enzyme reaction will be slower. About temperature: If the temperature stays the same, then the speed of the enzyme reaction will not be completely affected. Background information: The function of enzymes is to speed up the biochemical reaction by lowering the activation energy, they do this by colliding with the substrate.

Results Part 1: Effects of Heat on Bacterial Growth Table 1. Bacterial Growth Based on Heat 40 °C (Group 1) 55°C (Group 2) 80°C (Group 3) 100°C (Group 4) and (Group 5) Time (min) 10 20 30 40 10 20 30 20 30 40 10 20 30 40 Escherichia coli X X X

Sucrase activity increases with increasing sucrose concentration Materials and Methods Effect of pH on Enzyme Activity 1. Dependent Variable amount of product (glucose and fructose) produced 2. Independent Variable pH 3. Controlled Variables temperature, amount of substrate (sucrose) present, sucrase + sucrose incubation time Effect of Temperature on Enzyme Activity 1.

LABORATORY REPORT Activity: Enzyme Activity Name: Natalie Banc Instructor: Elizabeth Kraske Date: 09.22.2016 Predictions 1. Sucrase will have the greatest activity at pH 6 2. Sucrase will have the greatest activity at 50 °C (122 °F) 3. Sucrase activity increases with increasing sucrose concentration Materials and Methods Effect of pH on Enzyme Activity 1. Dependent Variable amount of product (glucose and fructose) produced 2.

: The hypothesis was a failure because the absorbency was not consistently increasing or decreasing as the pH level increased. The absorbency kept decreasing and increasing at random pH levels. When the characteristics of the enzyme reaction were tested, test tube one was given ten drops of enzyme and ten drops of substrate as well as distilled water. The contents then turned from a clear to dark yellow when mixed with absorbency (A400) of 1.370, the highest absorbency out of all tests. The reactant that was lacking in the control reaction was the enzyme.

Enzymes are proteins that catalyze chemical reaction, and they work best at their optimal conditions (optimum pH, temperature etc.) but when the environment is not close to the optimum conditions, the enzymes denature and do not function anymore1. An excellent example would of the effect of temperature on yeast fermentation would be that the bacterial cells if exposed to very high temperature (above the optimal) would no longer function since their enzymes are denatured. The yeast would produce the most Carbon dioxide in the optimal temperature (45 °C ±1/°C) and other temperatures below the optimal temperature would not produce sufficient Carbon dioxide and any temperature above will produce too much that it will lead to the sinking of the bread and death of yeast because its enzymes have been denatured, therefore the reaction will stop. The bread will certainly sink if is not exposed to the right temperature the yeast will not ferment

These enzymes have a secondary and tertiary structure and this could be affected by increases and decreases in temperature beyond the optimum temperature of the enzyme to work in. Mostly enzymes are highly affected any changes in temperature beyond the enzymes optimum. There are too

The focus of the research topic for this biochemistry lab is the action of enzymes. The essential question for the lab was: How is catalase used to prevent the buildup of hydrogen peroxide? The research conducted was about enzymes and the conditions they react in. Since temperature is a factor that directly influences the rate of enzyme reactions, the hypothesis is: If the substrate temperature increases, then the reaction rate of the enzymes will also increase. This was tested by putting a teaspoon of yeast into 10 milliliters of cold, warm, and room temperature hydrogen peroxide and timing how long the reaction lasted.

When enzymes denature, they are inactive and can no longer function properly. High temperature, and PH levels can cause substances to become denatured. When the PH changes, the enzymes stop working, and increasing the temperature will cause a permanent change to the shape of the active site, overall causing the enzyme to no longer have the ability to speed up reactions. Catalase (enzyme) is a common enzyme that is found in all living things. This enzyme catalyzes the decomposition of hydrogen peroxide (substrate) into water and oxygen when it is not denatured.

How Temperature Affects Bacterial and Fungal Amylase Activity Vanessa Romero Vanessa Romero 0058506 Group 1: Vanessa Romero, Kayla Montero, Aixa Andion-Arias, Sophia Tavarez Biology 1010L Section U36 Abstract: Several experiments were conducted on bacterial and fungal amylase, examining the rate at which both break down starch at various temperatures. Enzymes act as catalysts to accelerate reactions. Amylase is a type of enzyme that catalyses the breakdown of starch into sugars. In order to record the rate at which starch was broken down at different temperatures, bacterial amylase was placed in water baths of 0°C, 25°C, 55°C, and 85° for five minutes.

Amylase hydrolyses (breaks down) starch and glycogen into more simple and readily digestible forms of sugar (glucose). Commercially available Amylase solutions can be easily used to breakdown complex carbohydrates (e.g. starch) into simpler forms of sugars (e.g. disaccharides and monosaccharaides). Copper Sulphate can block the activity of Amylase, which is a known non-competitive irreversible enzyme inhibitor. The light absorbent method can be used to study this phenomenon of breakdown and blockade of breakdown of starch in the laboratory. After studying these properties of Amylase and Copper sulphate I designed my experiment to study the inhibitory effect of Copper Sulphate on the enzymatic activity of 1% and 2% Amylase solution.

Along with being found in plants, they are also present in liver cells, kidney cells, leukocytes and erythrocytes. For the concentration of enzyme experiment, the hypothesis was if the concentration of an enzyme increases, then the enzyme activity will increase as well. The hypothesis was proven to be true, because there are more enzymes to react with substrates. For the enzyme—factors affecting, the hypothesis concluded was if the temperature increases, than the enzyme activity will increase. This however was proven wrong, because enzymes become unstable at higher temperatures.

It was well known that the collisions between enzyme and substrate molecules increased with an increase in temperature that result in an increase in reaction rate and thus the conversion. It was observed that with an increase in enzyme loading from 1-2% (w/w) increase in percentage conversion. Usually, an increase in enzyme loading increases the number of active sites and therefore more substrate molecules converted into products. The highest conversion could be attained when the enzyme loading was taken to be 2% in combination with the temperature 50 ˚C.