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Yes, gelatin is a hydrolysed product of collagen

3 min read

Over 450,000 tons of gelatin are produced globally every year from animal by-products. This widely used gelling agent is fundamentally a hydrolysed product, created by breaking down the complex protein collagen into shorter polypeptide chains.

Quick Summary

Gelatin is derived from the partial hydrolysis of collagen, a structural protein found in animal connective tissues. This process breaks down the collagen's triple helix into shorter protein fragments, giving gelatin its unique gelling properties.

Key Points

  • Partial Hydrolysis: Gelatin is explicitly a product of the partial hydrolysis of collagen, breaking the large triple helix structure into smaller polypeptide chains.

  • Source Material: The process uses collagen-rich animal by-products like skin, bones, and connective tissues as raw materials.

  • Distinct from Collagen Peptides: Unlike collagen peptides, which are fully hydrolysed for higher bioavailability, gelatin is only partially hydrolysed, allowing it to retain its gelling properties.

  • Gelling Properties: The partial hydrolysis and thermal processing enable gelatin to form a gel by re-tangling its chains upon cooling, a key characteristic in its culinary applications.

  • Controlled Process: The degree of hydrolysis during manufacturing can be adjusted with varying heat, acid, or alkali treatments to produce different types of gelatin with distinct properties.

  • Incomplete Protein: Despite being 98-99% protein, gelatin is not a complete protein because it lacks the essential amino acid tryptophan.

In This Article

What Exactly Is Hydrolysis?

Hydrolysis is a chemical process where water is used to break down a larger molecule into smaller ones. In the case of gelatin, this process breaks the peptide bonds within the long, complex protein chains of collagen. Collagen, the raw material, is an insoluble fibrous protein that provides structural support to animal skin, bones, and cartilage. The hydrolysis of collagen converts this rigid, insoluble protein into a more water-soluble substance with very different properties.

The Manufacturing Process

The production of gelatin is a multi-step industrial process that relies heavily on controlled hydrolysis.

  1. Pretreatment: Raw materials, such as animal bones and hides, are prepared. This includes washing, degreasing, and either an acid or alkali treatment to swell the material and soften the collagen. The choice of acid or alkali affects the final gelatin's properties, creating Type A (acid-treated) or Type B (alkali-treated) gelatin.
  2. Hydrolysis and Extraction: The pre-treated material is heated in multiple stages with hot water. This thermal hydrolysis causes the collagen's triple helix structure to unwind and break apart, releasing gelatin into the water. Each extraction stage uses higher temperatures to draw out more gelatin, but also risks further degradation.
  3. Refining: The raw gelatin solution is then purified. This involves filtration to remove fat and insoluble particles, and ion exchange to remove salts.
  4. Concentration and Drying: Excess water is removed using vacuum evaporators until the solution thickens. It is then sterilized, cooled, and extruded into "gelatin noodles," which are dried with sterile air until brittle.
  5. Milling and Blending: The brittle gelatin is ground into a fine powder or granulated to meet specific product requirements.

Gelatin vs. Other Hydrolysed Products

While gelatin is a hydrolysed product, it is often confused with its more intensely processed counterpart, collagen peptides. The difference lies in the degree of hydrolysis.

Comparison Table: Gelatin vs. Collagen Peptides

Feature Gelatin Collagen Peptides (Hydrolysed Collagen)
Hydrolysis Partially hydrolysed. Completely hydrolysed.
Molecular Structure Longer, unfolded amino acid chains. Much smaller, pre-cut peptide fragments.
Gelling Property Yes, forms a gel when cooled. No, does not form a gel.
Solubility Dissolves only in hot water. Dissolves in both hot and cold water.
Digestion Easier to digest than raw collagen, but harder than peptides. Easiest for the body to absorb due to small size.
Use Case Thickeners in gummies, marshmallows, aspics, and desserts. Nutritional supplements, added to coffee, smoothies, etc..

The Role of Hydrolysis in Gelatin's Properties

Hydrolysis is the crucial step that dictates gelatin's unique characteristics. The controlled partial breakdown of collagen transforms its triple helix structure, which is responsible for the rigidity of connective tissue, into the single-strand polypeptides that give gelatin its functional properties. When heated, these polypeptide chains untangle, allowing them to dissolve in water. As the solution cools, the chains re-associate to form a tangled, three-dimensional network that traps water molecules, resulting in a gel. This thermo-reversible gelling ability is what makes gelatin so valuable in the food industry. The extent of hydrolysis, controlled by temperature and pH during manufacturing, determines the final product's gel strength, viscosity, and melting point. For example, gelatin derived from fish has a lower melting point than that from beef or pork.

The Amino Acid Profile: An Incomplete Protein

As a hydrolysed product, gelatin's nutritional profile is also a direct consequence of its origin. Gelatin is composed primarily of protein, with a high concentration of amino acids such as glycine, proline, and hydroxyproline, which are abundant in collagen. However, it is not a nutritionally complete protein because it is deficient in certain essential amino acids, most notably tryptophan. Despite this, its unique amino acid profile and high glycine content are associated with potential health benefits, including supporting skin health, joint function, and gut integrity. The health effects of gelatin are still a topic of ongoing research. For more information, you can consult authoritative sources like Wikipedia on Gelatin.

Conclusion: Gelatin Is Fundamentally a Hydrolysed Product

In conclusion, the answer to the question, 'is gelatin a hydrolysed product?' is a resounding yes. It is the result of the controlled partial hydrolysis of collagen, an insoluble protein found in animal connective tissues. This chemical process is what transforms collagen into the functional, thermo-reversible gelatin used extensively in the food, pharmaceutical, and cosmetic industries. Understanding this process provides insight into why gelatin behaves as it does, distinguishing it from both its raw material, collagen, and its fully processed counterpart, collagen peptides.

Frequently Asked Questions

Collagen is the large, triple-helix protein found naturally in animal connective tissues. Gelatin is the smaller, partially hydrolysed protein derived from collagen after it has been cooked or processed with heat and acid or alkali.

Gelatin undergoes partial hydrolysis, leaving its protein chains long enough to form a tangled, three-dimensional network that traps water when cooled. Collagen peptides, being fully hydrolysed, have protein fragments that are too small to form this gel network.

No, conventional gelatin is not vegan or vegetarian. It is always sourced from animal by-products containing collagen, such as bones, skins, and connective tissues of cows, pigs, or fish.

Compared to raw, unprocessed collagen, gelatin is easier to digest because its proteins have already been broken down into shorter chains through hydrolysis. However, it is less easily absorbed than fully hydrolysed collagen peptides.

No, gelatin is not a complete protein. Although it is high in protein, it is missing the essential amino acid tryptophan and is deficient in others, meaning it doesn't provide all the essential amino acids the human body needs.

At home, gelatin is made by cooking bones, skin, and cartilage-rich cuts of meat or fish for a long time. The collagen in these parts is naturally hydrolysed by the heat into gelatin, which dissolves into the liquid and forms a gel when cooled.

The hydrolysis process unwinds and breaks the triple helix of collagen into individual polypeptide strands. These strands can then re-tangle and re-form weak bonds upon cooling, which is the mechanism that creates the gel structure.

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Medical Disclaimer

This content is for informational purposes only and should not replace professional medical advice.