Procedure: 1. Dissolve one teaspoon or one packet of active yeast in a small amount of warm water. Keep still for about 5 minutes. 2. Dilute a small amount of dishwashing liquid in about ¼ cup of water, or dissolve soap in water. 3. Place about ¼ cup of the dishwashing liquid solution or soap solution into the plastic bottle. Two to three drops of food color can be added and mixed. 4. Add ½ cup of hydrogen peroxide to the soap solution. 5. What is your observation? 6. Add the yeast to the mixture in the bottle. 7. What is your observation? Explain the phenomenon. Which reagent caused the reaction to proceed?

Procedure: 1. Dissolve one teaspoon or one packet of active yeast in a small amount of warm water. Keep still for about 5 minutes. 2. Dilute a small amount of dishwashing liquid in about ¼ cup of water, or dissolve soap in water. 3. Place about ¼ cup of the dishwashing liquid solution or soap solution into the plastic bottle. Two to three drops of food color can be added and mixed. 4. Add ½ cup of hydrogen peroxide to the soap solution. 5. What is your observation? 6. Add the yeast to the mixture in the bottle. 7. What is your observation? Explain the phenomenon. Which reagent caused the reaction to proceed?

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

See similar textbooks

Similar questions

Mechanisms of catalysis: Electrostatic catalysis summary + example
Catalysis through proximity and orientation effects involves: (select all that applies) Group of answer choices binding of acidic and/or basic groups in the binding site facilitating chemical reactions by binding substrates close to specific groups binding of substrate in specific, restrictive orientations depending on metal ions for catalysis
Concentrations in biochemical systems are often very dilute. Consequently, scientific notation and logarithms are often used to express concentrations. In scientific notation, numbers are expressed as coefficient x 10" To convert a number to scientific notation, proceed as follows: 1. Move the decimal place so that there is one digit in front of the decimal. 2. Account for the moved decimal in the value of x. If the decimal moved to the right, x is negative; if it moved to the left, x is positive. A logarithm is basically an exponent. Unless otherwise indicated, a logarithm is the a of 10". The numbers after the decimal point are significant; the number before the decimal just identify the location of the decimal point for the number. Notice that it is easy to estimate a logarithm from scientific notation; it's the exponent! Logarithms are commonly used to express the concentration of H. The pH is defined as pH= log (In), where the base number is 2.303. The same general rules as logs…
True/False Question: Enzymes perform catalysis by selectively increasing the rates of the forward reactions, while decreasing the rates of the reverse reactions. O True O False athis resnonse.
True or False Immobilization improves the stability of the enzyme. EnaLne, has a half-life of 10 days in free solution, but under identical conditions of temperature, pH, and medium composition, the measured half-life of a packed column is 30 days. The enzyme is immobilized in a porous sphere 5 mm in diameter.
Reactants: Sodium Hydroxide (NaOH) Potassium Permanganate (KMnO4) Glucose (C12H22O11) What is the purpose of the sodium hydroxide in the redox reaction experiment?
The task I have to do is to investigate the purification of Lactic Acid by means of Extraction with solvents and I found this but I need to explain it with a reaction mechanism, I also need a simpler explanation: -Method Extraction with solvents. These processes are based on the coefficient of distribution of lactic acid between water and various organic solvents. The Jenemann process describes a continuous countercurrent system using isopropyl ether as solvent. The process is expensive and dangerous because ether is flammable and forms explosive peroxides.
The decomposition reaction of hydrogen peroxide (H₂O₂) proceeds as follows: 2 H₂0₂ → 2 H₂O + 0₂ 2 This reaction can occur without a catalyst, in the presence of a chemical catalyst (platinum) or of a biological catalyst (catalase). 1- From the values given in the table below, determine the catalytic power of each catalyst (ratio of the catalyzed rate of reaction to the uncatalyzed rate). 2- Which catalyst is the most efficient? Reaction conditions No catalyst Platinum Catalase Ea (kJ.mol¹) at 20 °C 75 49 8
Mechanisms of catalysis : 2.1 Acid-base catalysis summary + example 2.2 Electrostatic catalysis summary + example 2.3 Covalent catalysis summary + example 2.4 Enzymen catalysis summary 2.5 Mechanism of chymotrypsin summary. These mechanisms involve several of the above-mentioned catalyses. In these summaries, do not just draw a diagram of the proposed mechanisms. It is more important to understand which reaction steps involve what kind of catalysis and how these help to reduce the activation energy needed for the reaction (e.g. a step in the reaction mechanism could be electrostatic catalysis to stabilise the transitions state) 2.6 Mechanism of lysozyme summary. These mechanisms involve several of the above-mentioned catalyses. In these summaries, do not just draw a diagram of the proposed mechanisms. It is more important to understand which reaction steps involve what kind of catalysis and how these help to reduce the activation energy needed for the reaction (e.g.…
s) In two experiments carried out in a research lab, an enzyme reaction is run with and without an inhibitor. Samples were taken over time to measure the concentration of product as the reaction proceeds, with raw data given below. Data were collected at 34 °C and pH 7.5, using [S] = 0.115 M (for both trials) & [E], = 0.0024 M (for both trials): Product concentration (mol P/L) No inhibitor [1] = 0.019 M 0 0 0.0011 0.0023 0.0031 0.0045 0.0074 0.0119 0.0195 0.0271 0.0410 0.0479 0.0550 0.0588 0.0600 Time min 0 3.5 9 13 17 26 43 69 104 156 208 311 415 519 0.0016 0.0038 0.0052 0.0078 0.0111 0.0180 0.0281 0.0412 0.0525 0.0587 0.0598 0.0600 0.0600 A. Determine the initial reaction velocities for both reactions. B. From these data, can you determine what type of inhibition is occurring? If so, show evidence of the type of inhibition occurring. If not, describe what experiment(s) should be done to determine the type of inhibition (competitive, non-competitive or uncompetitive), as well as how…
enzymes are naturally occurring catalysts responsible for various biochemical reactions. Give a modern and recent application of an enzyme used in a biochemical reaction a - the commercial or trade name of the catalyst and enzyme. b - the properties of the catalyst and enzyme (e.g., shape, size, colour, price). c - the advantages and the disadvantages of the chosen catalyst and enzyme d - catalytic reaction (e.g., the reactant, product, reaction equation, phase, selectivity, promoter, catalyst support, operating temperature & pressure).
In modern and recent application of a catalyst and an enzyme used in a chemical and biochemical reaction a) give the commercial or trade name of the catalyst and enzyme of both rxn b) the properties of the catalyst and enzyme (e.g., shape, size, colour, price).