Human Muscle Protein Synthesis Rates after Intake of Hydrolyzed Porcine-Derived and Cows’ Milk Whey Proteins—A Randomized Controlled Trial

Nutrients

ErikT. Hansen¹  Gerrit van Hall²  Søren Reitelseder³  Lars Holm³  Anders Sjödin⁴  LineQ. Bendtsen⁴  Arne Astrup⁴  Christian Ritz⁴  TanjaK. Thorning⁴ 

[1] Danish Crown Ingredients, DK-1711 Copenhagen V, Denmark;Department of Biomedical Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, DK-2200 Copenhagen N, Denmark;Institute of Sports Medicine Copenhagen, Department of Ortopaedic Surgery M, Bispebjerg Hospital, DK-2400 Copenhagen NV, Denmark;The Department of Nutrition, Exercise and Sports, Faculty of Science, University of Copenhagen, DK-1958 Frederiksberg C, Denmark;

关键词: dietary proteins;    porcine proteins;    muscle protein synthesis;    amino acids;    FSR;   

DOI  :  10.3390/nu11050989

来源: DOAJ

【 摘 要 】

Background: Whey protein has been shown to be one of the best proteins to stimulate muscle protein synthesis rate (MPS), but other high quality proteins, e.g., animal/porcine-derived, could have similar effects. Objective: To investigate the effects of hydrolyzed porcine proteins from blood (HPB) and muscle (HPM), in comparison to hydrolyzed whey protein (HW), on MPS after intake of 15 g alone or 30 g protein as part of a mixed meal. We hypothesized that the postprandial MPS would be similar for porcine proteins and whey protein. Design: Eighteen men (mean ± SD age: 24 ± 1 year; BMI: 21.7 ± 0.4 kg/m²) participated in the randomized, double-blind, three-way cross-over study. Subjects consumed the three test products (HPB, HPM and HW) in a random order in two servings at each test day. Serving 1 consisted of a drink with 15 g protein and serving 2 of a drink with 30 g protein together with a mixed meal. A flood-primed continuous infusion of (ring-¹³C₆) phenylalanine was performed and muscle biopsies, blood and urine samples were collected for determination of MPS, muscle free leucine, plasma amino acid concentrations and urea excretion. Results: There were no statistical differences between the MPS measured after consuming 15 g protein alone or 30 g with a mixed meal (p = 0.53) of HPB (0.048 ± 0.007 vs. 0.049 ± 0.008%/h, resp.), HPM (0.063 ± 0.011 vs. 0.062 ± 0.011 %/h, resp.) and HW (0.058 ± 0.007 vs. 0.071 ± 0.013%/h, resp.). However, the impact of protein type on MPS reached statistical tendency (HPB vs. HPM (p = 0.093) and HPB vs. HW (p = 0.067)) with no difference between HPM and HW (p = 0.88). Plasma leucine, branched-chain, essential and total amino acids were generally higher for HPB and HW than HPM (p < 0.01), which reflected their content in the proteins. Muscle-free leucine was higher for HPB than HW and HPM (p < 0.05). Conclusion: Hydrolyzed porcine proteins from blood and muscle resulted in an MPS similar to that of HW, although with a trend for porcine blood proteins to be inferior to muscle proteins and whey. Consequently, these porcine-derived muscle proteins can be used similarly to whey protein to support maintenance of skeletal muscle as part of supplements and ingredients in foods.

【 授权许可】

Unknown