Pea Protein A Dairy-Free Option

With age, people often unwittingly fail to ingest sufficient protein in their diets.

Protein is a major building block in our body. It is especially important to help preserve muscle mass.

If you are not already ingesting excess calories, an easy way to ensure against protein insufficiency is a concentrated powder made from high-quality organic peas.

Studies show that older adults may need anywhere from 11% to 250% more protein than adults in general.^1-9

Old or young, protein is essential as a supply of amino acids. These proteins are transformed into functional proteins that take care of almost every physiologic need from cell structure to waste clearance.¹⁰

Sufficient amounts of protein are needed to inhibit sarcopenia—the age-related muscle loss that boosts the risk of frailty, falls, and disability.^11-14

But whey, egg, and soy protein supplements may be off-limits for those who are allergic to dairy, egg, or soy or are lactose intolerant, vegetarian, or vegan.

Researchers have been eager to find a plant-based protein supplement that is nutritious, hypoallergenic, and high in essential amino acids. A new pea protein powder provides low-fat protein with high digestibility—free of dairy, egg, soy, lactose, gluten, and sugar.

This plant-based protein contains muscle-promoting branched-chain amino acids and glutamine that can help avert age-related muscle loss and promote recovery from exercise.

Retaining Muscle Mass While Aging

Aging is associated with a marked reduction in cellular protein synthesis.¹⁵

Muscle strength and function diminishes after 40. That loss—called sarcopenia—accelerates after the age of about 75, even among those who have been physically active throughout their lives.^11,14,16

Since muscles generate much of the mechanical stress required to keep bones healthy, the reduced muscle activity from sarcopenia may increase susceptibility to osteoporosis. A 2016 study suggested there is significant “cross-talking” between muscle and bone cells,¹⁷ potentially setting up a cycle of declining health.

Muscle loss also hikes the risks that follow surgery or traumatic events, because muscles act as a “metabolic reservoir” of amino acids that maintain the protein synthesis required for survival and recovery.^18,19

Fortunately, the use of protein supplements, especially when combined with exercise, has been demonstrated to have an anabolic, or tissue-building, effect on muscle mass among aging adults.^20-22

Daily supplementation with 15 grams of essential amino acids—the building blocks of protein—was found to increase muscle synthesis and lean body mass in older women within three months, “possibly offsetting the debilitating effects of sarcopenia.”²³

Additionally, research has linked a diet low in calories, but rich in high-quality vegetable protein, to reduced cardiovascular-risk profiles in adults of all ages, including LDL-cholesterol and blood pressure.²⁴

And clinical research reveals that older individuals require a higher daily intake of protein than normally recommended for younger persons.^1-9

Aging adults—along with vegans, vegetarians, the lactose-intolerant, those with allergies to dairy, soy, or egg, and people concerned about the GMOs commonly found in soy—now have a high-quality alternative in high-quality protein derived from the pea plant.

Pea-Protein

Pea protein has been shown to exert numerous healthful effects when taken by aging humans.

In 2016, scientists showed that meals high in pea (and bean) protein favorably affected appetite regulation more so than meals high in animal protein, with similar energy and protein content. The legume protein-rich meals resulted in reduced appetite scores, hunger, and prospective consumption, and a greater sensation of postprandial (after-meal) fullness.²⁵

Supplemental pea protein is now available in a proprietary formula that contains no common allergens such as dairy or egg, while delivering:

• Beta-glucan fiber, which supports healthy cholesterol and postprandial blood sugar,^26-30

• Agave inulin and FOS (fructooligosaccharides), prebiotics that support digestive and immune health,^31-33

• Branched-chain amino acids (BCAAs), which promote muscle synthesis,^34,35 and

• Glutamine, which is a key amino acid in a number of metabolic functions.^36-38

While pea protein has BCAA values comparable to those in the “gold standard” protein supplements whey, egg, and casein, it provides significantly higher amounts of arginine, which is essential for nitric oxide synthesis.³⁹

Glutamine: Critical Muscle and Whole-Body Support

Glutamine—the most abundant amino acid in the body, is highly concentrated in the skeletal muscles.^40,41

Research indicates that output levels of human growth hormone increase four-fold after supplementing with glutamine.⁴² Glutamine can also help replenish muscle stores of glycogen after exercise,⁴³ providing a ready fuel source for muscles.

In addition to its effects on exercise, glutamine contributes to a number of key functions, including support for the immune system and prevention of infections and improved gut barrier function.³⁷

During stressful states of illness or injury, glutamine becomes “conditionally essential,” meaning that the body cannot supply an adequate amount and it must be taken in from food or supplements.^37,44 A wealth of evidence indicates that this amino acid can play a key role in treating serious and critical illnesses,^45-48 injuries,⁴⁹ infections,^48,50 and postoperative wound-healing.^37,51,52

Branched-Chain Amino Acids Inhibit Muscle Loss

Abundant in pea protein are the three essential branched-chain amino acids—leucine, isoleucine, and valine—which play an important role in muscle protein synthesis and muscle recovery, damage, and fatigue during and after exercise.^53-58 BCAAs have also been shown to reduce muscle damage, inflammation, and perceived exertion and fatigue during exercise.⁵⁹

BCAAs are transported and metabolized differently than other amino acids. Instead of being broken down in the liver, they enter the bloodstream and are absorbed directly into the skeletal muscle. There, they pass into the mitochondria, which are the cells’ powerhouses.⁶⁰

Human research examining this novel handling of BCAAs in the bloodstream and in skeletal muscle has suggested that BCAAs play a critical role in muscle recovery from fatigue or from intensive physical activity such as resistance training.^53-58 They may also act as performance enhancers.⁶¹

Amino acid mixtures that have been enriched with BCAAs have shown promise for improving the muscle-wasting of sarcopenia in elderly humans, who were demonstrated to gain muscle mass during treatment.⁶² This implies that BCAAs may be effective in other conditions characterized by debilitation and muscle loss.

Complementary Beneficial Nutrients

Agave-derived inulin and fructooligosaccharides (FOS)—both of which are powerful prebiotics—as well as gluten-free oat bran, which contains beneficial beta-glucans, offer added health benefits to pea protein alone.

The long-chain prebiotic inulin, extracted from agave plant fiber, arrives at the colon intact and remains longer, and supports the growth of the beneficial intestinal bacteria, including Lactobacilli and Bifidobacteria.^32,33 Together, inulin and FOS favorably transform the composition of the gut microbiota to maintain digestive health and immunity.^31-33

Animal studies have shown that inulin-based prebiotics may improve ulcerative colitis,⁶³ prevent the initiation of colon cancer,^64,65 lower cholesterol and triglycerides,⁶⁶ and support calcium absorption for better bone health.⁶⁷

Oat bran is a source of the soluble fiber beta-glucans, which has been shown to promote a healthy postprandial glycemic response³⁰ and significantly reduce plasma cholesterol levels.²⁶

Pea protein delivers essential nutrients to help protect against muscle-wasting, it also protects against a wide array of diseases.

Pea Protein Validated in Human Studies

Published research shows that—well beyond protecting against sarcopenia—pea protein promotes beneficial effects including:

• Weight Loss: Pea protein was demonstrated in a clinical study to induce a feeling of fullness or satiety,²⁵ and in an animal study to significantly lower the hunger hormone ghrelin.⁶⁸ Both of these effects would reduce food intake. As a result, pea protein may help with weight-loss. Many people neglect protein when dieting. This is regrettable because of pea protein’s satiety and hormonal effects that can help the body burn fat faster.

• Healthier Heart: Pea protein decreases blood pressure.⁶⁹ In addition, a group of researchers found that, compared to a low-carbohydrate diet based on animal sources, a vegetable-based low-carbohydrate diet is associated with lower all-cause and cardiovascular disease rates.⁷⁰

• Lower Blood Sugar: Blood glucose levels may be reduced after consumption of a combination of pea protein and fiber, which suggests the potential for enhanced glycemic control. A 2014 study found that adding pea protein and fiber to a meal results in a blood sugar level that is lower at 30 minutes, compared to a control meal. The study author concluded that, “This trial supports the use of pea components as value-added ingredients in foods designed to improve glycemic control.”⁷¹

Sugar-free pea protein is the ideal alternative for those who are unable to take dairy-based, egg, or soy-protein supplements but wish to prevent sarcopenia and other age-related conditions.

Summary

Studies show that older individuals may need more protein than adults in general, especially if they want to prevent sarcopenia, the age-related loss of muscle tissue that increases the risk of frailty and disability.

The good news for vegans and those with food intolerances is that a new 100% organic pea protein supplement provides a nutrient-dense, low-fat protein that is high in essential amino acids, with excellent digestibility—free of dairy, egg, soy, lactose, gluten, and sugar.

Those already over-consuming protein calories should not take pea or other bulk protein supplements as they may accelerate certain aging processes.

If you have any questions on the scientific content of this article, please call a Life Extension® Wellness Specialist at 1-866-864-3027.

References

1. Gaffney-Stomberg E, Insogna KL, Rodriguez NR, et al. Increasing dietary protein requirements in elderly people for optimal muscle and bone health. J Am Geriatr Soc. 2009;57(6):1073-9.
2. Morais JA, Chevalier S, Gougeon R. Protein turnover and requirements in the healthy and frail elderly. J Nutr Health Aging. 2006;10(4):272-83.
3. Morse MH, Haub MD, Evans WJ, et al. Protein requirement of elderly women: nitrogen balance responses to three levels of protein intake. J Gerontol A Biol Sci Med Sci. 2001;56(11):M724-30.
4. Campbell WW, Crim MC, Dallal GE, et al. Increased protein requirements in elderly people: new data and retrospective reassessments. Am J Clin Nutr. 1994;60(4):501-9.
5. Houston DK, Nicklas BJ, Ding J, et al. Dietary protein intake is associated with lean mass change in older, community-dwelling adults: the Health, Aging, and Body Composition (Health ABC) Study. Am J Clin Nutr. 2008;87(1):150-5.
6. Karakelides H, Nair KS. Sarcopenia of aging and its metabolic impact. Curr Top Dev Biol. 2005;68:123-48.
7. Young VR. Amino acids and proteins in relation to the nutrition of elderly people. Age Ageing. 1990;19(4):S10-24.
8. Courtney-Martin G, Ball RO, Pencharz PB, et al. Protein Requirements during Aging. Nutrients. 2016;8(8).
9. Baum JI, Kim IY, Wolfe RR. Protein Consumption and the Elderly: What Is the Optimal Level of Intake? Nutrients. 2016;8(6).
10. Available at: https://www.nature.com/scitable/topicpage/protein-function-14123348. Accessed August 25, 2017.
11. Paddon-Jones D, Short KR, Campbell WW, et al. Role of dietary protein in the sarcopenia of aging. Am J Clin Nutr. 2008;87(5):1562s-6s.
12. Doherty TJ. Invited review: Aging and sarcopenia. J Appl Physiol (1985). 2003;95(4):1717-27.
13. Beasley JM, Shikany JM, Thomson CA. The role of dietary protein intake in the prevention of sarcopenia of aging. Nutr Clin Pract. 2013;28(6):684-90.
14. Beaudart C, McCloskey E, Bruyere O, et al. Sarcopenia in daily practice: assessment and management. BMC Geriatr. 2016;16(1):170.
15. Rattan SI. Synthesis, modifications, and turnover of proteins during aging. Exp Gerontol. 1996;31(1-2):33-47.
16. Waters DL, Baumgartner RN, Garry PJ. Sarcopenia: current perspectives. J Nutr Health Aging. 2000;4(3):133-9.
17. Reginster JY, Beaudart C, Buckinx F, et al. Osteoporosis and sarcopenia: two diseases or one? Curr Opin Clin Nutr Metab Care. 2016;19(1):31-6.
18. Wolfe RR. The underappreciated role of muscle in health and disease. Am J Clin Nutr. 2006;84(3):475-82.
19. Argiles JM, Campos N, Lopez-Pedrosa JM, et al. Skeletal Muscle Regulates Metabolism via Interorgan Crosstalk: Roles in Health and Disease. J Am Med Dir Assoc. 2016;17(9):789-96.
20. Baum JI, Wolfe RR. The Link between Dietary Protein Intake, Skeletal Muscle Function and Health in Older Adults. Healthcare (Basel). 2015;3(3):529-43.
21. Tieland M, Dirks ML, van der Zwaluw N, et al. Protein supplementation increases muscle mass gain during prolonged resistance-type exercise training in frail elderly people: a randomized, double-blind, placebo-controlled trial. J Am Med Dir Assoc. 2012;13(8):713-9.
22. Lancha AH, Jr., Zanella R, Jr., Tanabe SG, et al. Dietary protein supplementation in the elderly for limiting muscle mass loss. Amino Acids. 2017;49(1):33-47.
23. Dillon EL, Sheffield-Moore M, Paddon-Jones D, et al. Amino acid supplementation increases lean body mass, basal muscle protein synthesis, and insulin-like growth factor-I expression in older women. J Clin Endocrinol Metab. 2009;94(5):1630-7.
24. Jenkins DJ, Wong JM, Kendall CW, et al. The effect of a plant-based low-carbohydrate (“Eco-Atkins”) diet on body weight and blood lipid concentrations in hyperlipidemic subjects. Arch Intern Med. 2009;169(11):1046-54.
25. Kristensen MD, Bendsen NT, Christensen SM, et al. Meals based on vegetable protein sources (beans and peas) are more satiating than meals based on animal protein sources (veal and pork) - a randomized cross-over meal test study. Food Nutr Res. 2016;60:32634.
26. Queenan KM, Stewart ML, Smith KN, et al. Concentrated oat beta-glucan, a fermentable fiber, lowers serum cholesterol in hypercholesterolemic adults in a randomized controlled trial. Nutr J. 2007;6:6.
27. Vachon C, Jones JD, Wood PJ, et al. Concentration effect of soluble dietary fibers on postprandial glucose and insulin in the rat. Can J Physiol Pharmacol. 1988;66(6):801-6.
28. Rondanelli M, Opizzi A, Monteferrario F. [The biological activity of beta-glucans]. Minerva Med. 2009;100(3):237-45.
29. Braaten JT, Wood PJ, Scott FW, et al. Oat gum lowers glucose and insulin after an oral glucose load. Am J Clin Nutr. 1991;53(6):1425-30.
30. Biorklund M, van Rees A, Mensink RP, et al. Changes in serum lipids and postprandial glucose and insulin concentrations after consumption of beverages with beta-glucans from oats or barley: a randomised dose-controlled trial. Eur J Clin Nutr. 2005;59(11):1272-81.
31. Franco-Robles E, Lopez MG. Implication of fructans in health: immunomodulatory and antioxidant mechanisms. ScientificWorldJournal. 2015;2015:289267.
32. Wilson B, Whelan K. Prebiotic inulin-type fructans and galacto-oligosaccharides: definition, specificity, function, and application in gastrointestinal disorders. J Gastroenterol Hepatol. 2017;32 Suppl 1:64-8.
33. Corzo N, Alonso JL, Azpiroz F, et al. [Prebiotics: concept, properties and beneficial effects]. Nutr Hosp. 2015;31 Suppl 1:99-118.
34. Koopman R, Verdijk L, Manders RJ, et al. Co-ingestion of protein and leucine stimulates muscle protein synthesis rates to the same extent in young and elderly lean men. Am J Clin Nutr. 2006;84(3):623-32.
35. Katsanos CS, Kobayashi H, Sheffield-Moore M, et al. A high proportion of leucine is required for optimal stimulation of the rate of muscle protein synthesis by essential amino acids in the elderly. Am J Physiol Endocrinol Metab. 2006;291(2):E381-7.
36. Newsholme P, Curi R, Pithon Curi TC, et al. Glutamine metabolism by lymphocytes, macrophages, and neutrophils: its importance in health and disease. J Nutr Biochem. 1999;10(6):316-24.
37. L-glutamine. Altern Med Rev. 2001;6(4):406-10.
38. Lee WJ, Hawkins RA, Vina JR, et al. Glutamine transport by the blood-brain barrier: a possible mechanism for nitrogen removal. Am J Physiol. 1998;274(4 Pt 1):C1101-7.
39. Tapiero H, Mathe G, Couvreur P, et al. I. Arginine. Biomed Pharmacother. 2002;56(9):439-45.
40. Walsh NP, Blannin AK, Robson PJ, et al. Glutamine, exercise and immune function. Links and possible mechanisms. Sports Med. 1998;26(3):177-91.
41. D’Souza R, Powell-Tuck J. Glutamine supplements in the critically ill. J R Soc Med. 2004;97(9):425-7.
42. Welbourne TC. Increased plasma bicarbonate and growth hormone after an oral glutamine load. Am J Clin Nutr. 1995;61(5):1058-61.
43. Gleeson M. Dosing and efficacy of glutamine supplementation in human exercise and sport training. J Nutr. 2008;138(10):2045s-9s.
44. Lacey JM, Wilmore DW. Is glutamine a conditionally essential amino acid? Nutr Rev. 1990;48(8):297-309.
45. Avenell A. Hot topics in parenteral nutrition. Current evidence and ongoing trials on the use of glutamine in critically-ill patients and patients undergoing surgery. Proc Nutr Soc. 2009;68(3):261-8.
46. Novak F, Heyland DK, Avenell A, et al. Glutamine supplementation in serious illness: a systematic review of the evidence. Crit Care Med. 2002;30(9):2022-9.
47. Kelly D, Wischmeyer PE. Role of L-glutamine in critical illness: new insights. Curr Opin Clin Nutr Metab Care. 2003;6(2):217-22.
48. Tao KM, Li XQ, Yang LQ, et al. Glutamine supplementation for critically ill adults. Cochrane Database Syst Rev. 2014(9):Cd010050.
49. Wilmore DW. The effect of glutamine supplementation in patients following elective surgery and accidental injury. J Nutr. 2001;131(9 Suppl):2543S-9S; discussion 50S-1S.
50. Wischmeyer PE, Dhaliwal R, McCall M, et al. Parenteral glutamine supplementation in critical illness: a systematic review. Crit Care. 2014;18(2):R76.
51. Fan YP, Yu JC, Kang WM, et al. Effects of glutamine supplementation on patients undergoing abdominal surgery. Chin Med Sci J. 2009;24(1):55-9.
52. Sandini M, Nespoli L, Oldani M, et al. Effect of glutamine dipeptide supplementation on primary outcomes for elective major surgery: systematic review and meta-analysis. Nutrients. 2015;7(1):481-99.
53. Blomstrand E, Eliasson J, Karlsson HK, et al. Branched-chain amino acids activate key enzymes in protein synthesis after physical exercise. J Nutr. 2006;136(1 Suppl):269s-73s.
54. Greer BK, Woodard JL, White JP, et al. Branched-chain amino acid supplementation and indicators of muscle damage after endurance exercise. Int J Sport Nutr Exerc Metab. 2007;17(6):595-607.
55. Gualano AB, Bozza T, Lopes De Campos P, et al. Branched-chain amino acids supplementation enhances exercise capacity and lipid oxidation during endurance exercise after muscle glycogen depletion. J Sports Med Phys Fitness. 2011;51(1):82-8.
56. Shimomura Y, Yamamoto Y, Bajotto G, et al. Nutraceutical effects of branched-chain amino acids on skeletal muscle. J Nutr. 2006;136(2):529s-32s.
57. Jackman SR, Witard OC, Philp A, et al. Branched-Chain Amino Acid Ingestion Stimulates Muscle Myofibrillar Protein Synthesis following Resistance Exercise in Humans. Front Physiol. 2017;8:390.
58. Bajotto G, Sato Y, Kitaura Y, et al. Effect of branched-chain amino acid supplementation during unloading on regulatory components of protein synthesis in atrophied soleus muscles. Eur J Appl Physiol. 2011;111(8):1815-28.
59. Matsumoto K, Koba T, Hamada K, et al. Branched-chain amino acid supplementation attenuates muscle soreness, muscle damage and inflammation during an intensive training program. J Sports Med Phys Fitness. 2009;49(4):424-31.
60. Cole JT. Metabolism of BCAAs. In: Rajendram R, Preedy VR, Patel VB, eds. Branched Chain Amino Acids in Clinical Nutrition: Volume 1. New York, NY: Springer New York; 2015:13-24.
61. Kreider RB, Wilborn CD, Taylor L, et al. ISSN exercise & sport nutrition review: research & recommendations. J Int Soc Sports Nutr. 2010;7:7.
62. Solerte SB, Gazzaruso C, Bonacasa R, et al. Nutritional supplements with oral amino acid mixtures increases whole-body lean mass and insulin sensitivity in elderly subjects with sarcopenia. Am J Cardiol. 2008;101(11a):69e-77e.
63. Guarner F. Inulin and oligofructose: impact on intestinal diseases and disorders. Br J Nutr. 2005;93 Suppl 1:S61-5.
64. Femia AP, Luceri C, Dolara P, et al. Antitumorigenic activity of the prebiotic inulin enriched with oligofructose in combination with the probiotics Lactobacillus rhamnosus and Bifidobacterium lactis on azoxymethane-induced colon carcinogenesis in rats. Carcinogenesis. 2002;23(11):1953-60.
65. Verghese M, Rao DR, Chawan CB, et al. Dietary inulin suppresses azoxymethane-induced preneoplastic aberrant crypt foci in mature Fisher 344 rats. J Nutr. 2002;132(9):2804-8.
66. Rault-Nania MH, Gueux E, Demougeot C, et al. Inulin attenuates atherosclerosis in apolipoprotein E-deficient mice. Br J Nutr. 2006;96(5):840-4.
67. Nzeusseu A, Dienst D, Haufroid V, et al. Inulin and fructo-oligosaccharides differ in their ability to enhance the density of cancellous and cortical bone in the axial and peripheral skeleton of growing rats. Bone. 2006;38(3):394-9.
68. Overduin J, Guerin-Deremaux L, Wils D, et al. NUTRALYS((R)) pea protein: characterization of in vitro gastric digestion and in vivo gastrointestinal peptide responses relevant to satiety. Food Nutr Res. 2015;59:25622.
69. Li H, Prairie N, Udenigwe CC, et al. Blood pressure lowering effect of a pea protein hydrolysate in hypertensive rats and humans. J Agric Food Chem. 2011;59(18):9854-60.
70. Fung TT, van Dam RM, Hankinson SE, et al. Low-carbohydrate diets and all-cause and cause-specific mortality: two cohort studies. Ann Intern Med. 2010;153(5):289-98.
71. Mollard RC, Luhovyy BL, Smith C, et al. Acute effects of pea protein and hull fibre alone and combined on blood glucose, appetite, and food intake in healthy young men--a randomized crossover trial. Appl Physiol Nutr Metab. 2014;39(12):1360-5.