It is absolutely not necessary to produce amylase in an inactive form in our body, but it is not the case with trypsin.

Amylase is an enzyme that breaks down carbohydrates into simple sugars, and it is produced in an inactive form to prevent it from digesting the body's own tissues. If amylase were to be produced in an active form, it could potentially cause damage to the body's cells and tissues.

On the other hand, trypsin is an enzyme that breaks down proteins into amino acids. Unlike amylase, trypsin is produced in an inactive form in the pancreas, but it is activated in the small intestine where it is needed for digestion. This activation process ensures that trypsin is only active when and where it is needed, preventing it from causing harm to the body's own tissues.

In summary, it is necessary for amylase to be produced in an inactive form to prevent damage to the body, while trypsin is produced in an inactive form but is activated when needed for digestion.

This statement is incorrect. Both amylase and trypsin are produced in their inactive forms in our body.

- Amylase: Amylase is produced in the pancreas and salivary glands in an inactive form called pro-amylase or pancreatic amylase. When it reaches the small intestine, it is activated by the enzyme enterokinase.

- Trypsin: Trypsin is also produced in the pancreas in an inactive form called trypsinogen. When trypsinogen reaches the small intestine, it is activated by the enzyme enterokinase.

Producing these digestive enzymes in their inactive forms helps prevent them from digesting the tissues where they are produced. They are activated only when they reach their target environment, ensuring proper and controlled digestion.