In biological systems, endergonic reactions are often coupled to the exergonic hydrolysis of adenosine triphosphate (\(\text{ATP}\)) to make the overall metabolic process thermodynamically favorable. The thermochemical equations for the enzyme-catalyzed coupled synthesis of glutamine and for the hydrolysis of \(\text{ATP}\) at \(298\text{ K}\) are given below.

\[\text{Glutamate}^-\text{(aq)} + \text{NH}_4^+\text{(aq)} + \text{ATP}^{4-}\text{(aq)} \rightarrow \text{Glutamine(aq)} + \text{ADP}^{3-}\text{(aq)} + \text{HPO}_4^{2-}\text{(aq)} + \text{H}^+\text{(aq)} \quad \Delta G^\circ = -17\text{ kJ/mol}_{\text{rxn}}\]

\[\text{ATP}^{4-}\text{(aq)} + \text{H}_2\text{O(l)} \rightarrow \text{ADP}^{3-}\text{(aq)} + \text{HPO}_4^{2-}\text{(aq)} + \text{H}^+\text{(aq)} \quad \Delta G^\circ = -31\text{ kJ/mol}_{\text{rxn}}\]

Based on this information, what is the standard Gibbs free energy change, \(\Delta G^\circ\), for the uncoupled synthesis of glutamine represented by the equation below?

\[\text{Glutamate}^-\text{(aq)} + \text{NH}_4^+\text{(aq)} \rightarrow \text{Glutamine(aq)} + \text{H}_2\text{O(l)}\]