Tag Archives: digestive enzymes

Only 30 Grams of Protein Per Meal?

10 Jun

Only 30 Grams of Protein Per Meal?

Tim Skwiat, MEd, CSCS, Pn2

This is a really good—and important—question, and it’s one that we hear quite frequently, albeit it in a number of different ways. It can be best summed up like this: “I heard that you should only consume 30 grams of protein per meal, and anything beyond that is wasted. Is that true?”

When asked this question, prominent protein and amino acid researcher Dr. Donald Layman (Professor Emeritus in the Department of Food Science & Human Nutrition at the University of Illinois) said:

“It is one of my biggest pet peeves in the area.”1

 The short answer is: While there may be a limit on how quickly the body can absorb protein, this is presumption is not true, and there is really no evidence to indicate that 30 grams is the “magic number” that should be consumed per meal.

However, I wouldn’t be satisfied providing you a short answer—particularly without supporting evidence—and I hope that you wouldn’t be either.


A good starting point for some background on this question and the benefits of a high-protein intake is understanding the difference between protein “need” and “optimization,” which you can learn about it the following article:

Why Is Optimizing Protein Intake So Important?

For starters, as is outlined in that article, there are a host of metabolic advantages associated with a higher protein intake.2 Higher protein diets have been shown to:

  • Accelerate fat loss and spare calorie-burning lean body mass when following a reduced-calorie diet.
  • Prevent weight regain and contribute to long-term weight maintenance.
  • Optimize 24-hour muscle protein synthesis and facilitate the maintenance or building of calorie-burning lean muscle mass.
  • Boost metabolic rate.
  • Preserve metabolic rate after weight loss.
  • Increase satiety and improve appetite control.
  • Improve carbohydrate metabolism and glycemic regulation.
  • Increase calcium absorption.

As described in the section Establishing the ‘New Normal,’ a high-protein diet would involve an intake upwards of 0.8 – 1 gram of protein per pound of body weight per day. Thus, you can see that body weight is one of the factors that may dictate how much protein is consumed per meal. With that in mind, a 200-pound man and a 150-pound women would have significantly daily protein needs. If the 30-gram rule were in play, then each would have to spread their protein intake out over the appropriate number of meals (i.e., 7 and 5, respectively). However, the available evidence—both scientific research and real-world experience—tells us that, when it comes to body composition, meal frequency doesn’t matter when other variables (e.g., food choices, portion sizes) are controlled.

In one randomized controlled crossover trial published in The American Journal of Clinical Nutrition, researchers compared the effects of reducing meal frequency on a variety of health indicators in healthy, normal-weight adults. The study involved two 8-week treatment periods, during which time the participants consumed all of the calories (and protein, which was about 80 grams per day) needed for maintenance in either 3 meals per day or 1 meal per day.3

At the end of the study, the researchers found no effect of meal frequency on heart rate, body temperature, or the majority of blood chemistry variables. What they did find, however, was that the reduced meal frequency (i.e., 1 meal per day) result in a significant improvement in body composition marked by reduced body fat and modestly increased lean body mass, which one might have expected to drop.

In another randomized controlled crossover trial published in The American Journal of Clinical Nutrition, researchers from the University of Amsterdam provided further evidence that reduced meal frequency (a form of intermittent fasting) has no negative effect on lean body mass even when consuming an entire day’s worth of protein (80 – 100 grams) in a single 4-hour period.4

In a study published in The American Journal of Clinical Nutrition, French researchers a single protein feeding was more effective (in terms of protein synthesis) than four balanced protein feedings among a group of healthy older women.6 In a separate study published in The Journal of Nutrition, the same French researchers found no difference (in protein synthesis or breakdown) when healthy young women were given 0.77 grams of protein per pound of body weight per day either in one feeding or spread across four feedings.

Please see the section of the article above titled Show Me the Data for a litany of studies demonstrating that high-protein diets accelerate weight and fat loss and spare lean body mass.


The general consensus is that most folks will probably do best with 3 – 4 meals per day, spreading out their protein intake relatively evenly across those meals (rather than a “skewed” intake of protein). Please see the Balanced Bites section in the article cited above for more information.

As you’ll see in that section, researchers have made per-meal suggestions for protein intake based on maximizing muscle protein synthesis (MPS). In other words, a per-meal protein amount of about 0.18 grams of protein per pound of body weight optimally stimulates MPS and ingestion of protein beyond that amount does not appear to have any further impact on MPS.7,8 These findings have been similar among healthy young folks regardless of the type of food (i.e., protein supplements or whole food), whether at rest or after exercise, and regardless of fitness level.9–12

With that being said, a key finding to point out here is that the amount of protein needed to maximally stimulate MPS in healthy older men is substantially higher than the amount needed by healthy younger men. In other words, in addition to body weight, age also appears to be an important contributing factor when determining protein needs.

While larger amounts of protein can indeed be consumed and digested, they do not appear to further stimulate MPS, but they are oxidized at a higher rate, resulting in the production of urea.11,12 As Professor Layman has said on a number of occasions, “The notion that [protein] oxidation is bad I think is totally misleading.”1 As an adult, the body strives for balance/homeostasis, and increased protein oxidation concomitant with a higher intake is reflective of that (i.e., nitrogen balance). That being said, if we can swing the equation in favor of positive nitrogen balance while still consuming more protein, that may be worth discussing, which we will below.

Before moving on, one important thing to note is that these findings are based off acute protein-only feedings. In other words, it’s unknown how mixed meals may influence MPS.


With these MPS findings in mind, it’s plausible that the notion that the body can only “use” 30 grams of protein per feeding may have been born. However, if you go back to the article cited above, you’ll see that there are myriad benefits and metabolic advantages to high-protein diets beyond stimulating MPS.

For instance, high-protein diets increase satiety and improve appetite control.13,14 High-protein meals boost satiety, which means that protein-dense foods are much more likely to make you feel full and satisfied.13 What’s more, diets rich in high-quality proteins improve appetite control and reduce cravings, as well as reduce daily food intake.15

All foods that you eat requires calories to be burned in order to digest, absorb, and assimilate their nutrients. This is referred to as the Thermic Effect of Feeding (TEF). There is a general consensus in the scientific literature that protein stimulates TEF to a greater extent than other macronutrients (e.g., carbohydrates, fat).16 In fact, protein-rich foods are estimated to boost metabolic rate by as much as 30%, whereas as fats and carbohydrates are typically estimated to be in the 5 – 10% range.13

In other words, protein-rich foods have the greatest TEF, boosting the metabolism THREE to SIX TIMES more than carbs or fats.

This means that you burn more calories each day when you consume a high-protein diet, and it also means that protein-rich foods provide less metabolizable energy (than carbs or fats).17 This latter point is important to note. Going back to the section above about MPS, this means that “extra” protein that is oxidized provides less energy (i.e., calories) than carbs or fats, and as a result, the calories from protein are less likely to be stored as fat.

This leads to another great question. If you’re not eating protein, what else will you eat?

Along these lines, Professor Steve Simpson formulated the protein leverage hypothesis, which essentially posits that protein can reduce the intake of other nutrients (e.g., carbs, fats) due to a homeostatic mechanism based around a protein “seeking” behavior.18 In other words, protein is the driving force for appetite, and our bodies are programmed to eat toward a protein target.

Professor Simpson describes, “Interestingly, if protein in the diet is diluted, even by a small amount by extra fat and carbohydrate, the appetite for protein dominates and they will keep eating in an attempt to attain their target level of protein.”

A number of randomized controlled trials have tested Professor Simpson’s protein leverage hypothesis, and they have found that lower protein intakes are associated with the consumption of more snacks between meals and greater daily caloric intake than higher-protein diets.19,20

Further, in a recent meta-analysis (a high-level statistical analysis of the current body of research) published in the journal Obesity Reviews, a research team from the University of Sydney (including Professor Simpson) found that the amount of protein in the diet was negatively associated with total daily caloric intake. In other words, higher protein diets were associated with lower caloric intake, and lower protein intakes were associated with higher caloric intake, thus strongly supporting the the protein leverage hypothesis in lean, overweight, and obese humans.


One of the factors that may contribute to limiting how quickly the body can digest and absorb protein is saturation of the digestive enzymes responsible for the breakdown of protein (i.e., proteolytic enzymes). You see, the body has a limited number of digestive enzymes—which decline as a result of aging, environmental pollution, stress, processed foods, irradiated foods, not consuming enough raw foods, genetically modified food, and cooking methods—and that means the body can only digest protein at a certain rate.

Let’s take whey protein for example. Under normal circumstances, the maximum rate of absorption of whey protein is 8 – 10 grams per hour.21 Could the addition of proteolytic enzymes (i.e., enzymes that digest proteins) enhance the rate of absorption? That’s a great question, and it’s precisely one that researchers set out to answer in a recent study published in the Journal of the International Society of Sports Nutrition.22

In the study, on two separate occasions, a group of 41 healthy men drank a whey protein shake (containing 42.5 grams of protein)—first without any additional digestive enzymes, and then on a separate day, with the added proteolytic enzymes. The researchers measured the participants blood and urine at various points afterward (30 minutes, 1 hour, 2 hours, 3 hours, 3 ½ hours, and 4 hours) to assess the levels of amino acids (i.e., the building blocks of protein), which represents how much protein has been absorbed (in the blood) and the amount of nitrogen excreted (in the urine).

After drinking the whey protein shake by itself, the participants’ blood levels of amino acids (representing absorption) peaked after 4 hours, about 30% greater than baseline. After the participants drank the whey with added digestive enzymes, their levels of amino acids also peaked at 4 hours, however, in this case, they had increased by as much as 127% relative to baseline.

Over the course of the 4-hour time period, the addition of the protease enzymes led to a 3.5 TIMES greater increase in amino acid absorption.

Screen Shot 2016-06-10 at 9.07.26 AM

Remember that the researchers also measured the amount of nitrogen excreted in the urine as well. This measure is a rough approximation of whether our muscles are in a state of balance (i.e., nitrogen in equals nitrogen out), growth (i.e., positive nitrogen balance), or breakdown (i.e., negative nitrogen balance). The researchers found that when the participants consumed the whey with the addition of proteolytic enzymes, they excreted less nitrogen, indicating a positive nitrogen balance and a more favorable environment for recovery and muscle growth.

This research indicates that protease supplementation significantly increases the rate of absorption of whey protein in liquid form. Thus, the researchers speculate that the rate-limiting step in the digestion process may be saturation of the body’s endogenous proteolytic enzymes.

One of the reasons that I point this out is because BioTrust Low Carb (my personal protein supplement of choice and what I recommend to my clients) contains a patented, research-backed specialized blend of proteolytic enzymes called ProHydrolase®, which has been shown to substantially increase the rate of digestion of the proteins found in BioTrust Low Carb. Based on the findings from the study above, this increased rate of digestion likely means greater blood levels of amino acids (i.e., absorption) and less urinary nitrogen excretion (i.e., positive nitrogen balance).

[Another side benefit of ProHydrolase and enhanced protein digestion is the mitigation of GI discomfort (e.g., nausea, bloating, gas, cramping) associated with inadequate digestion of proteins.]

Researchers from Deerland Enzymes recently assessed the impact that ProHydrolase had on the breakdown of the proteins in BioTrust Low Carb, and the results were nothing short of amazing. Two samples of BioTrust Low Carb were tested for protein breakdown—one sample with ProHydrolase and one without. After just 15 minutes, 20% of the initial protein with ProHydrolase was already digested. After 60 minutes, 96% of the protein had been broken down with the addition of ProHydrolase. The protein samples without ProHydrolase showed little to no breakdown at all time points measured, which is consistent with the rate of digestion described in the study above.



The section above indicates that the body has a certain capacity to digest proteins limited by the amount of endogenous proteolytic enzymes. So, you may be asking yourself whether supplementation with digestive enzymes may be a good idea with other protein-containing meals to maximize protein absorption and utilization. This is a very good question, and while we can’t say for certain, it does seem to be a plausible conclusion.

In general, orally administered digestive enzyme products containing proteases have very few side effects. Issues tend only to arise in cases of hypersensitivity (i.e., allergic reaction) to the source of the enzymes, which may be bovine-, porcine-, or plant-based (e.g., fungal, papaya, pineapple).23

As you already know, the body has a finite number of endogenous proteolytic enzymes for protein digestion. Further compounding that, there are a number of additional factors that can affect the body’s natural digestive enzyme production and supply, including (but not limited to) aging, environmental pollution, stress, processed foods, irradiated foods, not consuming enough raw foods, genetically modified food, and cooking methods.

The notion that we’re born with a finite number of enzymes during our lifetime, stems from research conducted by Dr. Edward Howell, a noted pioneer in the field of enzyme research, who coined the Enzyme Nutrition Axiom, which states:

“The length of life is inversely proportional to the rate of exhaustion of the enzyme potential of an organism. The increased use of food enzymes promotes a decreased rate of exhaustion of the enzyme potential. Another rule can be expressed as follows: Whole foods give good health; enzyme-rich foods provide limitless energy.”24

Thus, age is inversely correlated with enzyme production, as the organs responsible for producing digestive enzymes become less efficient. This is particularly interesting to note because evidence suggests that suggests that older folks tend to be less sensitive to a specific dose of protein. In other words, whereas 20 grams of protein may be sufficient to stimulate muscle protein synthesis in healthy, young folks, it may take significantly more protein (e.g., up to 40 grams) to elicit the same response in older folks.25 While there are likely to be a number of factors in play, some speculate that the body’s supply of proteolytic enzymes (or lack thereof) may play a contributing role.

Further, food choices also affect the body’s ability to produce digestive enzymes. Dr. Howell discusses this at length; in fact, he states, “The increased use of food enzymes [e.g., supplemental enzymes, raw foods] promotes a decreased rate of exhaustion of the enzyme potential.”

For instance, raw, whole foods provide food enzymes, which help promote their digestion. Cooking methods (e.g., heating) destroys food enzymes, and by the same token, processed foods are void of said food enzymes. Certain micronutrients (e.g., magnesium, zinc, iron) are also required for optimal enzyme function. Via dietary displacement, if someone is eating predominantly nutrient-sparse foods, that means s/he is also eating fewer nutrient-dense foods, which contribute these vital nutrients for enzyme production.

Another factor that may affect digestive enzyme supply is stress. Stress initiates the sympathetic branch of the nervous system—the “fight or flight” response—which works in direct opposition with the parasympathetic nervous system, also known as the “rest and digest” branch of the nervous system. The parasympathetic division stimulates digestion whereas the sympathetic branch typically inhibits it.

The digestive system is densely innervated by both branches of the nervous system, and the sympathetic nervous system exerts a predominantly inhibitory effect upon GI muscle and provides a tonic inhibitory influence over mucosal secretion.27 When the parasympathetic branch of the nervous system is activated, digestive enzymes are released; on the other hand, when the sympathetic nervous system is activated saliva production is reduced and many digestive system functions are slowed or stopped.

With all of this in mind, supplementation with a high-quality digestive enzyme product (containing ample proteases) may be a good idea for many folks who are looking to optimize protein absorption.


Take-Home Points

  • There doesn’t appear to be a “magic number” for protein to which we need to limit ourselves on a per meal basis.
  • Factors that seem to be most important are body weight and age. Protein intake can be calculated on a daily (0.72 – 1g per pound of bodyweight), and it’s a good idea to spread this out over 3 – 4 meals (at least 0.18g per pound of body weight).
  • On a per meal basis, muscle protein synthesis (MPS) may be optimized at 0.18g of protein per pound of body weight.
  • However, are numerous metabolic advantages and benefits to consuming a high-protein diet beyond muscle protein synthesis, including improved satiety, increased metabolic rate, and positive dietary displacement (i.e., eating more protein-rich foods means eating less “other stuff”).
  • The body’s ability to digest protein may be limited by its endogenous production and supply of proteolytic enzymes. Choosing a protein supplement with a blend of proteolytic enzymes appears to be an effective solution to increasing protein absorption and augmenting nitrogen balance.
  • There are a number of factors that may impact the body’s supply of digestive enzymes, including age, stress, food choices, whether food is cooked or raw, and environment. Supplementation with digestive enzymes may be a safe, effective strategy to decrease the rate at body’s natural supply is exhausted as well as enhance protein digestion and absorption.



  1. Lennon D. Donald Layman, PhD – Leucine Kinetics, mTOR Activation & the Anabolic Response to Protein. http://sigmanutrition.com/episode123/.
  2. Pasiakos SM. Metabolic Advantages of Higher Protein Diets and Benefits of Dairy Foods on Weight Management, Glycemic Regulation, and Bone: Benefits of higher protein…. J Food Sci. 2015;80(S1):A2-A7. doi:10.1111/1750-3841.12804.
  3. Stote KS, Baer DJ, Spears K, et al. A controlled trial of reduced meal frequency without caloric restriction in healthy, normal-weight, middle-aged adults. Am J Clin Nutr. 2007;85(4):981-988.
  4. Soeters MR, Lammers NM, Dubbelhuis PF, et al. Intermittent fasting does not affect whole-body glucose, lipid, or protein metabolism. Am J Clin Nutr. 2009;90(5):1244-1251. doi:10.3945/ajcn.2008.27327.
  5. Jakobsen LH, Kondrup J, Zellner M, Tetens I, Roth E. Effect of a high protein meat diet on muscle and cognitive functions: a randomised controlled dietary intervention trial in healthy men. Clin Nutr Edinb Scotl. 2011;30(3):303-311. doi:10.1016/j.clnu.2010.12.010.
  6. Arnal MA, Mosoni L, Boirie Y, et al. Protein pulse feeding improves protein retention in elderly women. Am J Clin Nutr. 1999;69(6):1202-1208.
  7. Moore DR, Churchward-Venne TA, Witard O, et al. Protein Ingestion to Stimulate Myofibrillar Protein Synthesis Requires Greater Relative Protein Intakes in Healthy Older Versus Younger Men. J Gerontol A Biol Sci Med Sci. 2015;70(1):57-62. doi:10.1093/gerona/glu103.
  8. Morton RW, McGlory C, Phillips SM. Nutritional interventions to augment resistance training-induced skeletal muscle hypertrophy. Front Physiol. 2015;6. doi:10.3389/fphys.2015.00245.
  9. Cuthbertson D, Smith K, Babraj J, et al. Anabolic signaling deficits underlie amino acid resistance of wasting, aging muscle. FASEB J Off Publ Fed Am Soc Exp Biol. 2005;19(3):422-424. doi:10.1096/fj.04-2640fje.
  10. Symons TB, Sheffield-Moore M, Wolfe RR, Paddon-Jones D. A moderate serving of high-quality protein maximally stimulates skeletal muscle protein synthesis in young and elderly subjects. J Am Diet Assoc. 2009;109(9):1582-1586. doi:10.1016/j.jada.2009.06.369.
  11. Moore DR, Robinson MJ, Fry JL, et al. Ingested protein dose response of muscle and albumin protein synthesis after resistance exercise in young men. Am J Clin Nutr. 2009;89(1):161-168. doi:10.3945/ajcn.2008.26401.
  12. Witard OC, Jackman SR, Breen L, Smith K, Selby A, Tipton KD. Myofibrillar muscle protein synthesis rates subsequent to a meal in response to increasing doses of whey protein at rest and after resistance exercise. Am J Clin Nutr. 2014;99(1):86-95. doi:10.3945/ajcn.112.055517.
  13. Halton TL, Hu FB. The effects of high protein diets on thermogenesis, satiety and weight loss: a critical review. J Am Coll Nutr. 2004;23(5):373-385.
  14. Westerterp-Plantenga MS, Nieuwenhuizen A, Tomé D, Soenen S, Westerterp KR. Dietary Protein, Weight Loss, and Weight Maintenance. Annu Rev Nutr. 2009;29(1):21-41. doi:10.1146/annurev-nutr-080508-141056.
  15. Leidy HJ. Increased dietary protein as a dietary strategy to prevent and/or treat obesity. Mo Med. 2014;111(1):54-58.
  16. Westerterp KR. Diet induced thermogenesis. Nutr Metab. 2004;1(1):5. doi:10.1186/1743-7075-1-5.
  17. Boirie Y, Dangin M, Gachon P, Vasson MP, Maubois JL, Beaufrère B. Slow and fast dietary proteins differently modulate postprandial protein accretion. Proc Natl Acad Sci U S A. 1997;94(26):14930-14935.
  18. Simpson SJ, Raubenheimer D. Obesity: the protein leverage hypothesis. Obes Rev Off J Int Assoc Study Obes. 2005;6(2):133-142. doi:10.1111/j.1467-789X.2005.00178.x.
  19. Gosby AK, Conigrave AD, Lau NS, et al. Testing Protein Leverage in Lean Humans: A Randomised Controlled Experimental Study. Morrison C, ed. PLoS ONE. 2011;6(10):e25929. doi:10.1371/journal.pone.0025929.
  20. Martens EA, Lemmens SG, Westerterp-Plantenga MS. Protein leverage affects energy intake of high-protein diets in humans. Am J Clin Nutr. 2013;97(1):86-93. doi:10.3945/ajcn.112.046540.
  21. Bilsborough S, Mann N. A review of issues of dietary protein intake in humans. Int J Sport Nutr Exerc Metab. 2006;16(2):129-152.
  22. Oben J, Kothari SC, Anderson ML. An open label study to determine the effects of an oral proteolytic enzyme system on whey protein concentrate metabolism in healthy males. J Int Soc Sports Nutr. 2008;5(1):10. doi:10.1186/1550-2783-5-10.
  23. Lorkowski G. Gastrointestinal absorption and biological activities of serine and cysteine proteases of animal and plant origin: review on absorption of serine and cysteine proteases. Int J Physiol Pathophysiol Pharmacol. 2012;4(1):10-27.
  24. Howell E. Enzyme Nutrition. Penguin Group US; 1995. http://lib.myilibrary.com?id=717976. Accessed April 20, 2016.
  25. Breen L, Phillips SM. Nutrient interaction for optimal protein anabolism in resistance exercise: Curr Opin Clin Nutr Metab Care. 2012;15(3):226-232. doi:10.1097/MCO.0b013e3283516850.
  26. Browning KN, Travagli RA. Central nervous system control of gastrointestinal motility and secretion and modulation of gastrointestinal functions. Compr Physiol. 2014;4(4):1339-1368. doi:10.1002/cphy.c130055.


Taking Probiotics with Food

22 Jul

By Tim Skwiat, MEd, CSCS, Pn1

Question: It is frequently recommended that probiotics be taken on an empty stomach. If we take them right before we eat, won’t many of them die by being in the stomach with the food?

Answer: There are a few reasons why it’s recommended to take Pro-X10 with food. First of all, foods typically contain fermentable substrates that can help nourish probiotic organisms as they transit through the GI tract. In addition, many probiotics actually secrete certain enzymes that aid in the digestion of foods. What’s more, the original delivery mode of probiotics was via fermented foods.

In addition, Pro-X10 contains the kiwifruit extract Actazin, which is rich in an enzyme called actinidin that helps support the breakdown and digestion of proteins, including gluten. As a matter of fact, recent research suggests that the actinidin enzyme can enhance the digestion and breakdown of gluten by over 300%. (This further augments the compatibility between Pro-X10 and AbsorbMax, which forms quite the dynamic duo when it comes to digestive health.)

Believe it or not, the fasting pH of the stomach is actually lower (i.e., more acidic) than when a meal is administered. Generally speaking, in the fasted state, the gastric pH (i.e., stomach) is between 0.8 – 2, which on the acidic side. Gastric pH following food intake typically ranges from 4 – 7, which is exponentially less acidic.

Despite popular belief, this is yet another reason to take your probiotics with food. That is, it is a common misconception that the pH of the stomach is less acidic when it is empty; hence, the rationale for taking probiotics on an empty stomach. However, this is a false misconception, which ultimately leads to a greater die-off of the living organisms. Here are some additional references on the topic:

Should probiotics be taken with food or on an empty stomach? (Article)

Should probiotics be taken on an empty or full stomach? (Video)

Of course, all probiotics are not created equally. The probiotics in Pro-X10 are protected by microencapsulation technology that wraps these volatile microorganisms in a lipid layer, which protects them from the harsh environment of the stomach. What’s more, two of the non-microencapsulated strains (e.g., Saccharomyces boulardii and Bacillus subtilis) thrive in an acidic environment. As matter of fact, research investigating this very technology has found that it is 5 times more effective at delivering probiotics to the gut than traditional probiotics.

Clearly, taking probiotics with food, even a relatively small amount, seems like the ideal option. With that in mind, taking your Pro-X10 up to 15 minutes before a meal, during a meal, or up to 30 minutes after a meal would be considered an ideal time frame for administration.

Of course, if you understand the value of probiotics and the significance of gut health and the far-reaching implications of the gut microbiome, then you likely also know how important digestive enzymes are to digestive system function and overall health. Whereas probiotics provide the foundation for GI health, digestive enzymes are the “keys” that unlock food’s potential.

They are charged with the responsibility of breaking down the foods we eat into their constituent nutrients. That is, while we eat foods, the body needs the macro and micronutrients, vitamins, minerals, phytonutrients, etc., that are contained within foods. In the absence of adequate digestive enzymes, food goes undigested. This means missing out on important nutrients, but perhaps more importantly means chronic inflammation, difficulty losing weight, gas, bloating, and more.

With that in mind, the addition of AbsorbMax, a full-spectrum digestive enzyme supplement, may be helpful in optimizing digestive system function and health—and all areas of physiology that it affects. AbsorbMax contains an array of proteases, lipases, and amylases, which serve to fully break down proteins, fats, carbohydrates, respectively.

Even more, AbsorbMax contains specific digestive enzymes that may help with the breakdown of soluble and insoluble fibers found in vegetables, fruits, and other plant-based foods:

  • Alpha-Galactosidase
  • Beta-Glucanase
  • Cellulase
  • Hemicellulase
  • Pectin

These enzymes assist with the breakdown of difficult-to-digest plant-based fibers, also known as non-starch polysaccharides (NSPs), which contain a variety of resistant starches, glycogen, and related polysaccharides. Food preparation, chewing, a healthy population of gut microbes, and you guessed it, supplementation all assist in proper assimilation. It’s when these fibers go completely undigested that the carbohydrates are left to ferment and create undesirable symptoms like gas and other digestive discomfort.

These same digestive enzymes may also help release other nutrients (e.g., polyphenols) that may otherwise remain “trapped” in cell walls. AbsorbMax also contains the phytase enzyme, which helps inactivate phytic acid, often known as an anti-nutrient because of its affinity to bind to minerals (e.g., zinc, iron, etc.) and reduce their absorption.

As Dr. M. Mamadou says, probiotics and digestive enzymes are two partners that are neither to be confused nor separated.

Food Sensitivities, Allergies, and Intolerances

9 Nov

The digestive system, commonly referred to as the GI tract or gut, is an amazing series — that measures an amazing 25 feet in length — of organs charged with the demanding duty of converting the foods we into usable nutrients. Interestingly, it is also known in the science community as “the second brain” because of its vast network and highly influential landscape of the same tissue and chemicals that heavily populate our brains. This in and of itself is a very important topic for future discussion.

If you’ve ever experienced an adverse reaction to eating a meal, such as gas, bloating, stomach pain, diarrhea, congestion, skin, then it’s highly likely that you suffer from some food sensitivity. Food sensitivity is an all-encompassing term that includes food allergies, intolerances, or any other adverse reaction associated to eating a food.

The purpose of this article is to discuss both the differences and similarities between food allergies and intolerances, which are often used interchangeably but incorrectly so. It’s important to highlight the differences because their root causes are unique and the severity can also vary. And, as you’ll see, the treatment for food intolerances can be liberating to both your health and your waistline.

According to the Food Allergy & Anaphylaxis Network (FAAN), a food allergy is an immune response to food that your body views as potentially harmful. Specifically, your body mistakenly identifies a food protein as an allergen and attacks it with an immune response that involves a sudden and rapid release of chemicals. This response can involve your entire body including your skin, respiratory system, GI tract, and cardiovascular system.

The signs and symptoms of a food allergy can be mild to severe and they generally come on very rapidly. It’s extremely important to note that a food allergy can be fatal. Common signs are hives, rashes, itching, swelling, and other skin-related issues. In addition, more severe symptoms include trouble breathing, wheezing, and loss consciousness. Other signs are vomiting, abdominal cramps. and diarrhea.

It is estimated that nearly 15 million Americans suffer from food-related allergies. According to the FAAN, eight foods account for 90% of all food-related allergic reactions:

  • Milk
  • Eggs
  • Peanuts
  • Tree Nuts
  • Wheat
  • Soy
  • Fish
  • Shellfish

Diagnosis for a food allergy can generally be determined via skin prick or blood test, and a history of symptoms. The only treatment for a food allergy is avoidance. That is, the only way to prevent a reaction is to avoid the allergy-causing food.

Unlike food allergies, food intolerances generally do not involve the immune system. Rather, they describe an adverse reaction to a food substance or additive that involves digestion or metabolism. Unlike food allergies, the reactions to food intolerances are generally temporary and very rarely life-threatening.

The most common signs and symptoms of food intolerances include gas, bloating, stomach pain, diarrhea, nausea, headache, migraine, and irritability. As you can see, there is some minor overlap between intolerances and allergies, but there are important distinctions.

The symptoms coming on as a result of food intolerance are generally the result of food irritating your GI tract because your body cannot properly digest it. As a matter of fact, these intolerances often arise from the absence of a specific enzyme needed to fully digest a food. More on this in a minute, but first, here’s a list of common food intolerances:

  • Lactose. Lactose is the sugar found in dairy. Many people lack the enzyme lactase that is needed to specifically break down this nutrient.
  • Gluten. Gluten is a protein found in wheat to which many people are intolerant because of the lack of enzymes to break it down properly. Celiac disease is the most severe form, and it is treated more like an allergy (i.e., gluten avoidance). Less severe cases can be properly treated with the addition of enzymes.
  • Salicylates. Foods like apples, citrus fruits, strawberries, some spices, herbs, nuts, tea, wines, and coffee contain salicylates — also in aspirin —  which have been implicated in food intolerances.
  • Amines. Monosodium glutamate (MSG), nitrates, chocolate, cheese, bananas, avocados, tomatoes, and wine can also cause reactions attributed to their specific amine content.
  • Food colors and additives. These artificial ingredients can cause reactions. In general, it is highly recommended that these ingredients be because of their artificial nature and unknown long-term effects.

So, you know that if you have a food allergy that you have to avoid that specific food like the plague. It’s vital to your life. But, what about food intolerances? You may be wondering just how BIG of an impact these issues can have on your fat-loss success, and how much of a difference effectively alleviating them can make.

Well, in one study conducted at Baylor Medical College, 98% of participants displayed significantly improved body composition and/or scale weight by adhering to one single dietary practice: removing foods from their diet in which they tested positive for intolerances. At the same time, a matched control group who followed a calorie-restricted diet alone actually GAINED weight.

The fortunate reality is that you don’t have to suffer through uncomfortable digestive-related issues or put up with food intolerances affecting your fat loss any longer… and, even better, you DON’T have to follow some cumbersome diet that requires you to eliminate foods to do so.

There’s actually a simple solution that allows you to literally have your cake and eat it, too!

BioTrust AbsorbMax™ is a comprehensive blend of 16 unique digestive enzymes that allow you to fully break down and absorb the nutrients contained in any and every food you eat.

Just take one single capsule at the start of each meal, and you’ll be enjoying:

1.Optimal protein breakdown and absorption from meat to dairy to all veggie sources through a potent blend of 5 powerful enzymes that ensure each protein, regardless of source, is reduced to its fully absorbable peptide and free amino acid forms.

2.Optimal carbohydrate and fiber breakdown and absorption through a total of 10 unique carb and fiber enzymes that make sure you get all the goodness and nutrients from every vegetable, potato, bean, fruit, rice, and sprouted grain you eat.

3.Optimal dietary fat breakdown and absorption through dual action enzymes that cover a broad pH range.

4. A specialized enzyme to fully break down lactose from dairy while at the same time reducing or eliminating the bloating and gas that is regularly associated with these foods.

5. GlutenGone™ – A dynamic duo of 2 unique enzymes that has been shown in very recent research to be unmatched in its ability to fully digest gluten, assisting those with gluten intolerance and avoiding the harmful effects of this damaging protein.

6.Enhanced absorption of health-promoting, age-defying, and disease-fighting vitamins, minerals, phytochemicals, and antioxidants from all foods.

And if that wasn’t enough, AbsorbMax also boasts three other powerful support nutrients that not only help each enzyme do its job, but actually stimulate delivery of nutrients into the cells of the body, and even help avoid the delivery of those nutrients to belly fat stores!

First up is cayenne pepper, a well-known spice whose active compound is an extract called capsaicin. Capsaicin has been shown in research to increase intestinal blood flow by 16%, helping enhance nutrient delivery to the various cells in the body that need them.

But even more interesting is that capsaicin also has been shown in research to decrease blood flow and nutrient delivery to mesenteric adipose tissue (a.k.a. belly fat) by a substantial 12%! In other words, this distinctive ingredient makes AbsorbMax even more special by partitioning the nutrients that our unique enzymes break down away from belly fat and instead toward muscles and other body cells.

The next support ingredient is coral trace minerals. Because all enzymes rely on a variety of mineral co-factors to function properly, we went with none other than the best to enhance the AbsorbMax blend. For starters, coral minerals are all natural (unlike synthetic mineral supplements) and naturally contain the full spectrum of trace minerals so valuable to the human body. Additionally, coral minerals play a more important role in the body than any other supplement, as these important minerals can directly improve the heart and circulatory systems as well as cleanse the digestive system.

Lastly, AbsorbMax is completed with the addition of ginger, a common nutrient that has been shown in multiple research studies to further soothe the intestinal tract, which can be so easily irritated and inflamed.

If a food intolerance is causing you gastrointestinal strife, I strongly recommend looking into AbsorbMax. While an elimination diet is another option, it can be a terribly pain-staking and time-consuming process. If you are indeed concerned about a food allergy, then I strongly recommend further testing.