Delayed onset muscle soreness, resulting in uncomfortable and stiff muscles, is common after unaccustomed or strenuous exercise. While muscle strains induced by exercise are quite common in athletes, individuals with a lack of muscle fitness, and weak muscles as a result of aging, muscle and joint discomfort can also be the result of free radical damage and oxidative stress.
Formulated to Support Physical Recovery*
Though essential for survival, oxygen is also involved in toxic reactions that are a constant threat to our well-being. Most of the potentially harmful effects of oxygen are believed to be the result of the formation and activity of free radicals.2
Oxidative stress, encompassing oxidative damage to proteins, is brought on by the imbalance between free radical production and available antioxidants. Balance is of utmost importance for proper physiological function. Excessive free radicals from a normal body metabolism that includes glycation, for example, are believed to be major contributors to aging, muscle soreness and joint discomfort.3,4
Studies have shown that intense aerobic exercise can induce oxidative stress. Our body burns fuel at a faster rate with high-intensity physical exercise, which causes rapid chemical reactions that make free radicals at a faster rate. 4,5,6
Glycation occurs when sugar bonds with a protein or lipid to form compounds known as advanced glycation end products (AGE). These molecules speed up the oxidative process and damage cells. Research suggests that the accumulation of glycation end products in joint tissues cause joint stiff ness and discomfort.7
Our body’s response to oxidative stress includes redness, soreness, stiff ness or general discomfort. The immune system response to a physical condition under oxidative stress is perfectly normal and is actually a very important part of a healthy body. Our body naturally produces defense mechanisms in the form of antioxidants to quench free radical reactions. Enzymatic and non-enzymatic antioxidants work to neutralize oxidative stress by breaking down and removing free radicals and interrupting free radical chain reactions.
Therapeutic Proteolytic Enzymes
Proteolytic enzymes are responsible for protein degradation. When proteins are ingested, they pass thru stomach partially digested. In the small intestine, they are further degraded by proteolytic enzymes into smaller fragments. Studies have shown the therapeutic effect of proteolytic enzymes and potentially digesting oxidatively damaged protein accumulated as cellular debris.6
Identifying and degrading damaged proteins into smaller fragments for elimination may prevent accumulation or build-up that could otherwise create discomfort in joints and muscles.9
Proteolytic enzymes may also reduce muscle soreness and speed up recovery after an intense physical activity. In a small cohort study in men aimed to examine the effects of protease supplementation on delayed onset muscle soreness after an extraneous run. They concluded that protease supplementation including papain and bromelain in the blend may facilitate muscle healing and allow for faster muscle recovery after an intense physical activity.6
In addition, bromelain has shown to diminish the damaging effects of advanced glycation end products by degrading the protein receptor for AGE.10
Research has shown that enzymes including bromelain, papain and serrapeptase may be effective at reducing stress on muscle and joint function. One experimental study found that administering proteolytic enzymes that includes serrapeptase exhibit a therapeutic effect on oxidative stress reduction.11,12
Catalase, an antioxidant enzyme, is one of the body’s natural defenses against free radicals and oxidative stress. Oxidative cellular metabolism produces hydrogen peroxide molecules contributing to free radical damage. Catalase works to break down peroxide into water and oxygen thus protecting cells from free radicals. This enzyme is crucial in suppressing or preventing the formation of free radicals or reactive species in cells. Non-enzymatic antioxidants, such as the bioflavonoid rutin, is known to scavenge free radicals and contribute to protecting cells from oxidative stress. One study in vitro has shown that rutin had a therapeutic effect in reducing the amount of oxidative stress.13
In traditional medicine, rutin is known for its ability to help strengthen blood vessels and improve circulation. A review published in the International Journal of Molecular Sciences suggested that rutin may help reduce leg discomfort and cramping, likely due to its therapeutic effect in supporting the capillaries and overall leg circulation.14
In addition to the individual effects of antioxidants and proteolytic enzymes, these compounds interact in synergistic ways by protecting one another against oxidative destruction. Proteolytic enzymes are vital to many physiological processes in our body due to their catalytic function. With this known proteolytic property of proteases, they inhibit symptoms of physical conditions such as soreness and discomfort.6
References
1. U.S Department of Health and Human Services. The Centers for Disease Control and Prevention (CDC, 2019). National Center for Health Statistics for Exercise or Physical Activity. Report can be accessed at https://www.cdc.gov/nchs/fastats/exercise.htm
2. Whitney, E., Rolfes, R. (2016). Understanding Nutrition, Fourteenth Edition. Stanford, CT: Cengage Learning.
3. DeGroot, J., Bank, R. A., Bijlsma, J., TeKoppele, J. M., Verzijl, N., & Lafeber, F. (2004). Advanced glycation end-products in the development of osteoarthritis. Arthritis Research & Therapy, 6(Suppl 3), 78. doi:10.1186/ar1414
4. Simioni, C., et al. (2018). Oxidative stress: role of physical exercise and antioxidant nutraceuticals in adulthood and aging. Oncotarget. 9(24). doi: 10.18632/oncotarget.24729
5. Hussain, T., et al. (2016). Oxidative Stress and Inflammation: What Polyphenols Can Do For US? Oxidative Medicine and Cellular Longevity. doi:10.1155/2016/7432797 6. Miller, P.C., et al. (2003). The effects of protease supplementation on skeletal muscle function and DOMS following downhill running. Journal of Sports Sciences. 22. doi: 10.1080/02640410310001641584
7. Kim, C. S., Park, S., & Kim, J. (2017). The role of glycation in the pathogenesis of aging and its prevention through herbal products and physical exercise. Journal of exercise nutrition & biochemistry, 21(3), 55–61. doi:10.20463/jenb.2017.0027
8. Langseth, L. (1995). Oxidants, antioxidants, and Disease Prevention. Washington, D.C. International Life Sciences Institute (ILSI).
9. Davies, K.J. (1986). Intracellular proteolytic systems may function as secondary antioxidant defenses: an hypothesis. Journal od Free Radicals in Biology & Medicine. 2(2):129-34. 10. Stopper, H., Schinzel, R., Sebekova, K., Heidland, A. (2003). Genotoxicity of advanced glycation end products in mammalian cells. Cancer Letters. 190(2):151-6
11. Rathnavelu, V., Alitheen, N. B., Sohila, S., Kanagesan, S., & Ramesh, R. (2016). Potential role of bromelain in clinical and therapeutic applications. Biomedical reports, 5(3), 283–288. doi:10.3892/br.2016.720
12. Swamy, A.H., Patil, P.A. Effects of Some Clinically Used Proteolytic Enzymes on Inflammation. Indian Journal of Pharmaceutical Sciences. 70(1): 114-117. doi: 10.4103/0250-474X.40347
13. Nikfarjam, B.A., Adinen, M., Hajiali, F., Nassiri-Asl, M. (2017). Treatment with Rutin – A Therapeutic Strategy for Neutrophil-Mediated Inflammatory and Autoimmune Disease: Anti-inflammatory Effects of Rutin on Neutrophils. Journal of Pharmacopuncture, 20(1). doi: 10.3831/KPI.2017.20.003
14. Mansilha, A., & Sousa, J. (2018). Pathophysiological Mechanisms of Chronic Venous Disease and Implications for Venoactive Drug Therapy. International journal of molecular sciences, 19(6), 1669. doi:10.3390/ijms19061669
