Collagen is a structural animal protein, primarily extracted from from animal connective tissue — bovine hides and bones, pig skin, and fish skins and scales — much of it recovered as a byproduct of the meat and seafood industries. Collagen reaches confectionery formulators primarily as hydrolyzed collagen peptides used for protein fortification in gummies, chews, and functional candy formats. It is closely related to gelatin (which is partially hydrolyzed collagen) but behaves very differently: while gelatin gels a candy, hydrolyzed collagen does not gel at all, and this distinction drives the vast majority of formulation decisions around the ingredient.

What types of collagen are used in confectionery?

Collagen reaches confectionery formulators in several forms, distinguished by animal source, degree of hydrolysis, and collagen type:

- Hydrolyzed collagen peptides (bovine): derived from bovine hides or bones. Type I collagen dominant, with some Type III. The most widely used form in confectionery for protein-boost positioning [1].

- Hydrolyzed collagen peptides (marine/fish): derived from fish skins and scales, most often as byproducts of the seafood industry. Type I collagen. Lower thermal stability than mammalian collagen but suited to pescatarian, halal, and kosher-friendly product positioning [4,5].

- Hydrolyzed collagen peptides (porcine): derived from pig skin. Type I dominant. Widely used industrially but restricted in halal, kosher, and some regional markets.

- Chicken cartilage collagen (Type II): derived from poultry cartilage. Less common in mainstream confectionery, more common in joint-health supplement products [1].

- Native collagen: intact triple helix, largely insoluble in water. Rarely used in food; mostly directed to cosmetics and biomedical applications [3,7].

- Gelatin: technically a partially hydrolyzed collagen, but treated as a distinct confectionery ingredient because it gels — covered separately in this series [2].

What are the collagen types?

Collagen is not a single molecule but a family of at least 28 identified types, distinguished by their α-chain composition, structural assembly, and location in the body [3]. Only a few of these are directly relevant to food and confectionery applications.

Type I is the most abundant collagen in mammalian bodies, accounting for approximately 90% of total body collagen. It is composed of two α1(I) chains and one α2(I) chain wound into a triple helix and is found in skin, bones, tendons, and ligaments [3,7].  It is the dominant collagen type in essentially all hydrolyzed collagen peptides used in confectionery, and it is also the parent molecule of food gelatin.

Type II is found almost exclusively in cartilaginous tissues, including articular cartilage, tracheal cartilage, and the vitreous humor of the eye. It is composed of three identical α1(II) chains [3,7]. Type II collagen is primarily used in supplement and functional food products positioned around joint and mobility claims, with undenatured Type II being a distinct specialty category. It appears less commonly in mainstream confectionery.

Type III is composed of three identical α1(III) chains and is found in reticular fibers, skin, blood vessels, and internal organs, generally coexisting with Type I in the same tissues [3,7]. Commercially, bovine hydrolyzed collagen peptides typically contain Type I and Type III together in their natural ratio — approximately 90:10 to 80:20 — rather than as a purified single-type product.

Type IV forms a mesh-like network in basement membranes, the thin layer of tissue supporting epithelial cells, rather than the fibrillar structures characteristic of Types I, II, and III [3]. It has no meaningful application in confectionery, though it is occasionally referenced in supplement marketing.

Type V is present in small quantities alongside Type I, where it regulates the diameter of collagen fibrils during assembly [3]. It has no direct application in confectionery but may be present in trace amounts in bovine-sourced hydrolyzed collagen.

For confectionery formulators, the practical implications are that bovine hydrolyzed collagen is a Type I and Type III blend in natural ratio; marine collagen is essentially pure Type I with lower hydroxyproline content and reduced thermal stability; and Type II products are directed to joint-health positioning rather than general protein fortification, at a substantially higher cost per gram than Type I products.

‍

How is collagen produced?

Collagen production begins with raw connective tissue: bovine hides and bones, porcine skin, or fish skins and scales. The material is cleaned, defatted, and demineralized when needed (for bone-derived collagen, using dilute acid). It then undergoes an acid or alkaline pretreatment to swell the collagen matrix and remove non-collagenous proteins [2,5].

Hot water extraction breaks the native triple helix into single strands — the resulting solution is essentially gelatin. To produce hydrolyzed collagen peptides, gelatin is further hydrolyzed enzymatically with food-grade proteases such as Alcalase, papain, or bromelain, breaking the polypeptide chains into peptides with controlled molecular weight distribution, typically 2,000–10,000 Da [1]. The hydrolysate is deionized, filtered, and spray dried to a fine powder. Marine collagen follows the same pathway but begins from fish skin or scale streams, often recovered as byproducts of seafood processing [4,5].

What does collagen do in confections?

In confectionery, hydrolyzed collagen serves a fundamentally different purpose than gelatin. It does not gel, aerate, or provide structural function; instead, it delivers dissolved protein into the syrup or matrix without disrupting the setting behavior of gelling systems such as pectin or gelatin [1]. This makes it the ingredient of choice for protein-fortified gummies, chews, and hard candies where a marketing-relevant collagen dose — typically 2.5–10 g per serving — needs to dissolve cleanly into the cook without altering texture. Hydrolyzed collagen also contributes secondary functions: modest emulsification in fat-containing systems, minor foam stabilization in aerated candies, and, at higher inclusion, some water binding. The absence of a gelling function is a feature, not a limitation.

What is the molecular structure of collagen?

Native collagen has one of the most distinctive amino acid compositions in nature. Glycine occupies approximately every third residue and accounts for ~33% of total amino acids, proline for ~12%, and hydroxyproline for ~10% [3,6]. Hydroxyproline is essentially unique to collagen and is formed by post-translational hydroxylation of proline residues; its hydrogen-bonding capacity is what stabilizes the triple helix.

Three polypeptide α-chains, each approximately 1,000 amino acids and 100 kDa, wind together into a right-handed triple helix — the tropocollagen unit — at approximately 300 kDa [3,7]. On heat denaturation, the triple helix unfolds into random-coil single chains, producing gelatin. Further enzymatic hydrolysis cleaves the polypeptide backbone into peptides of 2,000–10,000 Da, producing hydrolyzed collagen — the form used in confectionery [1].

Marine collagen contains lower proline and hydroxyproline content than mammalian collagen, and consequently has a lower denaturation temperature (~25–30°C vs. ~35–40°C for bovine), a distinction with practical formulation implications where cold-processed or ambient-storage products are involved [4,5].

Because collagen lacks the essential amino acid tryptophan and is low in several others including methionine and cysteine, it does not qualify as a complete protein under FDA nutritional criteria. Its Protein Digestibility-Corrected Amino Acid Score (PDCAAS) is close to zero, which means that under 21 CFR 101.9, collagen contributes to total protein content on the Nutrition Facts Panel but cannot support a "high in protein" or "excellent source of protein" claim on its own. Formulators pursuing such claims typically pair collagen with a complete protein source such as whey.

‍

What are the functional properties of collagen in confections?

Solubility: Hydrolyzed collagen peptides are highly soluble in cold water, dissolving without a blooming step — a key operational advantage over gelatin [1].

Gelling: None. Hydrolyzed collagen does not gel at any practical concentration in confectionery systems. This is its defining functional distinction from gelatin, but it will change the texture in a gummy when it sets [2].

Thermal Behavior: As a fully hydrolyzed protein, hydrolyzed collagen is thermally stable across typical candy cook temperatures and does not denature in ways that affect performance. However, its free amino groups — particularly lysine — will participate in Maillard browning in the presence of reducing sugars during cooking and storage, contributing to color development and, if not managed, off-flavor formation over shelf life.

pH Stability: Hydrolyzed collagen tolerates acidic conditions better than gelatin and remains soluble across a broad pH range, useful in low-pH fruit gummies and hard candies [1].

Flavor: Neutral in most applications, though hydrolysates can carry a mild broth-like character detectable at high inclusion. Enzyme selection and hydrolysis conditions influence bitter peptide development, as with other protein hydrolysates [1].

Hygroscopicity and Shelf Stability: Collagen peptide powders are highly hygroscopic and require dry, low-humidity storage. Shelf stability in finished candies is limited primarily by Maillard browning of lysine residues over extended storage.

How is collagen regulated?

In the United States, collagen and hydrolyzed collagen peptides are permitted as food ingredients, with commercially used products supported by Generally Recognized as Safe (GRAS) notifications submitted to and reviewed by the FDA under the GRN system [9]. Multiple GRAS notices cover bovine, porcine, and fish collagen peptides. Collagen sourced from bovine tissues must comply with 21 CFR 189.5, which restricts the use of specified risk materials from cattle in human food as a BSE precaution.

Under the Food Allergen Labeling and Consumer Protection Act (FALCPA), collagen derived from fish must declare fish as a major allergen. In the European Union, collagen products carry no E-number but must comply with Regulation (EC) No 853/2004 on the hygiene of foods of animal origin. Halal and kosher certification of collagen products depends on species source and slaughter compliance and should be verified per market.

_____________________________________________________________________________________________

References

1. León-López, A., Morales-Peñaloza, A., Martínez-Juárez, V.M., Vargas-Torres, A., Zeugolis, D.I., & Aguirre-Álvarez, G. (2019). Hydrolyzed collagen — Sources and applications. Molecules, 24(22), 4031.

2. Schrieber, R., & Gareis, H. (2007). Gelatine Handbook: Theory and Industrial Practice. Wiley-VCH.

3. Ricard-Blum, S. (2011). The collagen family. Cold Spring Harbor Perspectives in Biology, 3(1), a004978.

4. Karim, A.A., & Bhat, R. (2009). Fish gelatin: properties, challenges, and prospects as an alternative to mammalian gelatins. Food Hydrocolloids, 23(3), 563–576.

5. Gómez-Guillén, M.C., Giménez, B., López-Caballero, M.E., & Montero, M.P. (2011). Functional and bioactive properties of collagen and gelatin from alternative sources: A review. Food Hydrocolloids, 25(8), 1813–1827.

6. Damodaran, S., & Parkin, K.L. (Eds.). (2017). Fennema's Food Chemistry (5th ed.). CRC Press.

7. Bornstein, P., & Sage, H. (1980). Structurally distinct collagen types. Annual Review of Biochemistry, 49, 957–1003.

8. Minifie, B.W. (1989). Chocolate, Cocoa and Confectionery: Science and Technology (3rd ed.). Van Nostrand Reinhold.

9. U.S. Food and Drug Administration. Generally Recognized as Safe (GRAS) Notice Inventory. Center for Food Safety and Applied Nutrition.

‍