Would a protein need to be hydrophobic in order for this to work:?

Question

The water-layer hypothesis states that trehalose molecules can form a coating layer around the protein that efficiently competes with the protein to form hydrogen bonds with the water molecules trapped between the protein and trehalose, thereby reducing the number of protein-solvent hydrogen bonds and the accompanying electrostatic solvation forces. A reduction in the solvation forces can consequently lead to an increase in intraprotein interactions, and thus a stabilization of the protein native structure. In the water-replacement hypothesis, key water molecules are thought to be replaced by sugar molecules which then provide the necessary interactions to stabilize protein folding and cellular functions. In the mechanical-entrapment hypothesis, key water molecules are trapped on the protein surface by a cage of sugar molecules forming a higher viscosity layer around the protein

Answer 1

"efficiently competes with the protein to form hydrogen bonds with the water", leans me to say that it is not a hydrophobic protein, proteins can be made up of various types of amino acids, non-polar, polar uncharged, negative charged, positive charged and aromatic..