catalytic action) Enzymes catalyse a reaction at max. rate at an optimum state Induced fit theory Enzyme’s shape changes when substrate binds to active site Amino acids are moulded into a precise form to perform catalytic reaction effectively Enzyme wraps around substrate to distort it Forms an enzyme-substrate complex → fast reaction E + S → ES → P + E Enzyme is not used up in the reaction (unlike substrates) Changes in pH Affect attraction between substrate and enzyme and therefore efficiency
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Bailey Rose 10/31/2011 Abstract In this lab exercise‚ the study of enzyme catalase‚ we viewed the breakdown of hydrogen peroxide into water and oxygen. The purpose was to isolate catalase from starch and measure the rate of activity under different conditions. Changes in temperature and pH along with Substrate Concentration and Enzyme Concentration were the conditions tested in the experiment. Our class performed this experiment by breaking up into three mega-groups and the data presented
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Collins Instructor: Catherine Rice Date: 07.09.2014 Predictions Sucrase will have the greatest activity at pH 5 Sucrase will have the greatest activity at 70 °C (158 °F) Sucrase activity increases with increasing sucrose concentration Materials and Methods Effect of pH on Enzyme Activity Dependent Variable amount of product (glucose and fructose) produced Independent Variable pH Controlled Variables temperature‚ amount of substrate (sucrose) present‚ sucrase + sucrose incubation time
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molecule of substrate. Amylase is an enzyme in human saliva and in other organisms and its substrate is starch. When the active site of amylase binds with the starch‚ hydrolysis takes place. When the hydrolysis (the breaking of a chemical bond with the insertion of the ions of a water molecule) of starch is complete you are left with a disaccharide called maltose. Enzymes are necessary for metabolic reactions‚ the question I pose is this--do variances of temperature‚ ph‚ substrate and enzyme concentration
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Physical Processes of Digestion: Activity 2: Exploring Amylase Substrate Specificity Lab Report Pre-lab Quiz Results You scored 100% by answering 5 out of 5 questions correctly. 1. Which of the following is true of enzymes and substrates? You correctly answered: c. Enzymes are specific about the substrates they can act upon. 2. Which of the following is/are reducing sugars? You correctly answered: e. both glucose and maltose 3. Cellulose and starch are both You correctly answered: e. polymers of glucose
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Instructor: Professor Jennifer Frere Date: 03.08.2015 Predictions Sucrase will have the greatest activity at pH 6 Sucrase will have the greatest activity at 60 °C (140 °F) Sucrase activity decreases with increasing sucrose concentration Materials and Methods Effect of pH on Enzyme Activity Dependent Variable amount of product (glucose and fructose) produced Independent Variable pH Controlled Variables temperature‚ amount of substrate (sucrose) present‚ sucrase + sucrose incubation time Effect
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ammonia Some fertilisers added to soils to help crop growth contain urea. Although some crop plants can absorb ammonium ions‚ most obtain their source of nitrogen as nitrate ions. The activity of urease can be measured by following the increase in pH as ammonia is produced in the reaction. A student was provided with urease extracted from bacteria and solutions of urea and two chemical inhibitors‚ thiourea and lead nitrate. The student prepared six reaction mixtures (1 to 6) as shown in Table
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proceed. For example‚ study from previous experiments demonstrates that the maltose present will not turn into glucose until it enters the intestine (different catalyst). There are diverse types of enzymes that work best under certain optimum conditions including temperature‚ pH and substrate concentration. Enzymes can be used more than once and are very important to cell functioning; therefore only small quantities of them are required in the cell. The effect of temperature on enzyme activity is; lower
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of the lab‚ we prepared a salivary amylase solution and aggregated acetic acid to detect the presence of mucin. Then‚ 4 test tubes were made of the following: Tube 1 = 3 ml starch + water + 37 degrees water bath; Tube 2 = 3 ml starch + saliva in water bath; Tube 3 = 3 ml starch (cooled) + 3 ml saliva (cooled) in ice bath; Tube 4 = 3 ml starch + 3 ml saliva 5 drops conc. HCL in water bath. An incubation period of 1 hour was followed and each was tested for starch and maltose. A similar procedure was
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aerogenosa‚ B. amyloliquefaciens) but also able to degrade Castrol oil. Out of two isolates one was able to produce Amylase enzyme but lack in producing other enzymes like beta-Glycosidase‚ Chitinase. Our work can be taken forward to study many more biological activities. Also each activity we study is a complete project in itself and our results promise for application of our isolates in Amylase production and also possible source of novel antibiotics. Keywords: Antimicrobial activity‚ Heavy metal
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