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BY
ACID
COMPOSITION
B. S. SCHWEIGERT,
OF PORK
AND
BARBARA
TAIT GUTHNECK,
D. A. GREENWOOD*
LAMB
CUTS
H. R. KRAYBILL,
AND
Meat Institute
Foundation,
University
of
Chicago, Chicago)
EXPERIMENTAL
Paired pork and lamb cuts were obtained and one cut from each pair was
cooked by recommended methods (7), while the remaining cut was retained for analysis of the uncooked meat. Proximate analysis data were
obtained on the fresh and cooked cuts. The samples were then partially
dehydrated and defatted, finely ground, and retained for the amino acid
studies. All amino acid analyses were made on the dehydrated and defatted samples. From these data and the proximate analyses, the amino
acid content of the crude protein (N X 6.25) and of the fresh cuts was calculated.
The amino acids were liberated from the samples by acid autoclaving
(0.5 gm. of sample in 25 ml. of 3 N HCl for 16 hours at 15 pounds pressure). The amino acid determinations
were made on suitable neutralized
aliquots.
All analyses were carried out on duplicate hydrolysates and
excellent agreement in the values was obtained for the two hydrolywere determined
sates. Leucine, valine, isoleucine, and phenylalanine
* Present address, Department
Logan, Utah.
of Chemistry,
1077
College,
The development
of accurate, sensitive microbiological
methods has
permitted the acquisition of data on the amino acid content of foods and
purified proteins as well as information on the amino acids in body fluids
These
and on the metabolism of the amino acids by the test organisms.
advances have been summarized in several reviews (14).
The data obtained thus far on meats indicate that the amino acid composition of the
protein of the lean tissues of pork, beef, and lamb cuts is very similar,
although some differences in the protein of muscle tissues and organ meats
have been observed in the case of histidine and lysine (5, 6).
The present study was undertaken to obtain further data on the amino
acid content of different pork and lamb cuts, to evaluate different methods
of analysis where indicated, and to obtain further information
on the
stability of the amino acids during cooking of the meats. The data obtained for leucine, valine, isoleucine, phenylalanine,
threonine, histidine,
lysine, arginine, methionine, and tryptophan are presented in this paper.
1078
AMINO
ACIDS
IN
MEAT
TABLE
Composition
of Media
_
.--__
4
4
2
2
2
2
1
1
gm.
mg.
ml.
I
(12))
acid
acid
100
100
200
100
100
100
25
2
2
(
I
(
Glutamic acid
Asparagine
Lysine
Cystine
Leucine
Threonine
Valine
Isoleucine
Alanine
Methionine
Arginine
Histidine
Tryptophan
Tyrosine
Serine
Phenylalanine
Proline
Glycine
TE,: P.er
m.
80
80
40
40
20
20
20
20
20
20
20
20
20
20
10
10
10
20
* The amounts as given for 100 ml. of double strength medium are those added per
100 tubes, with a final volume of 2 ml. of sample, water, and medium per tube. For
8. faecalis R assays the sodium acetate and Salts A are replaced by 5 gm. of sodium
citrate
and 1 gm. of KzHPOA per 100 ml. Salts A is composed of 100 mg. of KHzPOI
and 100 mg. of KzHPOa per ml.
t The amounts indicated are for the L isomer; where the DL isomer is used, twice
the amounts indicated are added. For the methionine assays the amino acids were
replaced by 1500 mg. of H,Oz-treated peptone (13), cystine, tryptophan, and tyrosine
at the amounts
indicated per 100 ml.
It is recognized that, if any racemization of the amino acids occurred
during hydrolysis, the analytical values would be low, since the D isomers
of these amino acids are inactive or essentially inactive for the test microorganisms.
The methods of analysis used were essentially those described in earlier
work (8-10) ; however, the composition of the media has been changed
somewhat from that used in the earlier work. Details are given in Table I.
All assayswere carried out with a final volume of 2.0 ml. and the acid production after incubating for 72 hours was determined titrimetrically.
Glucose
Sodium acetate
Adenine
Guanine
Uracil
Xanthine
Salts A
C (Henderson-Snell
Thiamine
Riboflavin
Nicotinic acid
Ca pantothenate
Pyridoxine
Pyridoxal
p-Aminobeneoic
Biotin
Pteroylglutamic
Constituents
Constituent*
SCHWEIGERT,
GUTHNECK,
KRAYBILL,
AND
Tryptophan
was determined by the Bates method
scribed by Graham and associates (11).
RESULTS
AND
1079
GREENWOOD
essentially
as de-
DISCUSSION
The assay results obtained with the present media were very satisfactory.
Tests to confirm the validity of the results obtained for histidine and
phenylalanine revealed that excellent agreement in the assay values was
obtained with the use of two different test organisms when applied to both
pork and lamb samples (Table II).
of H&i&e
Histidine
Sample;
Lamb,
I
I
Pork,
I
rib chop
shoulder
leg
breast
steak
loin
spareribs
Phenylalanine
description
L. arabinoSUJ
2.24
2.06
2.04
2.24
2.59
2.86
2.46
2.32
2.13
2.13
2.10
2.37
2.92
2.46
3.37
2.91
3.26
3.17
3.35
3.32
3.62
L. mse;1cr-
3.31
2.95
3.01
3.23
3.26
3.48
3.66
Other studies were conducted to compare the methionine values obtained by the microbiological
method with those obtained by a chemical
method (14) and also to compare different media with L. mesenteroides
and S. faecalis R. The results obtained with the microbiological
method
were in good agreement with those obtained by the chemical method for
samples varying over a wide range of potency (Table III).
The addition of yeast extract (Difco) to the medium did not influence the assay
values for methionine (Table III) for samples that were relatively low in
accessory factors (casein and soy bean meal) or for samples that were
rich in growth stimulants (lung and liver meal and pork muscle). Other
tests with the purified amino acid medium described in Table I either
with or without the addition of yeast extract did not reveal any consistent deviations from the methionine values indicated with either S. faecalis
R or L. mesenteroidesas the test organism.
The amounts of leucine, valine, isoleucine, threonine, phenylalanine,
arginine, histidine, lysine, methionine, and tryptophan in the crude protein of pork and lamb samples are presented in Tables IV and V. The
percentage of protein in the fresh and cooked samples is also presented
TABLE
II
and Phenylalanine
Values Obtained with Use of Different
Test Organisms
The values are given in the per cent of the partially dried and defatted samples.
Comparison
TAISLR III
Comparison of Chemicaland Microbiological
Determination
of Methionine*
The values are given in per cent methionine in the crude protein.
Microbiological
Sample; description
Medium A
Fish-meal
Gelatin
Soy bean meal, No. 1
I 2
Casein, No. 1
I 2
Pork muscle
Lung and liver meal
methodt
Medium B
2.85
0.80
1.15
1.06
2.65
2.77
2.55
1.64
2.90
0.90
1.14
2.66
1.12
2.84
2.43
1.65
TABLE
IV
Amino Acid Content of Fresh and Cooked Pork*
PKJtein
Sample; description
H
*
g
ii
p
B
2
S
g
G
Ei
3
22
d
B
k
Fresh samples
Rib chop
Loin
Steak
Loin
Spareribs
Shoulder
16.3127.854.57.284.904.805.063.716.123.157.852.431.33
16.5326.955.77.764.984.785.213.705.713.568.062.491.40
12.6240.147.67.164.814.824.803.865.852.727.982.581.33
16.3626.156.87.264.824.645.134.006.123.537.762.571.22
14.2038.647.77.585.005.025.374.476.322.888.022.671.34
14.8432.951.97.114.944.715.084.165.873.517.402.421.39
-~--~-7.364.914.805.113.98,6.003.237.852.53,1.33
Average............
Cooked samples
Rib chop
Loin
Steak
Loin roast
Spareribs
Shoulder
Average.
. .
* The values for protein, ether extract, and moisture are expressed as the percentage in the moist meat and the values for the amino acids are expressed as the percentage in the crude protein (N X 6.25).
1080
SCHWEIGERT,
GUTHNECK,
KRAYBILL,
AND
GREENWOOD
1081
and the amount of each amino acid in these samples can be calculated by
multiplying
the percentage of the amino acid in the protein by the protein percentage and dividing by 100. The amount of the amino acids
in the different cuts of pork and lamb is quite uniform, with the exception
of histidine.
Although the histidine values for lamb are in good agreeThe amount
ment for different cuts, they are lower than those for pork.
Amino
Sample;
Acid
Content
of Fresh
Lamb*
Rib chop
Loin
I
Shoulder
.-
Average............
samples
14.4538.346.56.825.024.244.353.836.522.437.042.211.22
14.4733.851.06.975.164.824.783.836.952.597.882.481.30
18.3311.869.37.675.124.644.983.786.972.537.972.611.45
15.2332.253.47.154.744.604.793.726.812.557.672.W1.31
12.8337.048.36.774.864.424.723.806.302.497.332.311.26
18.5815.864.76.984.904.685.023.986.872.798.002.451.29
_
~-~
-_
------7.064.974.574.773.826.742.567.652.431.30
Cooked
Rib chop
Loin
Shoulder
Fresh
samples
17.2041.0~41.27.625.M4.905.054.076.972.767.522.201.32
19.0635.744.07.764.754.824.923.987.202.877.682.151.25
22.5418.4.58.57.714.925.065.043.887.232.767.442.251.35
19.8439.240.07.634.904.944.784.207.182.677.872.361.27
20.2242.3~37.48.175.295.205.004.246.982.817.722.131.~
23.8525.948.97.775.204.965.083.966.342.947.682.181.35
-------__---_
Leg
Breast
Loin roast
Average.
Cooked
Protein
description
Leg
Breast
Loin
and
...
... ..
/I
7.785.024.984.984.066.982.807.652.211.33
* The values
for protein,
ether
extract,
centage
in the moist meat and the values
percentage
in the crude protein
(N X 6.25).
and
moisture
are expressed
as the per-
1082
AMINO
ACIDS
IN
MEAT
SUMMARY
1.
2.
3.
4.
5.
6.
7.
8.
9.
10.
11.
The data confirm previous findings that the amino acids so far studied
are essentially stable to cooking.
This is evidenced from the fact that
no appreciable changes were noted in the percentage of the amino acids
in the protein of the fresh and cooked samples (Tables IV and V).
The
retention of the amino acids in the cooked cuts was also determined by
comparing the total amount of each amino acid in the uncooked cuts
with the total amount in the cuts after cooking.
The percentage retentions obtained showed that no appreciable loss of the amino acids occurred during cooking.
For example, the percentage of valine retained
averaged 101 per cent (range 97 to 106 per cent), the lysine retained averaged 99 per cent (range 89 to 108 per cent), and the tryptophan
retained
averaged 104 per cent (range 96 to 115 per cent).
These studies are now
being extended to include other amino acids and studies on the availability of amino acids in uncooked and cooked meats.
SCHWEIGERT,
GUTHNECK,
KRAYBILL,
AND
GREENWOOD
1083
12. Henderson, L. M., and Snell, E. E., J. Biol. Chem., 172,15 (1943).
13. Lyman, C. M., Moseley, O., Wood, S., and Hale, F., Arch. Biochem., 10, 427
(1946).
14. Csonka, F. A., and Denton, C. A., J. Biol. Chem., 163,329 (1946).
15. Schweigert, B. S., Tatman, I. E., and Elvehjem, C. A., Arch. Biochem., 6, 177
(1945).
16. Hier, S. W., Graham, C. E., Freides, R., and Klein, D., J. Biol. Chem., 161, 705
(1945).
17. Greenhut, I. T., Schweigert, B. S., and Elvehjem, C. A., J. Biol. Chem., 166,
325 (1946).
18. Lyman, C. M., Butler, B., Moseley, O., Wood, S., and Hale, F., J. Biol. Chem.,
166, 173 (1946).
19. Greenhut, I. T., Potter, R. L., and Elvehjem, C. A., Arch. Biochem., 16,459 (1947).
20. Kuiken, K. A., Lyman, C. M., and Hale, F., J. Biol. Chem., 171, 561 (1947).
21. Lyman, C. M., and Kuiken, K. A., Texas Agr. Exp. Sta. Bull. 708 (1949).
22. Kraybill, H. R., in Sahyun, M., Proteins and amino acids in nutrition, New York
(1948).
ARTICLE:
THE AMINO ACID COMPOSITION OF
PORK AND LAMB CUTS