Performance Differences Among Collagen Protein, Gelatin, and Hydrolyzed Collagen Protein

Introduction to Collagen Protein, Gelatin, and Hydrolyzed Collagen Protein

Collagen (Collagen Protein) is an important functional substance that constitutes the animal body, prevalent in various organs within animals, and plays a significant role in regulating the normal physiological functions of these organs. 

Collagen protein possesses biocompatibility, biodegradability, and bioactivity that are unmatched by other synthetic materials, such as low antigenicity, ease of absorption by the human body, promotion of cell survival and growth, and platelet aggregation. After special treatment, collagen protein can be used in medical and health sectors for the treatment of burns and wounds, beauty, orthopedics, tissue repair, and wound hemostasis. 

Currently, it is applied in clinical settings such as collagen membranes for burn and trauma treatment, collagen medical injectables for cosmetic and orthopedic purposes, and collagen hemostatic sponges for trauma hemostasis. As a skin structural protein, collagen plays a moisturizing, conditioning, and hydrating role in skincare products. Therefore, collagen protein, as a natural biological resource, can be widely applied in food, medicine, livestock, cosmetics, fishery, and health care.

Gelatin is a denatured product of collagen protein under the action of high temperature, also with significant application value in food, medicine, and hygiene sectors. Gelatin is a high-nutritional-value, low-calorie health food. Its applications in food include: candy additives to make candy more elastic, tough, and transparent; frozen food additives like gelling agents and stabilizers; meat product improvers, for instance, adding gelatin to meat products can enhance product quality; it can also serve as a dairy product additive, food coating material, and in cake production. In the medical and health sector, gelatin is mainly used for making drug capsules.

Hydrolyzed collagen protein is a hydrolysis product of collagen, having a smaller relative molecular weight and is easier to degrade, thus holding a certain market in nutrition and health product development and daily chemical products development. Hydrolyzed collagen can be used as a biological fermentation culture medium and as a high-protein feed nutritional additive to replace imported fishmeal for the production of mixed feed.

Performance Differences among Collagen, Gelatin, and Hydrolyzed Collagen Protein

Although collagen, gelatin, and hydrolyzed collagen protein are homologous substances, they have significant differences in structure and properties. Collagen protein retains its unique natural helical structure and shows performance in certain aspects that is significantly superior to gelatin and hydrolyzed collagen protein, such as the hemostatic performance of collagen hemostatic sponge being better than gelatin sponge, and the settling ability of denatured fish collagen being significantly reduced if denatured. 

However, people's understanding often leads to confusion, thinking they have the same properties or even considering them as the same substance. Here are a few aspects to illustrate their differences.

Comparison of Relative Molecular Weight

Collagen protein has the largest relative molecular weight, with each polypeptide chain having a relative molecular weight of 100,000, and three polypeptide chains forming one collagen molecule with a relative molecular weight of 300,000; Gelatin's relative molecular weight mainly ranges from tens of thousands to 100,000; Hydrolyzed collagen protein has a smaller relative molecular weight than gelatin, primarily ranging from thousands to 30,000.

Comparison of Film-Forming Properties

Hydrolyzed collagen protein cannot form films, whereas collagen protein and gelatin can.

Comparison of Refibrillation Properties

Only collagen solution has the unique property of refibrillation, a property not possessed by its denatured product gelatin and degraded product hydrolyzed collagen protein.

Collagen molecules retain their unique triple-helix structure, while its hydrolysis products - gelatin and hydrolyzed collagen protein do not have this triple-helix structure. The reason is the irreversibility of hydrolysis.

Comparison of Cell Biological Properties

Due to the influence of hydrolysis, gelatin and hydrolyzed collagen protein lose the triple-helix structure inherent in collagen protein and therefore lose its bioactivity.

Collagen protein is a structural protein existing in the form of collagen fibers in vivo. Collagen extracted at low temperatures still maintains the triple-helix structure, has a relative molecular weight of 300,000, forms membranes with good flexibility, elasticity, and strength, and can refiber under simulated physiological conditions to significantly activate cell growth. 

Gelatin's triple-helix structure has been destroyed, and its relative molecular weight distribution is wide, ranging from tens of thousands to 100,000; Gelatin can gelatinize and form films, but gelatin films are brittle and less strong than collagen films. Hydrolyzed collagen protein is a mixture of polypeptides with a relative molecular weight ranging from thousands to tens of thousands; Hydrolyzed collagen protein cannot form films. 

Neither gelatin nor hydrolyzed collagen protein can form fibers again, and cell growth experiments have shown that they do not have the property of promoting cell growth, meaning neither gelatin nor hydrolyzed collagen protein have bioactivity.