The formation of an enzyme-substrate complex tends to be thermodynamically favorable due to interactions between the substrate and enzyme.

The correct option is: non-covalent interactions

Explanation:

Enzymes are the macromolecules that are responsible for catalyzing biochemical reactions in the cell and thus they are known as the biological catalysts. They have high specificity and selectivity.

In an enzyme-catalyzed reaction, the substrate molecules bind to the active sites present on the surface of the enzyme, resulting in the formation of a enzyme-substrate complex, which is stabilized by weak non-covalent interactions such as Van der Waals forces, hydrophobic interactions, electrostatic forces and hydrogen bonding.

"among the transition metal elements, manganese and zinc have a slight lowering of electronegativities. the reason behind this is that the nuclear charges of these elements are slightly weaker than the other transition metal elements due to the way their valence electrons are filled up. both manganese and zinc have their valence electrons filled up to the 4th shell with 1 pair of electrons (4s2) completely occupying it. although the electrons in the 3rd shell (3d) are yet to be paired since the outer most shell is filled up, the ability of the nucleus to attract electrons is lessened. hence,   the electronegativity (or the ability to attract electrons) is lessened."

he uptake of drugs from the intestine is often strongly influenced by diffusion. for example, consider a water-insoluble steroid for treating inflammation that is solubilized in aggregates of detergent molecules, called micelles. these micelles, aggregates of 80 soap molecules, have a molecular weight of 24,000, a diameter of 2.6 nm, and a charge of -27. the positively charge ions (counterions) in this system are na".