The DOI matches its Crossref record; 37 of the 38 references it cites were found in a registry or an index.
Minced beef is more rapidly digested and absorbed than beef steak, resulting in greater postprandial protein retention in older men
Open accessAbstract
Background Older individuals generally experience a reduced food-chewing efficiency. As a consequence, food texture may represent an important factor that modulates dietary protein digestion and absorption kinetics and the subsequent postprandial protein balance.Objective We assessed the effect of meat texture on the dietary protein digestion rate, amino acid availability, and subsequent postprandial protein balance in vivo in older men.Design Ten older men (mean ± SEM age: 74 ± 2 y) were randomly assigned to a crossover experiment that involved 2 treatments in which they consumed 135 g of specifically produced intrinsically L-[1-(13)C]phenylalanine-labeled beef, which was provided as beef steak or minced beef. Meat consumption was combined with continuous intravenous L-[ring-(2)H5]phenylalanine and L-[ring-(2)H2]tyrosine infusion to assess beef protein digestion and absorption kinetics as well as whole-body protein balance and skeletal muscle protein synthesis rates.Results Meat protein-derived phenylalanine appeared more rapidly in the circulation after minced beef than after beef steak consumption (P < 0.05). Also, its availability in the circulation during the 6-h postprandial period was greater after minced beef than after beef steak consumption (61 ± 3% compared with 49 ± 3%, respectively; P < 0.01). The whole-body protein balance was more positive after minced beef than after beef steak consumption (29 ± 2 compared with 19 ± 3 μmol phenylalanine/kg, respectively; P < 0.01). Skeletal muscle protein synthesis rates did not differ between treatments when assessed over a 6-h postprandial period.Conclusions Minced beef is more rapidly digested and absorbed than beef steak, which results in increased amino acid availability and greater postprandial protein retention. However, this does not result in greater postprandial muscle protein synthesis rates. This trial was registered at clinicaltrials.gov as NCT01145131.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Furthermore, Pennings et al. [73] observed ∼61% and ∼49% availability of amino acids from minced beef and beef steak over a 6-h postprandial period, respectively.”
From Nutritional Considerations for the Vegan Athlete (2023) · cites this paper as [73]
Citations
Cites
Sarcopenia: European consensus on definition and diagnosis
Cruz-Jentoft, A. J., Baeyens, J. P., Bauer, J. M., Boirie, Y., Cederholm, T., Landi, F., Martin, F. C., Michel, J.-P., Rolland, Y., Schneider, S. M., et al. (2010) · Age and Ageing · doi:10.1093/ageing/afq034 · Cited by 11,601
Slow and fast dietary proteins differently modulate postprandial protein accretion
Boirie, Y., Dangin, M., Gachon, P., Vasson, M.-P., Maubois, J.-L., & Beaufrère, B. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14930 · Cited by 1,453
Anabolic signaling deficits underlie amino acid resistance of wasting, aging muscle
Cuthbertson, D., Smith, K., Babraj, J., Leese, G., Waddell, T., Atherton, P., Wackerhage, H., Taylor, P. M., & Rennie, M. J. (2005) · The FASEB Journal · doi:10.1096/fj.04-2640fje · Cited by 1,211
Moore, D. R., Robinson, M. J., Fry, J. L., Tang, J. E., Glover, E. I., Wilkinson, S. B., Prior, T., Tarnopolsky, M. A., & Phillips, S. M. (2009) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.2008.26401 · Cited by 973
Katsanos, C. S., Kobayashi, H., Sheffield-Moore, M., Aarsland, A., & Wolfe, R. R. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00488.2005 · Cited by 923
Leucine. A possible regulator of protein turnover in muscle.
Buse, M. G., & Reid, S. S. (1975) · Journal of Clinical Investigation · doi:10.1172/jci108201 · Cited by 744
Pennings, B., Boirie, Y., Senden, J. M., Gijsen, A. P., Kuipers, H., & van Loon, L. J. (2011) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.110.008102 · Cited by 656
The digestion rate of protein is an independent regulating factor of postprandial protein retention
Dangin, M., Boirie, Y., Garcia-Rodenas, C., Gachon, P., Fauquant, J., Callier, P., Ballèvre, O., & Beaufrère, B. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.280.2.e340 · Cited by 572
Abumrad, N. N., Rabin, D. D., Diamond, M. P., & LACY, W. W. (1981) · Metabolism · doi:10.1016/0026-0495(81)90074-3 · Cited by 569
Volpi, E., Mittendorfer, B., Rasmussen, B. B., & Wolfe, R. R. (2000) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.85.12.7021 · Cited by 464
Cited by
Sorted by citations
Protein content and amino acid composition of commercially available plant-based protein isolates
Gorissen, S. H. M., Crombag, J. J. R., Senden, J. M. G., Waterval, W. A. H., Bierau, J., Verdijk, L. B., & van Loon, L. J. C. (2018) · Amino Acids · doi:10.1007/s00726-018-2640-5 · Cited by 1,169
The Western Diet–Microbiome-Host Interaction and Its Role in Metabolic Disease
Zinöcker, M. K., & Lindseth, I. A. (2018) · doi:10.20944/preprints201803.0064.v1 · Cited by 776
“mincing of meat) can break the cell structures and increase the total availability of nutrients [44].”
The Skeletal Muscle Anabolic Response to Plant- versus Animal-Based Protein Consumption
van Vliet, S., Burd, N. A., & van Loon, L. J. (2015) · The Journal of Nutrition · doi:10.3945/jn.114.204305 · Cited by 651
“In addition, this work has shown that a total of 50–70% of the dietary protein–derived AAs from milk and beef protein become available in systemic circulation when assessed over a 5- to 6-h postprandial period (17, 22, 29).”
BackgroundAging is accompanied by a blunted muscle protein synthetic response to protein ingestion
Wall, B. T., Gorissen, S. H., Pennings, B., Koopman, R., Groen, B. B. L., Verdijk, L. B., & van Loon, L. J. C. (2015) · PLOS ONE · doi:10.1371/journal.pone.0140903 · Cited by 352
Self-citationRémond, D., Shahar, D. R., Gille, D., Pinto, P., Kachal, J., Peyron, M., dos Santos, C. N., Walther, B., Bordoni, A., Dupont, D., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.4030 · Cited by 351
“However, the technological processing of meat (mincing, cooking conditions) could significantly affect meat protein digestion rate, and protein assimilation [389, 390], and thus offer solutions to counteract the chewing inefficiency problems.”
Background
Metadata
- Authors
- Pennings, B., Groen, B. B., van Dijk, J.-W., de Lange, A., Kiskini, A., Kuklinski, M., Senden, J. M., & van Loon, L. J.
- Venue
- The American Journal of Clinical Nutrition
- Publisher
- Elsevier BV
- Published
- 2013-07
- Volume
- 98
- Issue
- 1
- Pages
- 121-128
- ISSN
- 0002-9165 (ISSN-L)
- OpenAlex
- W2138339477
- Semantic Scholar
- 0b964dcf6f624542bb73655625de88bdedba3220
- Cited by
- 167
- References
- 38
- Citations by year
- 2026: 8 · 2025: 11 · 2024: 7 · 2023: 13 · 2022: 16 · 2021: 15 · 2020: 16 · 2019: 18 · 2018: 14 · 2017: 14 · 2016: 12 · 2015: 14 · 2014: 9
- FWCI
- 6.77
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- American Journal of Clinical Nutrition (publishedVersion)
- PubMed (publishedVersion)
- Research Publications (Maastricht University) (publishedVersion, other-oa)
- Research Bank (Australian Catholic University) (submittedVersion)
- Research Publications (Maastricht University) (submittedVersion, other-oa)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Health Sciences › Medicine › Physiology (medical) › Nutrition and Health in Aging
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Nutrition and Physiology
- Keywords
- ground beef, beef steaks, meat texture, protein digestion, protein absorption, amino acid availability, phenylalanine, tyrosine, skeletal muscle protein synthesis, older men, aging, masticatory efficiency
- MeSH terms
- Aged, Animals, Biological Availability, Blood Glucose, Carbon Isotopes, Cattle, Dietary Proteins, Digestion, Humans, Male, Meat, Muscle Proteins, Phenylalanine, Surveys and Questionnaires, Tyrosine, Muscle, Skeletal, Cross-Over Studies, Postprandial Period
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
