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Digestive Enzymes
13%
lost enzyme potential every 10 years
nearly 65%
of people worldwide experience lactose intolerance

Basic Food Enzymes
Enzymes are important for the body's proper absorption and utilization of food. Over time, the body's ability to make certain enzymes decreases as part of the normal aging process. Isotonix Digestive Health Formula combines essential enzymes to make digestion less of a chore.

Product Classification

Gluten-Free

Non-GMO

Vegan

Drinkable Supplement
Directions for use

Pour one level capful of powder into the overcap.

Add 2 ounces of water and stir.

Take once daily with meal.
Key Ingredients & Benefits

Lactase
or the sugar lactose in dairy products

Maltase
aids in the digestion of maltose to produce glucose

Sucrase
to break down sucrose to fructose and glucose

Cellulase
helps digest cellulose fibres
Isotonix Delivery System

:05 minutes
Isotonix Liquid Vitamins
- Formulated to survive digestion.
- Delivers concentrated nutrients to the site of absorption.
- Contains no fillers or binders.
- No artificial color or flavors.

:40 minutes
Standard Vitamin Tablet
- Contains lab-created coatings and lubricants.
- Often contains artificial colors, nutrients and flavors.
- Limited absorption of nutrient utilization.
Frequently Asked Questions
What are digestive enzymes?
Digestive enzymes are special catalytic proteins that help our bodies break down food to utilize the complete spectrum of nutrients in the food we eat. Isotonix™ Digestive Health Formula acts to supplement and maximize the activity of the body’s own enzymes in an easy-to-take, pleasant-tasting drink. Isotonix Digestive Health Formula provides additional digestive enzymes for the body in order to maximize the absorption of nutrients from the food we eat.
How do enzymes function in the body?
Enzymes are the workhorses of our cells. They are proteins that catalyze many thousands of biochemical reactions in the body. While most enzymes work inside our cells, digestive enzymes operate outside the cells in the gastrointestinal tract. The start of digestion begins with digestive enzymes secreted by salivary gland cells into our mouths. Cells lining the gastrointestinal tract also contribute enzymes, such as pepsin in the stomach. In addition, digestive enzymes are produced in the pancreas and are emptied into the upper part of the small intestine. These enzymes help to break apart proteins, allowing the body to optimize its effort to digest proteins from plant and animal sources as well as break down starch, lactose, fats and nucleic acids (DNA and RNA). The result is a more complete digestive process, resulting in better nutritional absorption. Isotonix Digestive Health Formula supplies enzymes that are not inactivated by stomach acid. What this means is that the supplemental enzymes mix with and work in concert with the ingested food and begin to work with the body’s own digestive enzymes to release as many of the nutrients as possible.
How do we digest food?
Even before we eat, our body‘s digestive action begins to take place. Simply smelling food activates our salivary glands ("mouth watering"). As the food enters the stomach, the stomach acid and pepsin work together to begin breaking the food down into material the small intestine (where most nutrients are absorbed) can use. Enzymes specific to each of the three nutrient groups are released at this stage, further breaking down the food, and contributing to the digestive and absorption processes. These processes continue into the large intestine until the food’s nutritional content is extracted by the body.
What are the three basic enzymes and the four specialty food enzymes?
There are three basic food enzymes that help us digest our food. Each has a specific function and purpose, and each is necessary for the releasing of nutrients into our bodies. They are protease (which digests proteins), amylase (which digests starch) and lipase (which digests fats). In addition to these basic enzymes, there are also some specialty enzymes including: lactase (for the sugar lactose in dairy products), maltase (for the sugar maltose in foods), sucrase (for table sugar and fruit), and cellulase (which helps us digest cellulose fibres). Each of these enzymes play a significant part in the body’s overall health by promoting better digestion of food and absorption of nutrients.
Scientific Research
- Afonso, C. L., E. R. Tulman, Z. Lu, E. Oma, G. F. Kutish, and D. L. Rock. 1999. The genome of Melanoplus sanguinipes entomopoxvirus. J Virol 73:533-52.
- Anthony H, Collins CE, Davidson G, et al. Pancreatic enzyme replacement therapy in cystic fibrosis: Australian guidelines. J Pediatr—Child Health. 1999; 35:125-129.
- Barrett A.J., Rawlings ND, Woessner JF. The Handbook of Proteolytic Enzymes, 2nd ed. Academic Press, 2003. ISBN 0120796104.
- Billigmann P. [Enzyme therapy—an alternative in treatment of herpes zoster. A controlled study of 192 patients]. [Article in German]. Fortschr Med. 1995; 113:43-48.
- Bock U, Kolac C, Borchard G, et al. Transport of proteolytic enzymes across Caco-2 cell monolayers. Pharm Res. 1998; 15:1393-1400.
- Brady, L., A. M. Brzozowski, Z. S. Derewenda, E. Dodson, G. Dodson, S. Tolley, J. P. Turkenburg, L. Christiansen, B. Huge-Jensen, L. Norskov, and et al. 1990. A serine protease triad forms the catalytic centre of a triacylglycerol lipase. Nature 343:767-70.
- Carriere, F., C. Withers-Martinez, H. van Tilbeurgh, A. Roussel, C. Cambillau, and R. Verger. 1998. Structural basis for the substrate selectivity of pancreatic lipases and some related proteins. Biochim Biophys Acta 1376:417-32.
- Chapin III, F.S., P.A. Matson, H.A. Mooney. Principles of Terrestrial Ecosystem Ecology. Springer-Verlag New York, NY. 2002
- Coenen TMM, Bertens AMC, De Hoog SCM, Verspeek-Rip CM. Safety evaluation of a lactase enzyme preparation derived from Kluyveromyces lactis. Food Chem Toxicol. 2000; 38:671-677.
- de Smet PA, Pegt GW, Meyboom RH. [Acute circulatory shock following administration of the non-regular enzyme preparation Wobe-Mugos]. [Article in Dutch]. Ned Tijdschr Geneeskd. 1991; 135:2341-2344.
- Diaz, B. L., and J. P. Arm. 2003. Phospholipase A(2). Prostaglandins Leukot Essent Fatty Acids 69:87-97.
- Dominguez-Munoz JE, Birckelbach U, Glassbrenner B, et al. Effect of oral pancreatic enzyme administration on digestive function in healthy subjects: comparison between two enzyme preparations. Aliment Pharmacol Ther. 1997; 11:403-408.
- Eckert K, Grabowska E, Stange R, et al. Effects of oral bromelain administration on the impaired immunocytotoxicity of mononuclear cells from mammary tumor patients. Oncol Rep. 1999; 6:1191-1199.
- Egmond, M. R., and C. J. van Bemmel. 1997. Impact of Structural Information on Understanding of Lipolytic Function, p. 119-129, Methods Enzymol vol. 284.
- Farkas G, Takacs T, Baradnay G, Szasz Z. [Effect of pancreatin replacement on pancreatic function in the postoperative period after pancreatic surgery]. [Article in Hungarian]. Orv Hetil. 1999; 140:2751-2754.
- Gilbert B, Rouis M, Griglio S, de Lumley L, Laplaud P. 2001. Lipoprotein lipase (LPL) deficiency: a new patient homozygote for the preponderant mutation Gly188Glu in the human LPL gene and review of reported mutations: 75 % are clustered in exons 5 and 6. Ann Genet 44(1):25-32.
- Girod, A., C. E. Wobus, Z. Zadori, M. Ried, K. Leike, P. Tijssen, J. A. Kleinschmidt, and M. Hallek. 2002. The VP1 capsid protein of adeno-associated virus type 2 is carrying a phospholipase A2 domain required for virus infectivity. J Gen Virol 83:973-8.
- Goni FM, Alonso A. 2002 Sphingomyelinases: enzymology and membrane activity. FEBS Lett. 531(1):38-46.
- Greenberger NJ. Enzymatic therapy in patients with chronic pancreatitis. Gastrenterol Clin North Am. 1999; 28:687-693.
- Hedstrom L. Serine Protease Mechanism and Specificity. Chem Rev 2002;102:4501-4523.
- Heikinheimo, P., A. Goldman, C. Jeffries, and D. L. Ollis. 1999. Of barn owls and bankers: a lush variety of alpha/beta hydrolases. Structure Fold Des 7:R141-6.
- Hooper NM. Proteases in Biology and Medicine. London: Portland Press, 2002. ISBN 1855781476.
- Identification of a variant associated with adult-type hypolactasia. Nat Genet 2002;30: 233-7. Free text. PMID 11788828.
- Kaul R, Mishra BK, Sutrador P, et al. The role of Wobe-Mugos in reducing acute sequelae of radiation in head and neck cancers—a clinical phase-III randomized trial. Indian J Cancer. 1999; 36:141-148.
- Kiessling WR. [Anaphylactic reaction in enzyme therapy of multiple sclerosis]. [Article in German]. Fortschr Neurol Psychiatr. 1987; 55:385-386.
- Klein G, Kullich W. [Reducing pain by oral enzyme therapy in rheumatic diseases]. [Article in German]. Wien Med Wochenschr. 1999; 149:577-580.
- Lowe, M. E. 1992. The catalytic site residues and interfacial binding of human pancreatic lipase. J Biol Chem 267:17069-73.
- Olds LC, Sibley E. Lactase persistence DNA variant enhances lactase promoter activity in vitro: functional role as a cis regulatory element. Hum Mol Genet 2003 Sep 15; 12(18): 2333-40. Free text. PMID 12915462.
- Puente XS, Lopez-Otin C. A Genomic Analysis of Rat Proteases and Protease Inhibitors. Genome Biol 2004;14:609-622.
- Puente XS, Sanchez LM, Overall CM, Lopez-Otin C. Human and Mouse Proteases: a Comparative Genomic Approach. Nat Rev Genet 2003;4:544-558.
- Retrieved from " http://www.lactospore.com/intro.htm"
- Retrieved from "http://en.wikipedia.org/wiki/Lactase"
- Retrieved from "http://en.wikipedia.org/wiki/Lipase"
- Retrieved from "http://en.wikipedia.org/wiki/Sucrase"
- Ross J, Jiang H, Kanost MR, Wang Y. Serine proteases and their homologs in the Drosophila melanogaster genome: an initial analysis of sequence conservation and phylogenetic relationships. Gene 2003;304:117-31.
- Rowan AD, Buttle DJ, Barrett AJ. The cysteine proteinases of the pineapple plant. Biochem J. 1990; 266:869-875.
- Schrag, J. D., and M. Cygler. 1997. Lipases and alpha/beta hydrolase fold. Methods Enzymol 284:85-107.
- Seyis I, Aksoz N. Production of lactase by Trichoderma sp.. Food Technol Biotechnol 2004;42:121–124. Free text.
- Solomon, Eldra P.; Berg, Linda R.; & Martin, Diana W. (2002). Biology (6th ed). Tho
- Spiegel, S., D. Foster, and R. Kolesnick. 1996. Signal transduction through lipid second messengers. Curr Opin Cell Biol 8:159-67.
- Stauder G, Ransberger K, Streichhan P, et al. The use of hydrolytic enzymes as adjuvant therapy in AIDS/ARC/LAS patients. Biomed Pharmacother. 1988; 42:31-34.
- Steffen C, Menzel J. [Enzyme breakdown of immune complexes]. [Article in German]. Z Rheumatol. 1983; 42:249-255.
- Steffen C, Smolen J, Miehlke K, et al. [Enzyme therapy in comparison with immune complex determinations in chronic polyarthritis]. [Article in German]. Z Rheumatol. 1985; 44:51-56.
- Svendsen, A. 2000. Lipase protein engineering. Biochim Biophys Acta 1543:223-238.
- The Merck Manual of Diagnosis and Therapy, Chapter 24
- Tjoelker, L. W., C. Eberhardt, J. Unger, H. L. Trong, G. A. Zimmerman, T. M. McIntyre, D. M. Stafforini, S. M. Prescott, and P. W. Gray. 1995. Plasma platelet-activating factor acetylhydrolase is a secreted phospholipase A2 with a catalytic triad. J Biol Chem 270:25481-7.
- Wald M, Olejár T, Pouková P, Zadinova M. Proteinases reduce metastatic dissemination and increase survival time in C57B16 mice with the Lewis lung carcinoma. Life Sciences. 1998; 63:PL237-243.
- Wald M, Závadová E, Pouková P, et al. Polyenzyme preparation Wobe-Mugos inhibits growth of solid tumors and development of experimental metastases in mice. Life Sciences. 1998; 62:PL43-48.
- Winkler, F. K., A. D'Arcy, and W. Hunziker. 1990. Structure of human pancreatic lipase. Nature 343:771-4.
- Withers-Martinez, C., F. Carriere, R. Verger, D. Bourgeois, and C. Cambillau. 1996. A pancreatic lipase with a phospholipase A1 activity: crystal structure of a chimeric pancreatic lipase-related protein 2 from guinea pig. Structure 4:1363-74.
- Wolf M, Ransberger K. [Effect of proteolytic enzymes on the reciprocal growth modification of normal and tumor tissues]. [Article in German]. Arch Geschwultstforsch. 1968; 31:317-331.
Reviews
Customer Rating
5.0 out of 5 star rating.
(60 reviews)
would recommend this product.
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Customer Images
Taste great! With this small packaging, make so much for convenient for me to carry out with me daily.
Response from Customer Service on 12/15/2024
Dear Valued Customer,
Thank you for taking the time to leave your thoughts on the Isotonix™ Digestive Enzymes Plus Powder. We're glad to hear that you find the packaging convenient for on-the-go use. It's fantastic that the product suits your daily needs.
Thank you.
UnFranchise Services Team
Digestive Enzymes
by Anonymous
on 09/30/2023
easy to drink and nice taste. not like tablet must swallow.
Isotonix Digestive
by JulianeC
Shop Consultant
on 09/12/2023
Can't live without this product. I use it 95% of time.
Response from Customer Service on 09/12/2023
Dear Valued Customer,
Thank you so much for your kind words about the Isotonix Digestive Health Formula! We're so delighted it has been so useful to you. We endeavor to create products that help to make life a bit simpler and it appears like this one does precisely that.
Thank you again!
The Product Information Team
Great after heavy meal!
by SIEW KINT
Shop Consultant
on 06/25/2023
I will take this digestive enzyme after a heavy meal and I find that it aids better digestion and I don't feel my stomach is bloated.
Response from Customer Service on 06/25/2023
Dear Valued Customer,
Thank you for taking the time to leave your thoughts on the Isotonix™ Digestive Enzymes Plus Powder. We are happy to hear you are pleased with the product.
Thank you.
UnFranchise Services Department
best drink with cold water
by KEAT GEORKC
Shop Consultant
on 05/10/2023
I love this enzyme so much, especially when i take outside food, it helps me to decrease my bloating problem.
Response from Customer Service on 05/12/2023
Dear Valued Customer,
Thank you for taking the time to leave your thoughts on the Isotonix™ Digestive Enzymes Plus Powder. We are happy to hear you are pleased with the product.
Thank you.
UnFranchise Services Department
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