Postprandial whole-body protein metabolism after a meat meal is
influenced by chewing efficiency in elderly subjects1⫺3
Didier Rémond, Marie Machebeuf, Claude Yven, Caroline Buffière, Laurence Mioche, Laurent Mosoni, and
Philippe Patureau Mirand
ABSTRACT
Background: The rate of protein digestion affects protein utilization
in elderly subjects. Although meat is a widely consumed protein
source, little is known of its digestion rate and how it can be affected
by the chewing capacity of elderly subjects.
Objectives: We used a [1-13C]leucine balance with a single-meal
protocol to assess the absorption rate of meat protein and to estimate
the utilization of meat protein in elderly subjects with different
chewing efficiency.
Design: Twenty elderly volunteers aged 60 –75 y were involved in
the study. Ten of them had healthy natural dentition, and the other 10
were edentulous and wore complete dentures. Whole-body fluxes of
leucine, before and after the meal (120 g beef meat), were measured
with the use of a [1-13C]leucine intravenous infusion.
Results: A rapid increase in plasma aminoacidemia and plasma
leucine entry rate was observed after meat intake in dentate sub-
jects. In complete denture wearers the increase in leucine entry
rate was delayed (P 쏝 0.05), and the amount of leucine appearing
in peripheral blood during the whole postprandial period was
lower than in dentate subjects (P 쏝 0.01). Postprandial whole-
body protein synthesis was lower in denture wearers than in
dentate subjects (30% compared with 48% of leucine intake,
respectively; P 쏝 0.05).
Conclusion: Meat proteins could be classified as fast digested pro-
teins. However, this property depends on the chewing capacity of
elderly subjects. This study showed that meat protein utilization for
protein synthesis can be impaired by a decrease in the chewing
efficiency of elderly subjects. Am J Clin Nutr 2007;85:
1286 –92.
KEY WORDS Leucine kinetics, protein metabolism, meat,
chewing efficiency, elderly
INTRODUCTION
Aging is associated with a decline in body muscle mass, lead-
ing to a decrease in physical autonomy and an increase in vul-
nerability of elderly people. This loss of muscle mass must result
from an imbalance between the constant synthesis and degrada-
tion of muscle proteins. An alteration of muscle protein anabo-
lism in older subjects in the fed state was reported (1, 2), in
relation with a decrease in muscle sensitivity to a postprandial
increase of plasma free amino acids and in particular leucine
(3–5). This phenomenon could explain the slow erosion of mus-
cle mass during aging.
1286 Am J Clin Nutr 2007;85:1286 –92. Printed in USA. © 2007 American Society for Nutrition
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In response, dietary strategies aimed at optimizing a postpran-
dial increase in plasma amino acids, without increasing total
daily protein intake, were proposed. The use of rapidly digested
proteins (6), concentration of daily protein supply in one meal (7,
8), and specific amino acid supplementation (9, 10) were all
shown to improve protein retention, nitrogen balance, or muscle
protein synthesis in elderly subjects.
A rapid and intense rise in postprandial aminoacidemia is
therefore beneficial for protein anabolism in elderly subjects.
However, although the amino acid composition and the total
digestibility of all protein sources are now well known, the ki-
netics of their digestion and their impact on the postprandial rise
of plasma amino acids are still poorly described. Although a lot
of studies were done with milk proteins (6, 11), much less is
known of meat proteins, a high-quality (12) and widely con-
sumed protein source.
In addition, it seems possible that, for meat, this property could
vary according to the subject and in particular to the person’s
chewing efficiency (individual capability to transform a lump of
food into a proper swallowable food bolus). Aging is often as-
sociated with a decrease in chewing efficiency, leading to a lower
disruption of swallowed meat pieces (13). Chewing efficiency is
even worse in subjects with impaired mastication such as denture
wearers (14). Wearing dentures is known to lead to gastrointes-
tinal discomfort (15), but it could also decrease protein utilization
efficiency and modify the absorption kinetics of amino acids.
Therefore, this study was designed to determine the effect
of a meat meal on the postprandial variations in plasma ami-
noacidemia and whole-body protein metabolism in elderly
subjects. It was also designed to assess how chewing effi-
ciency can modify these indicators, with 2 groups of subjects
having different dentition characteristics, namely healthy
dentate subjects and full-denture wearers.
1
From the Institut National de la Recherche Agronomique, UMR 1019,
Unité de Nutrition Humaine, Centre de Clermont-Ferrand-Theix, Saint
Genès-Champanelle, France.
2
Supported by the Institut National de la Recherche Agronomique,
France.
3
Reprints not available. Address correspondence to D Rémond, Unité de
Nutrition Humaine, INRA Theix, Saint Genès-Champanelle, F-63122,
France. E-mail: dremond@clermont.inra.fr.
Received July 19, 2006.
Accepted for publication January 5, 2007.
 MEAT PROTEIN ASSIMILATION RATE IN THE ELDERLY
TABLE 1
Characteristics of the 2 groups of healthy elderly subjects with either healthy natural dentition or complete dental prosthesis1
Natural dentition
Women Men
(n ҃ 4) (n ҃ 6)
Age (y) 67.5 앐 1.9 67.8 앐 1.1
Body mass (kg) 65.3 앐 3.7 74.6 앐 2.6
BMI (kg/m2) 26.0 앐 1.3 25.6 앐 1.2
1
All values are x៮ 앐 SEM.
SUBJECTS AND METHODS
Materials
Beef meat was obtained from semimembranous muscle kept
15 d postmortem at 4 °C. Then it was cut into slices, vacuum-
packed, cooked at 65 °C, and stored at Ҁ18 °C. Before use, the
meat was thawed by immersing packs in warm water and then
grilled until the inner temperature reached 65 °C.
L-[1-13C]leucine (99 atom%, determined by the manufacturer)
and sodium [13C]bicarbonate (99 atom%, determined by the man-
ufacturer) were supplied by Eurisotop (Gif-sur-Yvette, France). So-
lutions of tracers were tested for sterility and pyrogenicity before use
and filtered through a 0.22-␮m filter during each experiment.
Subjects
Twenty healthy elderly subjects (aged 60 –75 y) participated in
the study. Ten of them were dentate (ND) with at least 8 pairs of
natural postcanine teeth. The other 10 subjects were edentulous
(DP) for 욷5 y. They wore full dentures with a correct interoc-
clusal relation and good stability. The current dentures had been
in place for 욷6 mo, and subjects felt comfortable with them.
Chewing performance of these subjects is presented elsewhere
(16, 17). Chewing efficiency can be evaluated from oral indica-
tors (such as bite force and chewing duration), from the particle
size distribution after a given number of strokes on a brittle
material, or from bolus properties. It was shown that the denture
wearers of the present study swallowed fewer disorganized boli
than the dentate subjects (16). All subjects were in good general
health without medical treatment and ate meat on a regular basis.
Volunteer characteristics [age, body mass, body mass index
(in kg/m2)] in each group are given in Table 1. The study was
approved by the local ethical committee (CCPPRB-Auvergne),
and all subjects gave their informed consent.
Experimental protocol
Whole-body fluxes of leucine before and after the meal were
measured with the use of [1-13C]leucine as an intravenous tracer.
After an overnight fast, a catheter was inserted retrogradely into
a dorsal vein of the hand for blood sampling after introduction of
the hand in a 60 °C heated ventilated box. A second catheter was
inserted into a vein of the contralateral arm for tracer infusion.
After baseline collection of blood and breath samples, a priming
dose of NaH13CO2 (0.1 mg/kg) and [1-13C]leucine (3.6 ␮mol/kg)
was administered. A continuous infusion of [1-13C]leucine
(0.06 ␮mol · kgҀ1 · minҀ1) was then begun and continued for 580
min. After 150 min of infusion, the meat meal (a steak of 120 g)
was served to the volunteers. They were allowed to add salt and
to drink a glass of water. They had to ingest the whole meal within
20 min. Blood and breath samples were taken before the meal
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1287
Dental prosthesis P (ANOVA)
Women Men
(n ҃ 5) (n ҃ 5) Dentition Sex
72.6 앐 1.2 64.8 앐 2.6 0.5630 0.0487
61.6 앐 2.2 73.2 앐 2.3 0.3655 0.0014
25.6 앐 1.1 25.2 앐 1.4 0.7521 0.7541
(Ҁ60, Ҁ40, Ҁ20, and 0 min) and after the meal at 20-min inter-
vals for the first 300 min, and then at 340 and 420 min. Blood
samples (앒5 mL) were collected in tubes containing lithium-
heparin and immediately centrifuged at 1500 ҂ g for 10 min at
4 °C. Supernatant fluid was subsampled, frozen in liquid nitro-
gen, and stored at Ҁ80 °C. Expired breath samples were col-
lected and stored in 10-mL evacuated tubes (Becton-Dickinson,
Grenoble, France). Production rates of carbon dioxide were mea-
sured during 20-min periods (starting at Ҁ80, 20, 80, 140, 200,
280, 400 min) by open-circuit indirect calorimetry (Deltatrac;
Datex, Geneva, Switzerland).
Sample analysis
The 13C enrichments of leucine and ␣-ketoisocaproate (KIC)
were measured by gas chromatography–mass spectrometry (model
5971A; Hewlett-Packard, Paris, France) with the use of tertiary-
butyldimethylsilyl derivatives as described by Boirie et al (18). The
13
C enrichments of carbon dioxide were measured on a gas chro-
matography combustion isotope ratio mass spectrometer (Fisons
Instruments, VG Isotech, Middlewich, United Kingdom).
Plasma concentrations of amino acids were measured after
deproteinization with sulfosalicylic acid by ion-exchange chro-
matography (Bio-Tek Instruments ARL, St Quentin Yvelines,
France). Plasma urea concentrations were measured with the use
of enzymatic reactions on an autoanalyser (Cobas Mira; Roche
Diagnostic Systems, Neuilly sur Seine, France).
Calculations
Leucine fluxes were calculated from the time-dependent evo-
lution of the 13C enrichments of plasma leucine and KIC and
from expired carbon dioxide. The experimental design allowed
the determination of the rate of total leucine appearance (Tot Leu
Ra) in the peripheral circulation and the rate of total leucine
disappearance (Tot Leu Rd) from plasma, which is the sum of the
fluxes of leucine, either oxidized (Leu Ox) or used for protein
synthesis (nonoxidative leucine disposal or NOLD).
The equations used have been reported in detail by Boirie et al
(18). Briefly, the equations include the following:
Tot Leu Ra ⫽ (IR ⫺ (pV ⫻ Cleu(t) ⫻ dEleu/dt))/Eleu(t)
(1)
Tot Leu Rd ⫽ Tot leu Ra ⫺ (pV ⫻ dCleu/dt) (2)
Leu Ox ⫽ (VCO2 ⫻ ECO2)/(k ⫻ EKIC) (3)
NOLD ⫽ Tot Leu Rd ⫺ Leu Ox (4)
where IR is [13C]leucine infusion rate (␮mol · kgҀ1 · minҀ1), p is
the correction factor of the pool size for instant mixing
 1288 RÉMOND ET AL

TABLE 2
Leucine concentrations and flux kinetics after meal ingestion in healthy elderly subjects with healthy natural dentition or complete dental prosthesis1

Natural dentition Dental prosthesis

(n ҃ 10) (n ҃ 10) P (ANOVA)

[EAA]
Baseline (␮mol/L) 780 앐 24 790 앐 27 0.709
Ymax (␮mol/L) 1852 앐 64 1766 앐 83 0.452
tYmax (min) 134 앐 13 172 앐 20 0.153
[Leu]
Baseline (␮mol/L) 122 앐 5 118 앐 6 0.467
Ymax (␮mol/L) 355 앐 12 340 앐 20 0.542
tYmax (min) 136 앐 11 178 앐 20 0.089
Tot Leu Ra
Baseline (␮mol · kgҀ1 · minҀ1) 1.41 앐 0.06 1.39 앐 0.08 0.914
Ymax (␮mol · kgҀ1 · minҀ1) 3.14 앐 0.15 2.68 앐 0.20 0.091
tYmax (min) 98 앐 10 150 앐 18 0.012
AUC (␮mol/kg) 239 앐 11 185 앐 15 0.004
NOLD
Baseline (␮mol · kgҀ1 · minҀ1) 1.15 앐 0.05 1.14 앐 0.07 0.862
Ymax (␮mol · kgҀ1 · minҀ1) 2.47 앐 0.16 1.97 앐 0.08 0.047
tYmax (min) 96 앐 7 164 앐 15 0.002
AUC (␮mol/kg) 140 앐 20 89 앐 9 0.015
Leu Ox
Baseline (␮mol · kgҀ1 · minҀ1) 0.25 앐 0.02 0.23 앐 0.02 0.576
Ymax (␮mol · kgҀ1 · minҀ1) 0.78 앐 0.04 0.70 앐 0.06 0.293
tYmax (min) 178 앐 16 174 앐 16 0.941
AUC (␮mol/kg) 100 앐 9 104 앐 11 0.862
1
All values are x៮ 앐 SEM. EAA is the sum of threonine, valine, methionine, isoleucine, leucine, phenylalanine, histidine, and lysine. Tryptophan was not
properly quantified and therefore not considered. [EAA] and [Leu] are arterial concentrations of EAA and leucine, respectively. Tot Leu Ra, total leucine rate
of appearance in plasma; NOLD, nonoxidative leucine disposal; Leu Ox, total leucine oxidized; Ymax, zenith of values; tYmax, time to reach zenith value; AUC,
area under the curve of postprandial minus basal fluxes.

(p ҃ 0.25), and V is the leucine pool size (V ҃ 0.5 L/kg body wt).
The choice of these factors was previously discussed (18). Cleu(t)
is the mean plasma leucine concentration between 2 sampling
times (in ␮mol/L), dEleu/dt represents the time-dependent vari-
ations of [13C]leucine enrichment (in mol % excess), Eleu(t) is the
mean [13C]leucine enrichment between 2 sampling times (in mol
% excess), VCO2 is the carbon dioxide production rate (in
␮mol · kgҀ1 · minҀ1), ECO2 and EKIC are [13C]CO2 and [13C]KIC
enrichment (in mol % excess), respectively. The k is a correcting
factor for incomplete recovery of carbon dioxide in the breath; it
was assumed to gradually increase from a fasted value of 0.76 to
a maximum value of 0.91, 60 min after the beginning of the meal
(19). Postabsorptive leucine fluxes were calculated by averaging
sampling times from Ҁ60 to 0 min. Leucine intake was calcu-
lated assuming 2.29 g leucine/100 g cooked meat (20).
Statistical analysis
Time and time ҂ group effects on arterial concentrations and
leucine fluxes were tested with the use of the repeated option of
the PROC MIXED procedure of SAS (SAS/STAT Users Guide,
release 8.1, 2000; SAS Institute Inc, Cary, NC), with subjects as
random effect and with time, group, and time ҂ group as factors.
When significant time ҂ group interaction was found, the LS-
MEANS procedure was used to test differences at specific times,
between groups, and within groups compared with baseline.
Each postprandial curve was characterized by its zenith
(Ymax), by the time at which Ymax was observed (tYmax), by
baseline value (postabsorptive value), and postprandial area
under the curve (AUC; calculated by integrating the differ-
ence between postabsorptive flux and observed flux, trape-
zoidal method). Data were analyzed by analysis of variance
with the use of the GLM procedure of SAS, with dentition and
sex as factors.
RESULTS
Postabsorptive concentrations in measured essential amino
acids (EAAs) were not different between groups (Table 2). They
were unchanged within the 20 min after the beginning of the
meal. Then they sharply increased in both groups (Figure 1).
From 100 to 140 min, plasma EAA concentrations were greater
for the ND group than for the DP group. From 180 to 420 min, the
concentrations decreased in both groups. At 420 min, concen-
trations were still higher than postabsorptive values. Ymax and
tYmax for EAAs were not affected by chewing efficiency (Table
2). In both groups, plasma leucine kinetics was similar to EAA
kinetics (Figure 1). In the DP group, tYmax tended to be 40 min
later than in the ND group. The increase in plasma leucine con-
centrations as a result of meal intake in the ND group averaged
230 ␮mol/L.
The kinetics of plasma urea concentrations were not different
between groups (Figure 2). Increase in the carbon dioxide pro-
duction rate after the meal tended to be greater (P ҃ 0.080) in the
ND group than in the DP group (Figure 2). However, total post-
prandial increase in carbon dioxide production was not affected
by chewing efficiency.

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 MEAT PROTEIN ASSIMILATION RATE IN THE ELDERLY 1289
2000 9
*
1800 *
8
1600

7
Plasma EAA (µmol/L)ole

1400

Plasma urea (mmol/L)

1200
6
1000
5
800

600 4

400
3
200

0 2
-100 0 100 200 300 400 500 -100 0 100 200 300 400 500
Time (min) Time (min)

250
400

*
350 * * 225

300 *

CO2 production (mL/min)

Plasma leucine (µmol/L) ole

200
250

175
200

150 150

100
125
50

100
0
-100 0 100 200 300 400 500
-100 0 100 200 300 400 500
Time (min)
Time (min)

FIGURE 1. Mean (앐 SEM) plasma essential amino acids (EAAs) and
leucine concentrations during the last 60 min of the postabsorptive period and
the first 420 min after a meat meal in 2 groups of volunteers having either
healthy natural dentition (E; n ҃ 10) or complete dental prosthesis (F; n ҃
10). Data were analyzed by a mixed-model ANOVA, and time ҂ group
interaction was significant for both measures (P 쏝 0.01). Statistical differ-
ences between the 2 groups: *P 쏝 0.05. Time effect was significant for both
measures (P 쏝 0.001), and lines at the bottom of the graph indicate a signif-
icant difference (P 쏝 0.05) from baseline for each curve.
FIGURE 2. Mean (앐 SEM) plasma urea concentrations and carbon
dioxide (CO2) productions during the last 60 min of the postabsorptive period
and the first 420 min after a meat meal in 2 groups of volunteers having either
healthy natural dentition (E; n ҃ 10) or complete dental prosthesis (F; n ҃
10). Data were analyzed by a mixed-model ANOVA, and time ҂ group
interaction was significant for carbon dioxide production (P 쏝 0.01) but not
for urea (P ҃ 0.501). Time effect was significant for both measures (P 쏝
0.001), and lines at the bottom of the graph indicate a significant difference
(P 쏝 0.05) from baseline for each curve.

The variations in 13C enrichment of plasma leucine and KIC
throughout the sampling period are presented in Figure 3. Before
the meal, [13C]leucine and [13C]KIC enrichments reached a pla-
teau (4.21 앐 0.07 and 3.91 앐 0.08 mol % excess, respectively),
and no significant differences were observed between premeal
means (Ҁ60 to 0 min). Postabsorptive fluxes of leucine (Tot
Leu Ra, Leu NOLD, and Leu Ox) were not different for the ND
and DP groups (Table 2). In both groups Tot Leu Ra was not
affected during the 20 min after the onset of the meal. There-
after, it rapidly increased for the ND group to reach a maxi-
mum at 앒100 min (Figure 4). The increase was more pro-
gressive in the DP group; the maximum of Tot Leu Ra tended
to be lower (P ҃ 0.091) than for the ND group and was reached
50 min later (Table 2). In both groups Tot Leu Ra returned to
baseline concentrations before the end of the sampling ses-
sion. Tot Leu Ra AUC was 23% lower in the DP group
(P 쏝 0.01) than in the ND group.
Leu Ox kinetics were different in the ND and PD groups
(Figure 4) with Leu Ox increase tending to be delayed in the DP
group. However, postprandial leucine oxidation (Leu Ox AUC)
was not affected by chewing efficiency. Leu NOLD kinetics
(Figure 4) in both groups displayed a similar pattern to changes
in Tot Leu Ra. Leu NOLD AUC was 36% lower in the DP group
(P 쏝 0.05) than in the ND group.
DISCUSSION
The present study was designed to characterize the modifica-
tions of whole-body protein metabolism in elderly subjects after
a meat meal and to determine how it is affected by chewing
efficiency. For this purpose, the leucine appearance rate and the
NOLD rate were compared in 2 groups of elderly subjects: one
group of subjects with a good natural dentition and another group
of complete denture wearers known to have a poor chewing
efficiency (21). Postprandial increase in the leucine appearance
rate was used as a surrogate of meat leucine entry rate because
leucine meat was not labeled and because postprandial variations
in endogenous leucine appearance rates were reported to be sim-
ilar in slowly and fast digested proteins (6). However, it could
underestimate meat leucine entry rate because of the transitory

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 1290 RÉMOND ET AL

**
5.5

**

**
3.0

**
5.0 *
Leucine enrichment (mol % excess) B

4.5 2.5

Tot Leu Ra ( µmol·kg ·min )

-1
4.0
2.0

-1
**
3.5 *

**
**
**
3.0
1.5
2.5
2.0 1.0
1.5
1.0 0.5

0.5
0.0
0.0 -100 0 100 200 300 400 500
-100 0 100 200 300 400 500
Time (min)
Time (min) 1.0

5.5
5.0 0.8

Leu Ox (µmol·kg ·min )

*

-1
4.5
KIC enrichment (mol % excess)

**
-1
4.0 0.6

3.5
3.0 0.4

2.5
2.0 0.2

1.5
1.0 0.0
0.5 -100 0 100 200 300 400 500
Time (min)
0.0 3.0
-100 0 100 200 300 400 500
Time (min)
2.5
**

FIGURE 3. Mean (앐 SEM) 13C enrichments of plasma leucine and *

**

*
␣-ketoisocaproate (KIC) during the last 60 min of the postabsorptive period
NOLD (µmol·kg-1·min-1)

2.0
and the first 420 min after a meat meal in 2 groups of volunteers having either
healthy natural dentition (E; n ҃ 10) or complete dental prosthesis (F; n ҃
10). Data were analyzed by a mixed-model ANOVA, and time ҂ group 1.5
interaction was significant for 13C enrichment of leucine (P 쏝 0.001) but not
for 13C enrichment of KIC (P ҃ 0.414). Statistical differences between the 2
1.0
groups: *P 쏝 0.05, **P 쏝 0.01. Time effect was significant for both measures
(P 쏝 0.001), and lines at the bottom of the graph indicate a significant
difference (P 쏝 0.05) from baseline for each curve. 0.5

postprandial decrease in whole-body protein degradation but in
a similar way in both groups.
Postprandial increase in the plasma amino acid concentrations
observed in the present study was in agreement with data re-
ported for young adults after a beef meat meal (22–24), with the
highest concentrations being generally recorded 90 –180 min
after the beginning of the meal. In the present work, a close
relation was observed between the variations in plasma leucine
concentrations and plasma leucine entry rate.
In reference to their absorption rate, proteins have been clas-
sified as “fast” or “slow” proteins (11). The present observations
indicate that meat proteins could be categorized as fast proteins;
variations in aminoacidemia and leucine appearance rate are
closer to what is observed with whey proteins (fast proteins) than
with casein (slow proteins) (6, 11). Together with its high-protein
content, the rapid digestion of meat makes it a good source of
protein to produce a rapid and intense rise in postprandial ami-
noacidemia in elderly subjects.
0.0
-100 0 100 200 300 400 500
Time (min)
FIGURE 4. Mean (앐 SEM) total leucine appearance (Tot Leu Ra) rates,
leucine oxidation (Leu Ox) rates, and nonoxidative leucine disposal (NOLD)
during the last 60 min of the postabsorptive period and the first 420 min after
a meat meal in 2 groups of volunteers having either healthy natural dentition
([circo; ]n ҃ 10) or complete dental prosthesis (F; n ҃ 10). Data were
analyzed by a mixed-model ANOVA, and time ҂ group interaction was
significant for Tot Leu Ra, Leu Ox, and Leu NOLD (P 쏝 0.01). Statistical
differences between the 2 groups: *P 쏝 0.05, **P 쏝 0.01. Time effect was
significant for the 3 measures (P 쏝 0.001), and lines at the bottom of the graph
indicate a significant difference (P 쏝 0.05) from baseline for each curve.
Both the plasma leucine concentration and the total whole-
body rate of appearance of leucine were lower in denture wearers
than in dentate subjects 60 –140 min after the meal, and the
greatest values were reached in denture wearers 앒60 min later
than in dentate subjects. Together with the pattern of carbon

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 MEAT PROTEIN ASSIMILATION RATE IN THE ELDERLY
dioxide production, these observations indicate a delayed ab-
sorption of meat proteins in denture wearers. To flow out of the
stomach, solid food has to be reduced to small-sized particles,
and it was observed in young subjects that incomplete commi-
nution of ham cubes during mastication decreased the gastric
emptying rate (25). With the use of the same subjects and meat
preparation as in the present study, a parallel study was con-
ducted to analyze the effect of chewing impairment on ready-to-
swallow meat boli properties (16). It was shown that denture
wearers swallow fewer disrupted boli than dentate subjects.
Thus, a decrease in the gastric emptying rate could explain the lag
in meat protein absorption observed in the present study. These
observations clearly show that ranking protein according to di-
gestion rate not only depends on the intrinsic quality of the
protein but also on the physiologic characteristics of the con-
sumer, mainly chewing efficiency and gastric emptying rate.
Both of these characteristics can be altered in the elderly (21, 26).
The amount of leucine appearing in peripheral blood during
the whole postprandial period was lower in denture wearers than
in dentate subjects (63% compared with 82% of leucine intake).
This difference is surprising; we were expecting a delay in
leucine appearance but not a difference in the total amount of
leucine absorption. For both groups, the appearance rate returned
to baseline values 2 h before the last sampling time, indicating
that no more detectable amounts of dietary leucine entered the
peripheral blood. Thus, the decrease in total entry rate does not
seem to be attributable to an insufficiently long sampling time. It
could theoretically be due to a higher inhibition of whole-body
proteolysis in denture wearers than in dentate subjects. However,
it seems unlikely because it was shown that postprandial inhibi-
tion of whole-body proteolysis in the elderly is not affected by the
digestion rate (6). In addition, proteolysis inhibition is greater
when leucinemia is higher (4, 27), which is the opposite of what
is observed in denture wearers.
Thus, the lower amount of leucine appearing in plasma of
denture wearers is more likely due to a higher retention of in-
gested leucine in splanchnic organs. Whether it is due to a longer
retention of amino acids in the digestive lumen (incomplete di-
gestion) or to a higher extraction by splanchnic tissues (digestive
tract, liver) remains undetermined. A lower gastric emptying rate
is likely to occur together with prolonged intestinal digestion
because of fewer disrupted pieces of meat. Whether this results
in a lower efficiency in the digestion of meat is unclear because
an increase in transit time could compensate more or less for the
differences in initial buccal disintegration of meat. Few investi-
gators have studied the impact of chewing on digestive processes
and more particularly on meat digestion. Farrell (28) observed
that the degree of mastication required for maximum digestion is
low and that there is no reason to suppose that full denture
wearers are less capable of digesting their food. This study ad-
dressed whole-gut digestibility and did not provide information
on the digestion in the small intestine, where amino acid absorp-
tion takes place. It was shown in subjects with ileostomies that
beef meat proteins (from fried rump steak) have a high (94%) true
ileal digestibility (29). However, swallowing of poorly disrupted
boli could produce a decrease in digestion in the small intestine,
as a consequence of stomach outflow of larger pieces of food,
which may limit protein accessibility for digestive enzymes. This
could lead to a shift in the site of meat digestion, from the small
intestine to the large intestine.
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1291
A greater utilization of dietary leucine in splanchnic tissues in
denture wearers than in dentate subjects also has to be consid-
ered. A high variability in splanchnic extraction of dietary
leucine exists in elderly subjects; its range was 26 – 88% in 6
elderly men (11) and 17.5– 62.6% in 14 elderly women (30). In
addition, a greater splanchnic extraction was reported with
slowly digested proteins when compared with fast digested pro-
teins (6). Although in the present study the magnitude of the
difference in absorption rate was much smaller than between
slowly and fast digested proteins (6), the fact that denture wearers
are chronically exposed to slower absorption rates may induce
adaptation in the long term and lead to an increase in amino acid
splanchnic extraction.
Finally, because of the delayed absorption of meat proteins
and to the lower total amount of amino acids entering peripheral
blood in the postprandial period, whole-body protein synthesis
was lower in denture wearers than in dentate subjects (30%
compared with 48% of leucine intake was used for protein syn-
thesis during the whole postprandial period in dentate subjects
and denture wearers, respectively). Muscle protein metabolism
was not investigated in the present study, which would have
needed muscle biopsy sampling to determine the protein frac-
tional synthesis rate. Nevertheless, the result on whole-body
protein synthesis is consistent with previous experiments show-
ing that muscle protein synthesis sensitivity to feeding is altered
during aging (1, 2). Higher amounts of blood free amino acids are
necessary to stimulate muscle protein synthesis (4, 5, 31, 32). The
increase in postprandial aminoacidemia observed in the present
study in elderly denture wearers was inadequate to reach maxi-
mal stimulation of whole-body protein synthesis.
We thank the physician and nurse of the Human Nutrition Unit for con-
ducting the experiment; to C Pouyet, C Cossoul, and J Prugnaud for mass
spectrometry analysis; and to G Bayle for amino acid analysis.
The authors’ responsibilities were as follows—DR: planned and imple-
mented the study, analyzed statistics, interpreted data, and wrote the manu-
script; MM: volunteer recruitment volunteers and sample collection and
analysis; CY: volunteer recruitment and sample collection and analysis; CB:
volunteer recruitment and sample collection and analysis; L Mioche: study
design and critical revision of the manuscript; L Mosoni: study design and
critical revision of the manuscript; PPM: study design and critical revision of
the manuscript. None of the authors had a conflict of interest.
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