Yes but only if you're talking about treated apple juice with a naturally small amount of water mixed in.
The free energy change of the reaction; Fe (s) + Au3+ (aq) -> Fe3+ (aq) + Au (s) is calculated to be -443.83KJ/mol.
For the reaction shown in question 7, we can divide it into half equations as follows;
Oxidation half equation;
6 Al (s) -------> 6Al^3+(aq) + 18e
Reduction half equation;
3Cr2O7^2-(aq) + 42H^+(aq) + 18e -----> 6Cr^3+(aq) + 21H2O(l)
The balanced reaction equation is;
6Al(s) + 3Cr2O7^2-(aq) + 42H^+(aq) -----> 6Al^3+(aq) + 6Cr^3+(aq) + 21H2O(l)
The E° of this reaction is obtained from;
E° anode = -0.04 V
E°cathode = +1.50 V
E° cell = +1.50 V - (-0.04 V) = 1.54 V
Given that;
ΔG° = -nFE°cell
n = 3, F = 96500, E°cell = 1.54 V
ΔG° = -(3 × 96500 × 1.54)
ΔG° = -443.83KJ/mol
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Answer: The concentartion of solution will be 0.224 M
Explanation:
Molarity : It is defined as the number of moles of solute present per liter of the solution.
Formula used :

where,
n= moles of solute =
= volume of solution in ml = 275 ml
Now put all the given values in the formula of molarity, we get

Therefore, the concentration of solution will be 0.224 M
Whichever one has the smallest amount of H+ Ions.
Answer:
The A option is the correct answer: Non-native disulfide bonds form after beta-mercaptoethanol is removed, so the protein cannot refold correctly
Explanation:
Beta-Mercaptoehanol is responsible to reduce the four disulfide bonds present in ARNase; Urea deals with non covalente bonds. In presence of both ARNase is denatured.
If Urea is first removed by dialysis, and later is removed Beta-Mercaptoethanol, the enzyme recovers ist activity.
If Beta-Mercaptoethanol is first removed, disulfide bonds different from native use to be formed. As a result ARNase is not an active enzyme