Background: β-lactoglobulin (BLG) is a protein found within whey protein (WP) that is rich in essential amino acids, most notably, leucine (LEU). LEU is considered the most potent EAA in the postprandial stimulation of muscle protein synthesis (MPS), such that suboptimal protein/essential amino acid (EAA) doses containing higher LEU content elicit muscle anabolism comparable to larger protein doses. Our objective was to test the effects of naturally LEU-rich BLG (~10 g protein) versus isonitrogenous whey protein isolate (WPI, ~10 g) on MPS. Methods: Ten healthy young men (26 ± 2 y; 179 ± 2 cm; 81 ± 3 kg) received BLG (1.57 g LEU) or WPI (1.02 g LEU) in a randomised double-blind cross-over fashion. A primed constant intravenous infusion of [1,2 ¹³C₂] LEU was used to determine MPS (isotope ratio mass spectrometry) at baseline and in response to feeding (FED) and feeding-plus-exercise (FED-EX; 6 × 8 unilateral leg extensions; 75% 1-RM). Plasma insulin and EAA’s were quantified. Results: Plasma EAA, branched-chain amino acid (BCAA), and LEU concentrations increased rapidly following both protein supplements but exhibited a significantly greater EAA/BCAA/leucinemia following BLG (p < 0.05 for all). MPS increased significantly in both FED (~52%) and FED-EX (~58%) states, with no significant differences between supplements. Conclusions: Both BLG and WPI effectively stimulated MPS doses in young healthy males, with BLG offering an advantage in EAA/BCAA/LEU bioavailability. It follows that future research should explore the potential of BLG in populations exhibiting anabolic resistance and exercise anabolism deficiency, such as older adults as well as frail and clinical populations, to assess its utility in preserving muscle mass under conditions of suboptimal protein intake.

Objectives: The impact of combining animal and plant protein sources on digestibility is unclear, despite their increasing clinical use. Using a non-invasive dual stable isotope tracer approach, we assessed the digestibility, bioavailability and utilization of distinct protein blends in older adults, and associated plasma amino acid profiles and muscle protein synthesis (MPS) rates. Methods: Thirty-two older men (69 ± 3 y) consumed one of four protein blends (A (51:49, casein/soy); B and C (35:25:20:20, whey/casein/soy/pea); D (80:20, casein/whey)) alongside primed constant infusions of [1,2-¹³C₂] leucine for 8 h. Arterialized blood and vastus lateralis muscle biopsies were collected during a trickle feed protocol with all blends providing 20 g total protein, universally labeled ¹³C-spirulina, and ²H-cell free amino acid mix to determine digestibility. This trial was registered at Clinicaltrials.gov (ID-NCT07038655). Results: No differences (¹³C:²H ratios) were found in digestibility between the protein blends (p > 0.05). Mean (±SEM) fed state MPS at 2.5 h was 0.078 ± 0.009%/h, 0.075 ± 0.012%/h, 0.085 ± 0.007%/h and 0.065 ± 0.011%/h for drinks A, B, C and D, respectively, with a main time effect observed (p < 0.01), but no significant differences between drinks. Plasma essential amino acids (EAAs) increased significantly from baseline for all blends by 40 min (p < 0.05), with no differences between blends at any time point. Conclusions: These findings suggest that protein quantity (and/or leucine content), rather than composition, appears to be the most important factor driving MPS. Future work should focus on clinical populations where protein requirements and digestibility characteristics may differ.

Background: Beta-lactoglobulin (BLG) is a protein found within whey protein (WP) that is rich in essential amino acids, most notably, leucine (LEU). LEU is considered the most potent EAA in the postprandial stimulation of muscle protein synthesis (MPS), such that sub-optimal protein/essential amino acid (EAA) doses containing higher LEU content elicit muscle anabolism comparable to larger protein doses. Here we explored the effects of naturally LEU-rich BLG (~10 g protein) versus isonitrogenous whey protein isolate (WPI, ~10g) on MPS. Methods: Ten healthy young men (26 ± 2 y; 179 ± 2 cm; 81 ± 3 kg) received BLG (1.57g LEU) or WPI (1.02g LEU) in a randomised double-blind cross-over fashion. A primed constant intravenous infusion of [1,2 13C2] LEU was used to determine MPS (isotope ratio mass spectrometry) at baseline and in response to feeding (FED) and feeding-plus-exercise (FED-EX; 6X8 unilateral leg extensions; 75% 1-RM). Plasma insulin and EAA’s were quantified. Results: Plasma EAA, branched chain amino acid (BCAA) and LEU concentrations increased rapidly following both protein supplements but exhibited a significantly greater EAA/BCAA/leucinemia, following BLG (P< 0.05 for all). MPS increased significantly in both FED and FED-EX (n = 8) states, with no significant differences evident between supplements. Conclusions: Both BLG and WPI effectively stimulated MPS doses in young healthy males, with BLG offering an advantage in EAA/BCAA/leucine bioavailability. It follows that future research should explore the potential of BLG in populations exhibiting anabolic resistance and exercise anabolism-deficiency, such as older adults, also in frail and clinical populations, to assess its utility in preserving muscle mass under conditions of sub-optimal protein intake.