6
Animal Glue
ROBERT L. BRANDIS
St. Johnsville, New York
Animal glue has been used as an aqueous ad-
hesive and size for thousands of years, and in
more recent times has also found acceptance as
a protective colloid, flocculant, and adhesive
composition.
Commercial manufacture dates back to 1690
in Holland, 1700 in England, and the early 19th
Century in the United States.) By 1900 there
were at least 60 producers of animal glue in the
United States; now there are only two.
Glue is derived from collagen, the major pro-
teinaceous component of animal and fish skins,
as well as tendons and the proteinaceous matrix
of bones. In recent times the important com-
mercial raw materials for making animal glue
come from tanneries, which supply limed splits
and chrome tanned pieces, and from slaughter
houses, which furnish fleshings, hide pieces
and bones.
The terms gelatin, technical gelatin, and an-
imal glue refer to similar materials obtained
from approximately the same stock but through
different treatments. Edible gelatin and photo-
graphic gelatin are produced under more strin-
gent conditions, producing a product of
excellent color and clarity, low ash and low
grease, combined with a very low bacteria
count. These gelatins, because of manufactur-
ing costs, sell for considerably more than tech-
nical gelatin and animal glues. Edible and
photographic gelatins have tended to keep mar-
ket share and have been the subject of contin-
uing research.
I. Skeist (ed.), Handbook of Adhesives
© Van Nostrand Reinhold, New York, NY 1990
Technical gelatin and animal glue, on the
other hand, have seen their market share con-
siderably eroded in the last 25 years. This de-
cline has been brought about by the advent of
synthetic polymers, which have taken over the
sizing of synthetic fibers and the binding of pa-
perback books. (But telephone books and cat-
alogs have stayed with animal glue because of
its superior durability and flexibility as well as
lower cost.)
Because of the recent demise of a number of
glue factories in the western world, there is
currently a worldwide shortage of glue, partic-
ularly in the higher test grades. At this time
there are only two manufacturers in the United
States: Milligan & Higgins Division, Hudson
Industries Corp., of Johnstown, New York,_
who make hide glue; and Swift Adhesives (Div.
of Reichhold Chemicals), St. Joseph, Mis-
souri, who make bone glue. Cattle are the ma-
jor source, with rabbits and sheep contributing
to a much lesser degree. A substantial amount
of hide and bone glue is imported from Brazil,
Chile, China, and other countries, and finds its
way primarily into compounded adhesives and
protective colloids. Leading importers of ani-
mal glue are Hudson Industries Corp., Olym-
pic Adhesives, Inc., Nicholson & Co.,
Transatlantic By-Products Corp., and Swift
Adhesives (Div. of Reichhold Chemicals).
It is estimated that domestic consumption of
technical gelatin and animal glue is 25-30 mil-
lion pounds per year. 2
123
124 HANDBOOK OF ADHESIVES

CHEMISTRY hydrolysis, yielding tightly coiled lateral ag-

Animal glue is essentially the hydrolytic prod-
uct of collagen, the main protein in animal skins
and bones. Collagen as its exists in its natural
state is water-insoluble and resistant to mild
acids and alkalies as well as proteolytic en-
zymes other than the collagenases. Veis and
Cohen discuss the structure of collagen:
A collagen fibril may thus be pictured as ...
segments varying in length and cross-section
area due to differences in the cross-link distri-
bution and the lateral ordering of the polypep-
tide chains ... The segments are chain
networks held together by sets of the acid-sta-
ble or B bonds. These segments contain and are
held in the gross structure by the acid-labile A
bonds and physical forces. 3
The conversion of collagen to soluble poly-
peptides involves the breaking of covalent
bonds and the disruption of physical forces
through the use of either acid and heat or alkali
and heat. Acid and heat cause selective disrup-
tion of some bonds plus selective peptide bond
gregates of peptide chains. Alkali and heat
bring about a much more complete cross-link-
age breakdown, resulting in randomly coiled
peptide chains.
Veis 3 .4 describes the collagen-gelatin transi-
tion as a stepwise process involving the melting
of a trihelical network to an amorphous form,
followed by the sequential hydrolysis of var-
ious types of covalent bonds.
Collagen from different species and even dif-
ferent parts of the same species varies in sta-
bility to acids, alkalies and heat because of
differences in intramolecular and intermolecu-
lar organization. Glue molecules may be con-
sidered to be polypeptide chains containing
amino acid sequences of varying lengths de-
pending upon the treatment. 5 The amino acid
analysis done by Eastoe, and corroborated by
others, on an ox hide gelatin indicated that there
are 18 separate amino acids present in varying
amounts. 6
Table 1 agrees within tolerable limits with
that of Eastoe but also characterizes the ionic
nature of the R-radicals on each amino acid.

Table 1. Amino Acids in Animal Glue. 5

Residues Per
Character of R-Radical
J()OO Total of
Amino Acid All Residues Distinctive Groups Ionic Character
Glycine 335.0 Neutral
Proline 128.0 Pyrrolidine in the chain Neutral
Alanine 113.0 Neutral
Hydroxyproline 94.5 Hydroxypyrrolidine in the chain Neutral
Glutamic acid 72.0 Carboxyl Acid
Arginine 47.0 Guanido Basic
Aspartic acid 46.5 Carboxyl Acid
Serine 35.0 Hydroxyl Neutral
Lysine 27.0 Amine Basic
Leucine 23.0 Neutral
Valine 20.0 Neutral
Threonine 18.0 Hydroxyl Neutral
Phenylalanine 13.0 Phenyl Neutral
Isoleucine 12.0 Neutral
Methionine 5.0 Thiomethyl Neutral
Hydroxylysine 5.0 Amine, Hydroxyl Basic
Histidine 4.5 Imidazole Basic
Tyrosine 4.4 p-Phenylene, Hydroxyl Very weakly
acid

Additional amino acids:?

Glutamine 20 Primary Amide Neutral
Asparagine 20 Primary Amide Neutral