High isostatic pressure (HIP) can be used as an interesting tool to modifying enzymes performance. This study evaluated milk-clotting using recombinant chymosin processed by HIP at 212 MPa/ 5min/ 10 ºC (condition previously determined as able to maxime the milk-clotting activity of this enzyme). After the process, the enzyme was added to the milk and the clotting step was evaluated by rheological assay (to assess the storage modulus (G’)), by infrared scanning (measured in the Turbiscan for obtaining of the backscattering) and by confocal microscopy (CSLM). In addition the wet yield of the gel was also evaluated. The HIP recombinant chymosin promoted faster milk-clotting (10.7% faster by rheological assay) and the gels produced were more consistent (G' value 20.6% higher) than those obtained with non-processed enzyme. Higher Δ backscattering values (6% higher) were observed for milk gels produced with processed enzyme, indicating that the HIP processing of the enzyme increased its ability to promote protein aggregation in the milk. In addition, images obtained by confocal microscopy showed a faster reduction in the total number of pores, with an increased average pore area for gels obtained with the HIP processed enzyme. Furthermore, the wet yields of the gels obtained from HIP processed recombinant chymosin were significantly greater (4.3%). Thus HIP emerges as an interesting alternative to improve the performance of recombinant chymosin, accelerating milk-clotting, possibly reducing the cost of these enzymes and allowing for an increase in cheese yield.