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Pectinase Enzyme Report

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Introduction
Pectinase is a group of enzyme which catalyzes the breakdown of pectin-containing substances. It is an integral part in various industrial applications including treating of cotton fabric, paper bleaching, extraction and clarification of fruit juices, removal of pectin from pectic waste waters and tea leaves maceration and other biotechnological applications (Kashyap et al., 2000; Rajendran, 2011 ). These enzymes are commonly produced by Erwinia sp., Aspergillus niger, and by plants such as peaches, carrots, apples and citrus (Alonso et al., 2003). This group of enzymes consists of pectinesterase (PE (E.C 3.1.1.11)), polygalacturonase (PG (E.C 3.2.1.15)) and pectin lyase (PL (E.C 4.2.2.10)) (Singh & Mandal, 2012). Among the pectinolytic enzymes, Plygalacturonase, is the most abundant (Sharma, 2012). The production of pectinase is induced by the presence of pectin. Like other hydrolases (enzymes that catalyze the breakdown of carbohydrates), pectinase is produced alongside growth of the microorganism to breakdown complex polysaccharides such as pectin for nutritional purposes (Hoondal et al., 2002). Pectin content for viable pectinase production using agro-industrial residues range from 0.5-30.0% (Jayani et al., 2005).
Pectin is a polysaccharide found in the cell walls of all plant tissue. It gives the plant rigidity since it acts as intercellular cement. Pectinase turns …show more content…

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Enzymes are a form of protein that lowers activation energy and speeds up reactions as a catalyst. They are made by the stringing together of an abundant amount of amino acids and folded into a specific shape for chemical reactions. Turnip Peroxidase is the enzyme used in this lab and is derived from the vegetable. Enzymes are not used up or permanently altered by their environment Peroxidases are found in a range of organisms and function to break down alcohol (H2O2) and creates byproducts of oxygen and water. In this experiment, the reducing agent guaiacol is added with the substrate, hydrogen peroxide, to create water and oxygen.

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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.

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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.

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ABSTRACT To catalyze a reaction, an enzyme will grab on (bind) to one or more reactant molecules. In this experiment we examined how increasing the volume of the extract added to the reaction would affect the rate of the reaction. The enzyme used was horseradish peroxidase which helps catalyze hydrogen peroxide. Using different pH levels, the absorbance rate of the reaction was measured to see at which condition the enzyme worked best. The rates of absorption were calculated using a spectrophotometer in 20 second intervals up to 120 seconds.

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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.

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Enzymes speed up chemical reactions enabling more products to be formed within a shorter span of time. Enzymes are fragile and easily disrupted by heat or other mild treatment. Studying the effect of temperature and substrate concentration on enzyme concentration allows better understanding of optimum conditions which enzymes can function. An example of an enzyme catalyzed reaction is enzymatic hydrolysis of an artificial substrate, o-Nitrophenylgalactoside (ONPG) used in place of lactose. Upon hydrolysis by B-galactosidase, a yellow colored compound o-Nitrophenol (ONP) is formed.

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