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Protein in dog foods

R. Glenn Brown

Introduction - Functions of protein

ietary protein from whatever
source has several functions.
r .n Foremost is the provision of amino
y | acids from which the animal may
make the proteins that comprise its
tissues (1). A secondary function of
dietary protein in pet diets is as a
source of flavors. When heated in
the presence of either carbohydrates Met1 nn+yin
:: 0.39 111:
or fats, proteins develop what are called "reaction Phenylalanin.e-:.:....
flavors" (2) which readers will associate with the + tyrn 0.72 20. 7...
flavors of cooked meats, cooked fish or heated oilseed
proteins. For this reason, palatability is increased with Th Inn ~~~~~~~~~...
.....^ no.
0.47 0 13...1. ....

both increased levels of protein as well as time and Tryp.

: .:: :.......... 2' j2 . . :i:'
. ........... . . . ...... ....... .. ...1...9......
....tophan. . ... ....

conditions of heating (2). In dry dog foods, the protein :~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~.

portion of the product may contribute to the overal
structural integrity of the particles. In canned
products, the source of protein contributes to the tex-
ture of the product giving it the moisture-binding
characteristics which impart a "juicy" appearance.
The appearance and texture of chunks can be influenced
by the choice of protein source. Texturized vegetable
proteins (soy) chinks are frequently better able to
withstand the rigors of retorting and maintain their
shape and appearance. Chunks of striated voluntary
muscle may lose much of their integrity on processing
at the temperatures and times used in retorting for food
safety. In recent years, for a variety of reasons, there
has been concern about the sources of protein in canine
diets. The use of soy products in dog diets has been
questioned because of soy's nutritional properties and
because of its alleged role in gastric torsion and bloat.
The purpose of the following is to review some aspects
of protein nutrition in canine diets with reference to
quality of protein.
(For copies of this article contact: The CVMA Pet Food
Certification Program Dep't CVMA, 339 Booth, Ottawa,
Ont KIR 7K1.)
La version francaise paraitra dans la Revue du mois de juillet.
Nutrition Consultant
CVMA Pet Food Certification Program
339 Booth Street
Ottawa, Ontario
KIR 7K1
528
amino.acids 6.26 ...... 1786
*Calculated on thbs'is of the:de: eig2% rti ad
te potin n he ie wa 16%
tha
Proen~esinqaityassm n nitrogen.t
Protein quality assessment
Protein quality refers to the efficiency with which the
amino acids from the diet are converted into tissues.
That efficiency in turn is dependent on the concentra-
tion of essential amino acids in the diet. Table 1
presents a list of the essential amino acids for dogs as
well as the requirements for them. The term "essen-
tial" means that the animal cannot make the amino
acid in question by normal transamination reactions.
The synthesis of tissue from dietary amino acids is
under genetic control and the amino acids in tissue pro-
teins are used in precise amounts and sequence. When
a particular essential amino acid is not available, pro-
tein synthesis stops. Other essential amino acids cannot
be used or substituted for the missing one. That missing
essential amino acid is called the "limiting amino acid"
because its absence limits the utilization of other essen-
tial amino acids. When the limiting amino acid is sup-
plied, utilization of the other essential amino acids may
continue. In a dietary sense, the essential amino acid
present in a food in lowest concentration relative to
the animal's needs is called the first limiting amino
acid. That present in the second lowest concentration
is referred to as the "second limiting amino acid" and
so forth. The quality of dietary protein depends almost
entirely on its ability to furnish sufficient amounts of
528~~~~~ Ve_
Can Vet J Volume 30, June 1989 Ca ~ oue30 ue18
essential amino acids. The best quality proteins have
no limiting amino acids, whereas those of lesser quality
may have one or more limiting amino acids.
The quality of a dietary protein is influenced by its
digestibility, which may be adversely effected by pro-
cessing or excess of single amino acids that interfere
with the utilization of others (3). Since protein quality
is tied to the amino acid requirements of a particular
species or breed of animal, it follows that the quality
of protein is different for different species. Caution
should be exercised when extrapolating measures of
protein quality determined for humans to dogs or cats.
For example, humans do not have a requirement for
taurine, whilst cats do, and protein sources that are
devoid of taurine may be quite good for humans but
unacceptable for cats. Likewise, the fact that histidine
and arginine are essential for dogs but not mature
humans argues that protein sources which are limiting
in these amino acids would be acceptable for humans
but not dogs.
There are a number of measures of protein quality.
The first and crudest is the protein efficiency ratio
(PER) which measures the ability of dietary protein
to be converted into tissue. The method works only
with young, growing animals and may be influenced
by the level of energy or fat in the diet as well as by
the level of dietary protein. The PER is calculated as:
Weight gain of animal
PER =
Protein intake of animal
The PER for animal proteins is typically 2.5.
The most frequently quoted measure of protein
quality is biological value (BV) which is defined as the
percent of absorbed protein retained. This measure
gauges the efficiency with which the body is able to
convert dietary amino acids that had been absorbed
into tissues. It is calculated as:
Food N - (Fecal N + Urinary N)
BV =
Food N - Fecal N
Can Vet J Volume 30, June 1989
There are some practical problems using BV as a
measure of quality. It is possible to have a protein
source which is not very digestible, have a very high
BV if the residue that is absorbed is very well utilized.
To overcome this difficulty, a measure was devised
which would compensate for differences in digestibility.
This is called net protein utilization (NPU) which is
the BV multiplied by the coefficient of digestibility.
This adjusts for differences in true availability of the
dietary amino acids to the animal.
The amino acid score (AAS) is a chemical method
to assess quality which compares the amount of the first
limiting amino acid (AA) in a test protein with the level
of the same amino acid found in a reference protein (4).
It is calculated as:
mg of AA/g of test protein
AAS =
mg of AA/g of reference protein
The AAS has the advantage of being rapid and
generally reproducible. The disadvantage is that it does
not compensate for differences in digestibility that can
be caused by processing.
The biological equivalent of the AAS is something
called the slope ratio method, which compares the
growth performance produced by a test protein with
that of a reference protein such as defatted whole
egg (5). It is calculated as:
Slope of response curve for
animals fed test protein
Slope Ratio =
Slope of response curve for
animals fed reference protein
The slope ratio method usually uses growth as the
response and may be sensitive to differing levels of
energy.
It should be apparent from this brief review of the
principal methods used to measure protein quality that
all methods have shortcomings. It is important to note
that while protein quality varies with the animal species
529
in question, proteins that are of poor quality in one
monogastric species may be of poor quality in other
monogastrics. The sensitivity to quality, however, is
conditioned on the rate of growth or the level of
demand made to synthesize proteins such as lactation,
trauma, athletic performance, stress, etc. Animals that
are relatively inactive, mature and under no particular
stress may not be very sensitive to moderate differences
in protein quality.
Sources of protein
There are relatively few sources of protein for pet
foods when compared to the 2000 + foods that are
common in the human diet (6). The principal reasons
for this are cost and availability. The two major
sources are animal byproducts and oilseeds. Cereal
sources are only marginal sources of pet food proteins.
The major sources are listed in Table 2.
Improvement of protein quality
The nutritional quality of a dietary protein to the
animal does not depend on the amino acid profile of
any single protein source but upon the sum of the
amino acid patterns of all proteins in the diet at any
one time. A variation in any one ingredient can cause
a shift in the amino acid profile of the finished diet.
To avoid this shift, a variety of sources are used when
making pet food. Since the biological quality of any
mixture of dietary proteins is controlled by the
concentration of limiting amino acids it is possible to
improve the overall quality of the mixture by careful
mixing of protein sources. This process is called com-
plementation. An example of this is blending cereals
that are low in lysine and/or tryptophan with small
amounts of animal proteins which are rich in those
amino acids. This is what happens when you put milk
on breakfast cereals. It does not take a large amount
530
of good quality protein to vastly improve the biological
quality of larger amounts of plant proteins.
A word of caution should be given about comple-
mentation. While the differences in essential amino
acid levels can be "ironed out" by the process, dif-
ferences in digestibility of the different sources are not
eliminated in blending. The digestibility of most cereal
and soy products is in the range of 71-80'7o, whereas
meats are digested at levels of 80-90% (7,8).
Comparison of amino acid profiles of
protein sources
The amino acid profiles of a selection of protein
sources used in dog foods are shown in Table 3.
Inspection of the data will indicate that within broad
classes of sources, the amino acid profiles do not vary
widely (9). It should be noted that soy products tend
to be limiting in the sulfur-containing amino acids but
are fairly rich in arginine. Most of the animal sources
are also rich in lysine and tryptophan, which are
limiting in commonly used cereals such as corn and
wheat. In dogs, unlike many monogastrics, histidine
is an essential amino acid at all stages of life, and pork
products are particularly rich in histidine, whereas
most cereals, chicken and soy products contain lesser
amounts. When compared with meat sources, soy
products have some limitations particularly with regard
to the level of sulfur-containing amino acids. It is
important to note that soy is rarely used as the sole
protein source in many dog foods, but is blended with
meat products either as fish or poultry meal or as fresh
processed meats. The latter source is of more recent
use and tends to eliminate some of the variations in
the quality of meat meals caused by poorly controlled
heating. When proteins of animal origin are combined
with those of plant sources, complementation of
limiting essential amino acids is achieved and the
Can Vet J Volume 30, June 1989
overall quality of protein in the product is raised. This
is most easily done by using small amounts of animal
products.
There has been a move amongst makers of dog
foods which are in the CVMA Pet Food Certification
Program to decrease or eliminate soy from their prod-
ucts. The nutritional quality of previous products
which contained soy was not the reason for this.
However, cost and availability of soy versus meat and
fish products in the Canadian market, the production
of flatulence and bloating in certain animals when soy
products are fed, and improved acceptance by dogs
of meat-containing foods, are all factors in moving
away from imported soy in pet foods.
Summary
The principal protein source in most commercial dog
foods is frequently a combination of animal and
oilseed proteins. In general the quality of dietary protein
is controlled by the concentrations of essential amino
acids and the digestibility of the protein. Animal
sources (except for gelatin) are usually of excellent
quality, while oilseeds such as soy are limited in the
concentrations of sulfur-containing amino acids pres-
ent, and cereals are limited in both lysine and
tryptophan. Combining sources of proteins will
compensate for such limitations and this process is
called complementation. As long as the principles of
complementation are observed and the digestibility of
the overall protein source is maintained, the source of
amino acids in the diet is less important than the con-
centration. The use of soy in dog foods in the CVMA
Can Vet J Volume 30, June 1989
Pet Food Certification Program has declined in recent
years because of economic reasons, acceptance,
supply, and other factors such as soy-related flatulence
and bloat.
References
1. McDonald P, Edwards RA, Greenhalgh JFD. Animal Nutrition,
2ed. London: Longman, 1976: 42-58.
2. Zapsalis C, Beck RA. Food Chemistry and Nutritional
Biochemistry. Toronto: J. Wiley and Sons, 1985: 581-616.
3. Hul, YH. Human Nutrition and Diet Therapy. Monterey, Calif.:
Wadsworth, 1983: 212-213.
4. FAO/WHO. Energy requirements and protein requirements.
WHO Tech Ref Ser No 522. Geneva: WHO, 1973: 63.
5. Samonds KW, Hegsted DM. Animal bioassays: Critical evalua-
tion with specific reference to assessing nutritive values for
humans, In: Evaluation of Proteins, Westport: AVI, 1977:
68-80.
6. Massachusetts Nutrient Data Bank. Department of Nutrition,
University of Massachusetts, Amherst.
7. Kendall PT, Holme DW. Studies on the digestibility of soyabean
products, cereals and plant byproducts in diets of dogs. J Sci
Food Agric 1982; 33: 813-822.
8. Meyer H. Nutrient digestibility and its relationship to alimentary
disorders in dogs. In: Nutrition and Behaviour in Dogs and Cats,
ed Anderson, RS. Toronto: Pregamon 1984: 55-69.
9. Rubin M, Hynson MT, Bossard EH. Variability of amino acids
and protein composition in common feed ingredients. Maryland
Nutrition Conference. University of Maryland, College Park:
March 17, 1977.
10. National Research Council. Nutrient Requirements of Dogs,
National Academy of Sciences. Washington: National Academy
Press. 1985.
11. National Research Council, United States - Canadian Tables
of Feed Composition, 3rd revision. National Academy of
Sciences. Washington: National Academy Press, 1982: 112-130.
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