Is gelatin biodegradable? (7 applications of gelatin)

This article will answer the question of the biodegradability of gelatin.

Furthermore, it will discuss other topics that include:

  • Properties of gelatin.
  • Applications of gelatin.
  • Eco-friendliness of gelatin.

Is gelatin biodegradable?

Yes, gelatin is biodegradable. Gelatin is an organic compound of proteins that are made from collagen Organic compounds derived from plants and animals are highly susceptible to enzymatic degradation by microorganisms such as bacteria and fungi.

Organic molecules such as cellulose, chitin, starch, glycogen, and proteins are broken down by microorganisms to get energy and also produce simpler molecules that are assimilated by the microbes.

What is biodegradation?

Biodegradation is the breakdown of organic matter by microorganisms, such as bacteria and fungi into the water, carbon dioxide, methane, and minerals. Heat energy is produced in the process.

Biodegradation occurs in three distinct stages: biodeterioration, bio-fragmentation, and assimilation.

Biodeterioration is the first stage of biodegradation that involves abiotic factors such as light, UV radiation, and water to help in the weakening of the structure of organic substances.

Bio-fragmentation is the second stage that involves the physical breakdown of organic matter into small particles, this is due to the biodeterioration of the organic matter in the first stage.

Assimilation is the last stage of biodegradation. It involves the bacteria and the fungi taking up the minerals and small biomass produced by the previous two stages into their biological systems.

The minerals are used as a source of energy and carbon for the synthesis of cells and tissues.

Biodegradation can occur in the presence or absence of oxygen. When biodegradation involves the microorganisms using oxygen, the process is called aerobic biodegradation.

Aerobic biodegradation produces carbon dioxide, water, and small biomass. Heat energy is also produced in the process. Aerobic biodegradation occurs very fast but it is not very efficient.

When biodegradation occurs in the absence of oxygen, it is called anaerobic biodegradation. The products of anaerobic biodegradation include water, carbon dioxide, and small biomass. 

In addition to these products, methane gas is also produced. Heat energy is released during the breakdown. 

Anaerobic biodegradation occurs slowly but is more efficient than aerobic biodegradation.

Biodegradation can be affected by several factors such as water, light, temperatures, the bioavailability of a molecule, and pH.

Water helps in the biodeterioration and mechanical fragmentation of substances, increasing the surface area for microbial degradation.

Light emits radiations that help in the biodeterioration and bio-fragmentation of organic matter. UV radiation is the most effective radiation. 

Temperature affects the rate of biodegradation. Some microorganisms are very active in high temperatures while others are active in low temperatures. The optimum temperatures for the microorganisms increase the rate of biodegradation.

Bioavailability is the availability of an organic substance to microorganisms. Highly concentrated organic matter has high bioavailability and this increases the rate of biodegradation.

pH is the measure of acidity or basicity of a substance. Some microorganisms are very active in acidic pH while others are active in neutral or alkaline pH. Optimum pH increases the rate of biodegradation.

What is gelatin?

Gelatin is an organic compound that is derived from collagen obtained from the body parts of animals.

It is highly made from the byproducts of leather and animal meat. The most used parts include cattle bones, split cattle hides, pork skins, and pork meat.

Due to high religious concerns about the use of animals to produce gelatin, fish byproducts have also been used to produce gelatin.

Gelatin can be made in industries by treating the aforementioned animal parts with acid and alkali while gelatin can be made at home by boiling collagen-rich body parts

Different processes of gelatin production involve the breaking down of bonds connecting the collagen molecules.

What is the component of gelatin?

Gelatin is derived from processing the collagen fibers that are acquired from the connective tissues of animals such as bones and muscles.

Collagen.

This is the main structural protein in the extracellular matrix of animals. It is found in the connective tissues together with the elastic fibers. Collagen is the most abundant protein in mammals.

Connective tissues with most collagen include bones, cartilage, tendons, skin, and ligaments.

The hardness and stiffness of collagen depend on biomineralization and it results in rigid collagen found in bones and compliant collagen found in the tendons. The intermediate between rigid and compliant collagen forms cartilage.

Collagen is produced by fibroblast cells.

There are different types of collagen, they include:

  • Type I collagen: this type of collagen is found in the tendons, bones, organs, and vasculature.
  • Type II collagen: this type of collagen forms the cartilage.
  • Type III: This type of collagen forms the reticular fibers, it is found alongside type I collagen.
  • Type IV: this collagen type forms layers of the basement membrane called the basal lamina.
  • Type V: this collagen forms the hair, cell surfaces, and placenta.

Uses of collagen.

Collagen is used in the following ways:

  • It is used as a healing aid for burns. 
  • It is used to reconstruct fractured bones.
  • It is used as a dermal filler to treat wrinkles and skin aging.
  • Collagen is used in the regeneration of tissues.
  • It is used in the manufacturing of artificial skin.

How is gelatin processed?

The process of gelatin production undergoes three distinct stages that include:

  • Pretreatment: this stage is essential in making the raw material ready for processing. It also helps in the removal of impurities that may affect the properties of gelatin.

Pretreatment involves the use of dilute acid solutions to remove calcium and other salt impurities.

Hot water is used to remove fat content to less than 1%. The pretreatment process also involves the use of hairs from the hide.

  • Hydrolysis: This is the main stage of converting collagen to gelatin.

After the pretreatment, the collagen molecule is converted to gelatin through hydrolysis. Hydrolysis can be achieved through the use of acids, alkali, and enzymes.

Acid is used to hydrolyze less complex collagen like that from pigs while alkali solution is used for more complex collagen, like those of cowhides.

Gelatin obtained from acid treatment is called type A gelatin, while that obtained from alkali treatment is called type B gelatin.

Enzymatic hydrolysis is still in its early stages of development and it is anticipated that it will take a shorter time than the alkali treatment, producing better quality gelatin.

  • Extraction: this is the stage after hydrolysis. It involves extracting the hydrolyzed gelatin using water or acids. 

It is a multi-step process that is dependent on pH and temperature.

  • Recovery: this is a multi-step process that includes processes such as filtration, evaporation, grinding, drying, and sifting.

Gelatin is protein-based and therefore temperature-sensitive, and it, therefore, should be recovered under low temperatures to avoid damage through degradation.

What are the applications of gelatin?

The following are the different applications of gelatin.

  • It is used as a thickener, stabilizer, or texturizer in creams, cheese, margarine, and yogurt.
  • It is used to create the mouthfeel of fats in fat-reduced products.
  • It is used in the production of some Chinese soups.
  • It is used as a gelling agent in food products such as gelatin desserts, aspic, marshmallows, candy corn, and trifles.
  • It is used in cosmetics to improve the texture and to act as a moisturizer.
  • The gelatin used to be applied in capsules to ease the swallowing.
  • Unrefined gelatin can be used as glue.
  • It is used to make hydrogels that are used in biotechnology for tissue engineering.

Is gelatin toxic?

Yes, gelatin can cause allergic reactions in some people.

According to a study, gelatin supplements can cause side effects such as burping, bloating, and upset stomach.

The Food and Drug Administration (FDA) body considers gelatin safe to use. Gelatin doesn’t cause known human diseases although researchers are cautious about people contracting animal diseases that might come with gelatin.

Conclusion.

This article has covered the question of the biodegradability of gelatin.

It has also covered other topics such as:

  • Applications of gelatin.
  • Components of gelatin.
  • The processing of collagen.
  • Types of collagen.
  • Toxicity of gelatin.

For any questions or comments please use the comment section below

Frequently Asked Questions (FAQs): is gelatin biodegradable?

Is gelatin environmentally friendly?

Yes, gelatin is biodegradable and therefore does not accumulate in the environment, causing pollution.

It is sustainable because it is produced from natural sources. 

Why is gelatin biodegradable?

Gelatin is biodegradable because it is an organic material derived from organic collagen protein. Collagen is highly susceptible to microbial degradation because of its organic nature.

What is gelatin made of?

Gelatin is made up of collagen, which is a protein molecule derived from the connective tissues of mammals.

Citations.

Alexandra Rowles. ( June 4, 2017). What Is Gelatin Good For? Benefits, Uses, and More.

Retrieved from:

https://www.healthline.com/nutrition/gelatin-benefits

MaryAnn De Pietro. ( December 12, 2021). What is Gelatin made of, and is it good for you? Reviewed by Amy Richter.

Retrieved from:

https://www.medicalnewstoday.com/articles/319124

Poppe, J. (1997). Gelatin, in A. Imeson (ed.) Thickening and Gelling Agents for Food (2nd ed.): 144–68. London: Blackie Academic and Professional.

Bogue, Robert H. (1923). “Conditions Affecting the Hydrolysis of Collagen to Gelatin”. Industrial and Engineering Chemistry. 15 (11): 1154–59. doi:10.1021/ie50167a018.

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