<u>Answer:</u> The change in temperature is 84.7°C
<u>Explanation:</u>
To calculate the change in temperature, we use the equation:

where,
q = heat absorbed = 1 kCal = 1000 Cal (Conversion factor: 1 kCal = 1000 Cal)
m = mass of steel = 100 g
c = specific heat capacity of steel = 0.118 Cal/g.°C
= change in temperature = ?
Putting values in above equation, we get:

Hence, the change in temperature is 84.7°C
You calculate the mass using dimensional analysis.
We are given with
The weight of the chain per unit length which is 2.16 kg/m
We are also given with the needed length of the chain which is 7.0 m
Therefore, the mass of the chain is
7.0 m x 2.16 kg / m = mass of the chain in kg<span />
Explanation:
In the extreme winters , the water inside pipes freeze, on freezing it's(water molecule) density decreases and volume increases and therefore, the ice then expands and pushes the water towards the faucet, causing high pressure buildup in the pipe and after a limit the pipe burst. This is what happened to the family in Ottawa, where winters are chilly.
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.