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It is well established that optimal nutrition and digestion are paramount for improving athletic performance [1]. Optimal nutrition and digestion are even more important for the endurance athletes that experience frequent digestive stress due to prolonged training, racing and environmental toxicity exposure [2-4]. Due to heavy training loads, endurance athletes must consume a large quantity of calories simply to sustain energy, weight and muscle. Doing so during times of stress can compromise digestion (recent study on endurance runners also reports increased intestinal permeability after running [5]).

The nutrient digestion is a very complex process and involves participation of the brain, the gut, and the interaction of other organs such as the pancreas, the liver, the kidneys, the muscles and the nervous system [6, 7]. (Read here how optimal gut health may improve performance: How Pre and Pro Biotics Improve Your Performance).

Perhaps one of the most critical components for successful nutrient absorption is the availability and utilization of digestive enzymes. Why are digestive enzymes important? The majority of digestive enzymes are proteins that catalyze chemical reactions. They work by binding a substrate and forming an enzyme/substrate complex, which then reacts to form a new product. Digestive enzymes bind macromolecules (i.e., proteins, carbohydrates, lipids or other large molecules and long-chain nutrients) in order to break them down into their smaller building blocks and facilitate digestion. For example, amylases break down carbohydrates, proteases break down proteins, and lipases break down fats.

The digestive enzymes are found throughout the entire digestive tract: in saliva, in the lining of the stomach, the pancreas, and the intestinal walls. They can be obtained from plant and animal sources, as well as from certain micro-organisms. However, maintaining adequate digestive enzymes in our bodies can be challenging. Despite the fact that digestive enzymes are available in raw food, processing and cooking can destroy them. Or, taking antacids (stomach acidity neutralization aids) can inactivate proteases by raising the pH in the stomach. Also, inadequate chewing may inhibit the release of natural enzymes from food and it can also limit the activity of amylases. Many, if not most of us often cook our foods, likely not chewing enough and if we feel some gut discomfort we may even pop a few antacids. In addition to avoiding over-cooking and trying to chew better, one can improve the bioavailability of the foods and reduce gut discomfort by introducing digestive enzymes.

Because of the importance of the digestive enzymes in nutrient absorption, and because their availability is often compromised, supplementation may be useful. In disease, supplementation of digestive enzymes has been extensively used to treat metabolic disorders, obesity, diabetes or intestinal disorders and inflammation [8-11]. In health, digestive enzyme supplementation may enhance digestion and promote wellbeing. Research shows that in multiple animal-feed models, supplementation of digestive enzyme blends aids digestion, nutrient absorption, overall health and performance [12].

In humans, in vitro systems have been successfully developed to study nutrient decomposition [13]. For example, the enzyme alpha-amylase, which is the dominant enzyme that hydrolyzes starch, has been shown to act synergistically with the alpha-glucosidase enzyme (a glycoside enzyme) [14, 15]. In fact, the rate of carbohydrate hydrolysis enhancement of up to 1017-fold is typical for glycosides, placing them among the most proficient enzymes [16]. A proteolytic enzyme, bromelain, which is a crude extract from pineapple, has demonstrated anti-inflammatory, anti-thrombotic, and fibrinolytic properties placing it as one potent phyto-therapeutic drug [17].

In addition to health benefits, research suggests that digestive enzyme supplementation may aid athletic performance, especially in endurance athletes, who often experience digestive stress during training and racing [3].  A clinical trial performed using a 160mg blend of amylase, cellulase and hemicellulase consumed with a meal replacement bar prior to exercise during a 60 minutes of high intensity cycling. Cyclists consumed a meal replacement bar and placebo, or a meal replacement bar and 160mg enzyme blend. Blood glucose levels were consistently and significantly higher for the enzyme group vs. the placebo. Lactate values were also significantly lower in the enzyme group. Subjects on the enzyme group were able to sustain 100% VO2max significantly longer than those in the placebo group [18]. A recent study on runners that regularly experience GI distress compared to runners that do not showed that running-induced intestinal permeability (appeared in both groups) might worsen GI symptoms because of the elevated serum LPS (lipopolysaccharide) levels in the GI symptomatic group [5]. Although elevated blood LPS and GI symptoms is somehow uncertain, the undoubtable inflammatory activity of elevated LPS can be neutralized with LPS-synthetic peptides derived from serum amyloid P component [19].

In conclusion, for hard training endurance athletes that consume higher amounts of calories and may have compromised digestion, digestive enzyme supplementation could be beneficial. The ability of enzymes to increase the rate at which nutrients are broken down can help increase blood glucose or protect against inflammation/toxicity and therefore, potentially lead to enhanced performance parameters.

 

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MultiV and MultiVPRO contains a potent Carbo Enzyme Blend (amylase, hemicellulase, cellulase and bromelain) that increases nutrient digestion and offers increased health and potential performance benefits to the endurance athlete.  These enzymes are further supported with the Pre and ProBiotic blend found specifically in MultiVPRO. Probiotics may additionally enhance the immunity, antioxidation, digestive enzyme activity and hematological profile [20].

References

  1. American College of Sports, M., A. American Dietetic, and C. Dietitians of, Joint Position Statement: nutrition and athletic performance. American College of Sports Medicine, American Dietetic Association, and Dietitians of Canada. Med Sci Sports Exerc, 2000. 32(12): p. 2130-45.
  2. Marynowski, M., et al., Role of environmental pollution in irritable bowel syndrome. World J Gastroenterol, 2015. 21(40): p. 11371-8.
  3. Waterman, J.J. and R. Kapur, Upper gastrointestinal issues in athletes. Curr Sports Med Rep, 2012. 11(2): p. 99-104.
  4. Halvorsen, F.A., et al., Gastrointestinal disturbances in marathon runners. Br J Sports Med, 1990. 24(4): p. 266-8.
  5. Karhu, E., et al., Exercise and gastrointestinal symptoms: running-induced changes in intestinal permeability and markers of gastrointestinal function in asymptomatic and symptomatic runners. Eur J Appl Physiol, 2017. 117(12): p. 2519-2526.
  6. Goodman, B.E., Insights into digestion and absorption of major nutrients in humans. Adv Physiol Educ, 2010. 34(2): p. 44-53.
  7. Levin, R.J., Digestion and absorption of carbohydrates–from molecules and membranes to humans. Am J Clin Nutr, 1994. 59(3 Suppl): p. 690S-698S.
  8. Tucci, S.A., E.J. Boyland, and J.C. Halford, The role of lipid and carbohydrate digestive enzyme inhibitors in the management of obesity: a review of current and emerging therapeutic agents. Diabetes Metab Syndr Obes, 2010. 3: p. 125-43.
  9. Mukherjee, M., Human digestive and metabolic lipases – a brief review. Journal of Molecular Catalysis B-Enzymatic, 2003. 22(5-6): p. 369-376.
  10. Roxas, M., The role of enzyme supplementation in digestive disorders. Altern Med Rev, 2008. 13(4): p. 307-14.
  11. Tiwari, A.K. and J.M. Rao, Diabetes mellitus and multiple therapeutic approaches of phytochemicals: Present status and future prospects. Current Science, 2002. 83(1): p. 30-38.
  12. Choct, M., Enzymes for the feed industry: past, present and future. World’s Poultry Science Journal, 2006. 62(01): p. 5-16.
  13. Kopf-Bolanz, K.A., et al., Validation of an in vitro digestive system for studying macronutrient decomposition in humans. J Nutr, 2012. 142(2): p. 245-50.
  14. Sun, Z.T. and C.A. Henson, A quantitative assessment of the importance of barley seed alpha-amylase, beta-amylase, debranching enzyme, and alpha-glucosidase in starch degradation. Arch Biochem Biophys, 1991. 284(2): p. 298-305.
  15. Dhital, S., et al., Mammalian mucosal alpha-glucosidases coordinate with alpha-amylase in the initial starch hydrolysis stage to have a role in starch digestion beyond glucogenesis. PLoS One, 2013. 8(4): p. e62546.
  16. Rye, C.S. and S.G. Withers, Glycosidase mechanisms. Curr Opin Chem Biol, 2000. 4(5): p. 573-80.
  17. Maurer, H.R., Bromelain: biochemistry, pharmacology and medical use. Cell Mol Life Sci, 2001. 58(9): p. 1234-45.
  18. Frank, L.L., et al., The effects of a pre-exercise feeding with or without fungal carbohydrases (Carbogen) on blood parameters and exercise performance in elite cyclists: a preliminary study. Int J Sport Nutr Exerc Metab, 2002. 12(3): p. 310-7.
  19. de Haas, C.J., et al., Lipopolysaccharide (LPS)-binding synthetic peptides derived from serum amyloid P component neutralize LPS. Infect Immun, 1999. 67(6): p. 2790-6.
  20. Isolauri, E., et al., Probiotics: effects on immunity. Am J Clin Nutr, 2001. 73(2 Suppl): p. 444S-450S.