Journal of Food Technology and Preservation

All submissions of the EM system will be redirected to Online Manuscript Submission System. Authors are requested to submit articles directly to Online Manuscript Submission System of respective journal.
Reach Us +44-1518-081136

Rapid Communication - Journal of Food Technology and Preservation (2023) Volume 7, Issue 3

Collagen: The structural protein that supports body's strength and flexibility.

Feng Yifeng*

College of Food Technology, Northwest A&F University, Xianyang, China

*Corresponding Author:
Feng Yifeng
College of Food Technology
Northwest A&F University, Xianyang, China
E-mail: feng.yifeng@nwsuaf.edu.cn

Received: 23-Mar-2023, Manuscript No. AAFTP-23-94093; Editor assigned: 24-Mar-2022, PreQC No. AAFTP-23-94093 (PQ); Reviewed: 08-Apr-2023, QC No. AAFTP-23-94093; Revised: 12-Apr-2023, Manuscript No. AAFTP-23-94093 (R); Published: 19-Apr-2023, DOI:10.35841/2591-796X-7.4.177

Citation: Yifeng F. Collagen: The structural protein that supports body's strength and flexibility. J Food Technol Pres 2023;7(4):177

Visit for more related articles at Journal of Food Technology and Preservation

Abstract

Collagen is a vital protein that makes up around one-third of the protein in our body. It is found in our skin, bones, muscles, tendons, and cartilage. It acts as glue that holds our body together, providing strength, support, and flexibility. Without collagen, our body would not be able to function properly. Collagen is a type of protein that is made up of long chains of amino acids. There are over 28 different types of collagen, but most of the collagen in our body belongs to one of three types: Type I, Type II, or Type III. Type 1 collagen is the most abundant collagen type in the human body and plays a crucial role in maintaining the structure, strength, and function of various tissues and organs.

Keywords

Collagen, Amino acids, Hydroxyproline, Ligaments.

Introduction

Collagen is a fibrous protein that provides support and structure to the body, and type 1 collagen is a specific type of collagen found in skin, tendons, ligaments, bones, and other connective tissues. Type 1 collagen is a triple helix composed of three chains of amino acids, each containing around 1,000 amino acids. These amino acids are arranged in a repeating pattern of glycine, proline, and hydroxyproline, which gives the protein its unique structure and stability. The triple helix of type 1 collagen is stabilized by intermolecular cross-links between lysine and hydroxylysine residues. Tendons and Ligaments: Type 1 collagen is the primary component of tendons and ligaments, which connect muscles to bones and bones to each other. It helps to maintain their strength and flexibility, allowing for smooth movement and preventing injury. Blood vessels: Type 1 collagen is also found in the walls of blood vessels, where it provides structural support and helps to maintain their elasticity and integrity [1,2].

Type II collagen is found in our cartilage, while Type III collagen is found in our skin, blood vessels, and internal organs. Collagen is produced by cells called fibroblasts, which are found in our skin, bones, and connective tissue. When fibroblasts produce collagen, they secrete it into the extracellular matrix, where it forms a network of fibers that provide support and strength to our tissues. Collagen is essential for maintaining the strength and flexibility of our body's tissues. As we age, our body's ability to produce collagen decreases, leading to a loss of skin elasticity, joint pain, and weaker bones. Collagen is also important for our skin's health. It helps to maintain the skin's elasticity, preventing wrinkles and sagging. In fact, collagen makes up around 80% of our skin's dermis layer, which is responsible for its structure and support. In addition to its benefits for our skin, collagen is also important for our joint health. It provides cushioning for our joints, helping to prevent injury and reducing joint pain and stiffness [3,4].

Collagen has also been shown to have benefits for our gut health. It helps to strengthen the gut lining, reducing inflammation and improving digestive function. While our body's ability to produce collagen decreases with age, there are several ways we can help to boost collagen production. One way is to eat a diet rich in collagen-building nutrients. This includes foods such as bone broth, salmon, berries, and leafy greens, which are high in vitamins and minerals that support collagen production. Supplements such as collagen peptides, which are easily absorbed by the body, can also be helpful in boosting collagen production. These supplements are typically made from animal sources such as bovine or fish collagen. Another way to support collagen production is to protect our skin from sun damage [5].

Conclusion

UV rays can damage collagen fibers, leading to premature aging and wrinkles. Using sunscreen and wearing protective clothing can help to prevent this damage. Finally, avoiding habits such as smoking and excessive alcohol consumption can also help to support collagen production. These habits can damage collagen fibers and reduce our body's ability to produce new collagen. Collagen is a vital protein that is essential for maintaining the strength and flexibility of our body's tissues. As we age, our body's ability to produce collagen decreases, leading to a loss of skin elasticity, joint pain, and weaker bones. Fortunately, there are several ways we can help to boost collagen production, such as eating a diet rich in collagen-building nutrients, taking supplements, protecting our skin from sun damage, and avoiding habits such as smoking and excessive alcohol consumption. By supporting our body's collagen production, we can maintain our skin's health, reduce joint pain and stiffness, and support our overall health and wellness.

References

  1. Cho KA, Ju SY, Cho SJ, et al. Mesenchymal stem cells showed the highest potential for the regeneration of injured liver tissue compared with other subpopulations of the bone marrow. Cell Biol Int. 2009;33(7):772-7.

    2. Indexed at, Google Scholar, Cross ref

  2. Içier F, Baysal T. Dielectrical properties of food materials-2: Measurement techniques. Crit Rev Food Sci Nutr. 2004;44(6):473-8.

    3. Indexed at, Google Scholar, Cross ref

  3. Aragrande M, Canali M. Integrating epidemiological and economic models to identify the cost of foodborne diseases. Exp Parasitol. 2020;210:107832.

    4. Indexed at, Google Scholar, Cross ref

  4. Troller JA. Trends in research related to the influence of “water activity” on microorganisms in food. Adv Exp Med Biol. 1991:305-13.

    5. Indexed at, Google Scholar, Cross ref

  5. Garrigues C, Johansen E, Crittenden R. Pangenomics–an avenue to improved industrial starter cultures and probiotics. Curr Opin Biotechnol. 2013;24(2):187-91.

    6. Indexed at, Google Scholar, Cross ref

Get the App