Post-prandial muscle protein synthesis rates following the ingestion of pea-derived protein do not differ from ingesting an equivalent amount of milk-derived protein in healthy, young males

Plant-derived proteins have received considerable attention as an alternative to animal-derived proteins. However, plant-derived proteins are considered to have less anabolic properties when compared with animal-derived proteins. The lower muscle protein synthesis rates following ingestion of plant- compared with animal-derived protein have been attributed to the lower essential amino acid content of plant-derived proteins and/or their specific amino acid deficiencies. This study aimed to compare post-prandial muscle protein synthesis rates following the ingestion of 30 g pea-derived protein with 30 g milk-derived protein in healthy, young males.

In a randomized, double-blind, parallel-group design, 24 young males (24 ± 3 y) received a primed continuous L-[ring-¹³C₆]-phenylalanine infusion after which they ingested 30 g pea (PEA) or 30 g milk-derived protein (MILK). Blood and muscle biopsies were collected frequently for 5 h to assess post-prandial plasma amino acid profiles and subsequent post-prandial muscle protein synthesis rates.

MILK increased plasma essential amino acid concentrations more than PEA over the 5 h post-prandial period (incremental area under curve 151 ± 31 vs 102 ± 15 mmol∙300 min∙L⁻¹, respectively; P < 0.001). Ingestion of both MILK and PEA showed a robust muscle protein synthetic response with no significant differences between treatments (0.053 ± 0.013 and 0.053 ± 0.017%∙h⁻¹, respectively; P = 0.96).

Post-prandial muscle protein synthesis rates following the ingestion of 30 g pea-derived protein do not differ from the response following ingestion of an equivalent amount of milk-derived protein. International Clinical Trials Registry Platform (NTR6548; 27–06-2017).