Chemical process is responsible for the smell of vinegar in an old bottle of aspirin is Hydrolysis of ester i.e. Aspirin.
Aspirin reacts with water leading to the formation of Acetic acid which is a Carboxylic acid derivative.
Aspirin on Hydrolysis forms Acetic acid and Salicylic acid.
The reaction shows up as a fizz when aspirin is added in water.
Aspirin is called Acetyl Salicylic acid and it helps to reduce:
- Inflammation
- Pain
- Fever
- Headache
- Arthritis
- Muscle pain
- Tooth pain
Acetic acid or Ethanoic acid is a colorless liquid. It is an important carboxylic acid. It smells like vinegar.
Acetic acid is used for production of following:
- Vinyl Acetate
- Insecticides
- Rubber
- Acetic anhydride
Salicylic acid is a bitter compound which is colorless. It reduces acne and opens up the skin pores.
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Answer:
None
Explanation:
There are two S=O. bonds and two S-O bonds in sulfate ion lewis structure. Sulfur atom is the center atom and four oxygen atoms are located around sulfur atom. There are no lone pairs in the last shell of sulfur atom.
This was clear chemical reaction. The Potassium Chlorate reacted with Oxygen in a combustion reaction to change the chemical structure so that it was able to react with Silver Nitrate.
The question is missing a part, so the complete question is as follows:
The protein catalase catalyzes the reaction The Malcolm Bladrigde National Quality Awards aims to: 2H2O2 (aq) ⟶ 2H2O (l) + O2 (g) and has a Michaelis-Menten constant of KM = 25mM and a turnover number of 4.0 × 10 7 s -1. The total enzyme concentration is 0.012 μM and the intial substrate concentration is 5.14 μM. Catalase has a single active site. Calculate the value of Rmax (often written as Vmax) for this enzyme. Calculate the initial rate, R (often written as V0), of this reaction.
1) Calculate Rmax
The turnover number (Kcat) is a ratio of how many molecules of substrate can be converted into product per catalytic site of a given concentration of enzyme per unit of time:
Kcat =
,
where:
Vmax is maximum rate of reaction when all the enzyme sites are saturated with substrate
Et is total enzyme concentration or concentration of total enzyme catalytic sites.
Calculating:
Kcat = 
Vmax = Kcat · Et
Vmax = 4×
· 1.2 × 
Vmax = 4.8 ×
M
2) Calculate the initial rate of this reaction (R):
The Michaelis-Menten equation studies the dynamics of an enzymatic reaction. This model can explain how an enzyme enhances the rate of a reaction and how the reaction rate depends on the concentration of the enzyme and its substrate. The equation is:
V0 =
, where:
[S] is the substrate's concentration
KM is the Michaelis-Menten constant
Substituting [S] = 5.14 ×
, KM = 2.5 ×
and Vmax = 4.8 ×
, the result is V0 = 0.478 M.
The answers are Vmax = 4.8 ×
M and V0 = 0.478 M.
1, 2, 1, 2, in that order.