Being widely abundant, grass proteins could be a novel source of plant proteins for human foods. In this study, ryegrass proteins extracted using two different approaches-chemical and enzymatic extraction, were characterised for their physico-chemical and in vitro digestion properties. A New Zealand perennial ryegrass cultivar Trojan was chosen based on its higher protein and lower dry matter contents. Grass protein concentrate (GPC) with protein contents of approximately 55 and 44% were prepared using the chemical and enzymatic approach, respectively. The thermal denaturation temperature of the GPC extracted via acid precipitation and enzymatic treatment was found to be 68.0 ± 0.05 °C and 66.15 ± 0.03 °C, respectively, showing significant differences in protein’s thermal profile according to the method of extraction. The solubility of the GPC was highly variable, depending on the temperature, pH and salt concentration of the dispersion. The solubility of the GPC extracted via enzymatic extraction was significantly lower than the proteins extracted via the chemical method. Digestion of raw GPC was also studied via a gastro-small intestinal in vitro digestion model and was found to be significantly lower, in terms of free amino N release, for the GPC prepared through acid precipitation. These results suggest that the physico-chemical and digestion characteristics of grass proteins are affected by the extraction method employed to extract the proteins. This implies that selection of an appropriate extraction method is of utmost importance for achieving optimum protein functionality during its use for food applications.