Microbubble growth and its apparent “shrinkage” during the transient approach to steady-state crystal growth have been monitored by dynamic light scattering in the region immediately ahead of ice crystals growing into aqueous solutions containing dilute concentrations of macromolecules. This interfacial bubble growth occurs in the presence of a solution of globular macromolecules, and is independent of the crystal growth direction. In contrast, bubble growth becomes crystal-facet dependent when the solution contains a biological antifreeze molecule, the antifreeze glycoprotein (AFGP-4). This solution elicited an immediate, 100 x increase in bubble size above the prismatic surface of ice, followed by a gradual decrease in the averaged bubble size concomitant with a large increase in the size polydispersity. Furthermore, when the steady-state crystal growth condition is reached (in approximately one hour), the average bubble size was still ∼ 80x the size of those found in the pure ice-water system. However, when the same solution is above the basal facet, after the steady-state growth condition is attained, the microbubble diameter is unchanged from that found in the pure ice-water system. The difference in microbubble growth in the vicinity of the dynamic ice-solution interface between solutions of AFGP-4 samples and that of other molecules suggests facet-specific affinity of AFGP by ice, a condition necessary for facet-specific crystal growth inhibition.