Gelatin is obtained by the hydrolysis of collagen which is the principal protein found in skin and
bones. Fish gelatin is being extracted commercially in Nova Scotia by Kenney & Ross at Port Saxon.
The raw material is the skin from deep water fish such as cod, haddock and pollock, and is obtained
from local salt fish and frozen fish processors. The uniqueness of fish gelatin lies in the amino acid
content of the gelatin. Although all gelatins are composed of the same 20 amino acids, there can be
a variation in the amount of imino acids, proline and hydroxyproline. With lower amounts of these
amino acids, there is less hydrogen bonding of gelatin in water solutions, and hence a reduction in
the gelling temperature. Gelatin from cod skin gels at 10ºC, whereas gelatin from carp skin would be
more similar to animal gelatin, which gels above room temperature. Most people think of gelatin as a
food additive or part of photographic film. With a lower gelling temperature, other commercial
applications of fish gelatin have been developed. These applications are discussed.
The amount of information reported in the literature on fish gelatin is somewhat limited (Mees, 1966;
Gustavson, 1956; Piez, 1965). Kenney & Ross has been producing fish gelatin since 1960, and this
conference gives us the opportunity to share with you some of the information that we have
developed. The product initially manufactured by us was marketed as a clarified fish glue, and
essentially was a fish gelatin used in industrial application. We have been marketing an edible type
of fish gelatin since 1981.
All gelatin is derived from collagen, the principal protein found in skin and bone. A simplified
characterization of the applications of gelatin would be into the following four uses:
Fish gelatin, with the exception of photographic film, is used in all these applications. However, fish
gelatin is used as the base for a light sensitive coating (or photoresist) for the electronics trade.
The precursor for gelatin is collagen. Collagen is the major structural protein found in the skin and
bones of all animals. The collagen molecule consists of 3 individual polypeptide chains (alpha
chains) which are wound around one another in a triple helix confirmation. This triple helix is
stabilized by hydrogen bonds between collagen molecules, which happens as the animal ages. A
collagen molecule of three alpha chains would measure 3000Aº in length (0.3 microns) and 15Aº in
diameter. Each alpha chain has approximately 1050 amino acids connected together. There are
twenty different amino acids in each alpha chain, and for each animal type of gelatin, these amino
acids are in a specific repeated pattern. Glycine, which represents a third of the amino acids content,
is in repeated sequence with two other amino acids. This might be represented as glycine-x-y. It is
not unusual for x to be proline and y to be a hydroxyproline residue.
Table 1 compares the content of amino acids in fish gelatin with that of calf skin gelatin. We sell our
gelatin as HiPure Liquid and Dry Gelatin. The amino acids are listed alphabetically together with
their functionality. A common way of stating the content of amino acids is by indicating the number
of residues per thousand amino acids. Note the comparison between fish gelatin and calf skin
gelatin for the amino acids proline and hydroxyproline.
The role of proline and hydroxyproline in collagen is very critical. There appears to be a relationship
between the temperature at which the animal (or fish) metabolizes and the properties of the skin and
resultant extracted gelatin. Gelatin derived from the skin of deep cold water fish has lower amounts
of proline and hydroxyproline, and as a result, water solutions will not gel at room temperature, but
will remain liquid to 8 to 10ºC.
Collagen in skin can be dissolved in dilute cold acid or salt solution, but with great difficulty and
generally poor yields. This is because collagen molecules are covalently cross-linked into fibrils that
may swell, but do not dissolve. If the skin and cold acid are heated, at a certain temperature the
collagen molecule undergoes a helix coil transition. The helix coil literally unfolds, and the collagen
becomes more readily soluble. The temperature at which this occurs depends upon the amount of
proline and hydroxyproline in the alpha chain, and this temperature is the point of denaturing. For
deep cold water fish collagen, this temperature is approximately 15ºC. Bovine collagen is
approximately 40ºC. Another term, which covers the same effect in the skin itself, is the shrinkage t
temperature. This is exactly what the term implies. At a certain temperature, the collagen in the raw
skin will relax and the skin will shrink. The shrinkage temperature of the raw skin is higher than the
denaturing temperature of the skin in acidified water, but the same relationship of proline and
hydroxyproline to the shrinkage temperature still holds.
Table 2 shows a comparison of the amino acid composition of some fish collagens that have been
published by Piez and Gross (1960). Glycine represents a third of the total amino acids residues.
There are similarities in the composition, but what is important, is the total amount of proline and
hydroxyproline, as well as the highest shrinkage temperature.
*Piez and Gross (1960)
Commercial extraction of gelatin depends upon both dissolving and hydrolyzing the denatured skin.
The gelatin may retain some covalent bonds between alpha chains, which would entail multiples of
the single alpha chain length of 95,000 daltons. There are also major proportions of shorter chain
polypeptide in the gelatin, as the chain is cleaved in the extraction process. This is not necessarily a
problem, as the end product may not need very high molecular fractions in order to accomplish the
The molecular weight of four gelatins were compared using gel permeation chromatography and
low angle light scattering (Berg and Frederick, private communication) in Fig. 1. The top curve is a
standard gelatin, and underneath it is calf skin gelatin. The second curve is fish gelatin extracted
with minimal hydrolysis. The lowest curve is commercial fish gelatin, which was hydrolyzed more to
achieve certain viscosity characteristics. The animal gelatins and the low hydrolysis fish gelatin all
have peaks at 190,000 and 95,000, characteristic of beta and alpha collagens respectively. About
10% of the wet weight of fish skin is Type I collagen. Fig. 2 is a comparison of molecular
composition of calf skin collagen with fish skin collagen, done by using polyacrylamide gel
electrophoresis (PAGE) according to the method of Laemml (1970), whereby molecules of different
molecular weights are separated using an electrical current. There are similarities between the two
collagens. The fish collagen consisted primarily of alpha 1 and alpha 2 chains in a 2:1 ratio. Beta
collagen would be two alpha collagens covalently linked together.
Fig. 3 plots the viscosity of a 10% solution of animal gelatin vs fish gelatin with minimal hydrolysis
and commercial fish gelatin. There are similarities between the gelatins, but note that the animal
gelatin gels at 32ºC, whereas the fish gelatin remains liquid down to 8ºC.
Norland HiPure Liquid Gelatin is supplied at 45% solids in water and is pourable solution at 7000
to 8000cps, about the viscosity of honey. The gelatin is protected by a mixture of methyl and propyl
Fish gelatin has similar chemical reactivity to animal gelatin. Aldehydes such as formaldehyde,
gluteraldehyde and glyoxal will cross-link and harden the gelatin under appropriate conditions. It
can be reacted with anydrides under alkaline conditions, reducing or eliminating the effect of
aldehydes as a hardening agent on the gelatin. Fish gelatin also provides a good medium for
precipitating silver halide emulsions, as this can be done at lower temperatures than with animal
Our factory is located on the southwestern tip of Nova Scotia, Canada, in an area rich in fishing
grounds. Skins are obtained from frozen fish producers, as well as salt fish processors. Large
quantities of skin are used in the plant, and 16,000 pounds of skins are handled daily.
I mentioned fish gelatin being used in a light sensitive coating. Our clarified fish glue was originally
used as a base for a water soluble photoresist (Holahan, 1965). If you have a color television set
there is a good possibility that the critical part of the television tube, the aperture mask, was made
using a photolithographic process with fish gelatin as the photoresist base. There are 400,000
holes or slots in the mask and the purpose of these holes is to delineate the color picture that is
projected onto the phosphors on the inside of the television tube. The optics are so critical, that
imperfections of a fraction of a micron can be visually seen on the screen, and would be a cause for
rejection. These masks are made in a continuous process whereby thin metal is unwound from a role
from one end of the equipment, and completed masks are stripped from the sheet at the other end
1,000 feet away.
Fish gelatin is also used in the manufacture of lead frames that hold the silicon chip in computers
and microprocessors (American Machinist, 1971). The chip is mounted on a pad at the center
portion of the lead frame, and each circuit on the chip is connected to a lead that surrounds it. The l
lead frame are made using a photochemical machining process and a fish gelatin photoresist.
A necessary part of the optics of a color video camera is a color stripped filter that separates the
color signals for the electronics of the camera. Each filter has a series of 3 different color stripes, 12
microns wide, put down on glass in a repeat pattern. The total size of the filter is approximately 1/2"
x 3/4". The stripes are put on the glass using a photolithographic process in the fish gelatin.
1) Gelatin is made from collagen, which is part of the skin and bones of animals and fish.
2) All gelatins have same 20 different amino acids, in slightly different proportions for different
3) The amount of the imino amino acids, proline and hydroxyproline, determines the shrinkage
temperature and the denaturing temperature, (The temperature at which the collagen helix
unwinds), and as a result, the temperature at which solutions of the extracted gelatins gels.
4) Gelatin from cold deep water fish such as cod, haddock, pollock, hake and cusk, gels at 8 to 10ºC
compared to calf skin gelatin which gels at 30 to 35ºC.
5) Fish gelatin is used in a variety of coating applications, the largest of which is a base for a water
Berg, R. and Frederick. Private communication. Biomaterials Centre, Dept. of Pathology, Rutgers
Medical School, Piscataway, NJ.
Burjanadze, T.V. 1982. Stabilization of collage structure; Dependence of collagen denaturation
enthalpy on the imino acid content. Biopolymers 21(8): 1587.
Chemically Milling Precision Parts. 1971. American Machinist 115: 50.
Gustavson, K.H. 1956. "The Chemistry and Reactivity of Collagen." Academic Press, New York, NY.
Holahan, J.F. 1965. Manufacture of color picture tubes. Electronics World 74(6):30-32,56.
Laemmll, U.K. 1970. Cleavage of structural proteins during the assembly of the head of
bacteriophage T4. Nature 227(5259): 680.
Mees, C.E.K. and James, T.H. 1966. "The Theory of the Photographic Process." 3rd ed. Macmillan
Company, New York.
Piez, K. 1965. Characterization of a collagen from cod skin containing three chromatographically
different chains. Biochemistry 4(12): 2590.
Piez, K.A. and Gross, J. 1960. The amino acid composition of some fish collagens: The relations
between composition and structure. J. Biol. Chem. 235(4): 995.
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