Gluten-Free - the finished product contains no detectable gluten (<10ppm)

No Detectable GMOs – the finished product contains no detectable transgenic DNA fragment or transgenic proteins

Vegetarian - Isotonix Digestive Enzymes with Probiotics is a vegetarian product

Isotonic-Capable Drinkable Supplements - easy-to-swallow supplements in liquid form are immediately available to the body for absorption

Quality Standards - GMP Operations and Standardised Ingredients

Checked For: Heavy Metals, Microbiological Contaminants, Allergens, Residual Solvents, Purity and Identity

Isotonix - the World's Most Advanced Nutraceuticals
Isotonic, which means “same pressure,” bears the same chemical resemblance of the body’s blood, plasma and tears. All fluids in the body have a certain concentration, referred to as osmotic pressure. The body’s common osmotic pressure, which is isotonic, allows a consistent maintenance of body tissues. In order for a substance to be absorbed and used in the body’s metabolism, it must be transported in an isotonic state.

Isotonix dietary supplements are delivered in an isotonic solution. This means that the body has less work to do in obtaining maximum absorption. The isotonic state of the suspension allows nutrients to pass directly into the small intestine and be rapidly absorbed into the bloodstream. With Isotonix products, little nutritive value is lost, making the absorption of nutrients highly efficient while delivering maximum results.

Amylase
Amylases are enzymes that catalyse the hydrolysis of alpha-1, 4-glycosidic linkages of polysaccharides to yield dextrins, oligosaccharides, maltose and D-glucose. Amylases are derived from animal, fungal and plant sources. Pancreatin contains amylase derived from the pancreas of animals, usually porcine pancreas. Amylase is also derived from barley malt and the fungus Aspergillus oryzae. There are a few different amylases. These enzymes are classified according to the manner in which the glysosidic bond is attacked. Alpha-amylases hydrolyse alpha-1, 4-glycosidic linkages, randomly yielding dextrins, oligosaccharides and monosaccharides. Alpha-amylases are endo-amylases. Exoamylases hydrolyse the alpha-1, 4-glycosidic linkage only from the non-reducing outer polysaccharide chain ends. Exoamylases include beta-amylases and glucoamylases (gamma-amylases, amyloglucosidases). Beta-amylases yield beta-limit dextrins and maltose. Gamma-amylases yield glucose. Amylases are used as digestants. Amylase activity is expressed as Dextrinising Units or DU.

Protease
Proteases (proteinases, peptidases or proteolytic enzymes) are enzymes that break peptide bonds between amino acids in proteins. The process is called proteolytic cleavage, a common mechanism of activation or inactivation of enzymes especially involved in blood coagulation or digestion. They use a molecule of water for this and are thus classified as hydrolases.

Proteases occur naturally in all organisms and constitute one to five percent of the gene content. These enzymes are involved in a multitude of physiological reactions from simple digestion of food proteins to highly regulated cascades. Peptidases can break either specific peptide bonds (limited proteolysis), depending on the amino acid sequence of a protein, or break down a complete peptide to amino acids (unlimited proteolysis). The activity can be a destructive change abolishing a protein's function or digesting it to its principal components, an activation of a function or a signal in a signaling pathway.

Lactase
Lactase (LCT), a member of the β-galactosidase family of enzymes, is involved in the hydrolysis of the disaccharide lactose into constituent galactose and glucose monomers. In humans, lactase is present predominantly along the brush border membrane of the differentiated enterocytes lining the villi of the small intestine.

Lactase is essential for digestive hydrolysis of lactose in milk. Deficiency of the enzyme causes lactose intolerance; most humans become lactose intolerant as adults.

Lipase
A lipase is a water-soluble enzyme that catalyses the hydrolysis of ester bonds in water–insoluble, lipid substrates. Most lipases act at a specific position on the glycerol backbone of a lipid substrate (A1, A2 or A3). In the example of human pancreatic lipase (HPL), which is the main enzyme responsible for breaking down fats in the human digestive system, a lipase acts to convert triglyceride substrates found in oils from food to monoglycerides and free fatty acids. A myriad of other lipase activities exist in nature, especially when the phospholipases and sphingomyelinases are considered.

Lipases are ubiquitous throughout living organisms, and genes encoding lipases are even present in certain viruses. While a diverse array of genetically distinct lipase enzymes are found in nature, most are built on an alpha/beta hydrolase fold and employ a chymotrypsin-like hydrolysis mechanism involving a serine nucleophile, an acid residue (usually aspartic acid) and a histidine.

Some lipases work within the interior spaces of living cells to degrade lipids. In the example of lysosomal lipase, the enzyme is confined within an organelle called the lysosome. Other lipase enzymes, such as pancreatic lipases, are found in the spaces outside of cells and have roles in the metabolism, absorption and transport of lipids throughout the body. As biological membranes are integral to living cells and are largely composed of phospholipids, lipases play important roles in cell biology. Furthermore, lipases are involved in diverse biological processes ranging from routine metabolism of dietary triglycerides to cell signalling and inflammation. Several different types of lipases are found in the human body, including pancreatic lipase, hepatic lipase, lysosomal lipase, gastric lipase, endothelial lipase and as various phospholipases.

Cellulase
Cellulase is an enzyme complex which breaks down cellulose to beta-glucose. It is produced mainly by symbiotic bacteria in the ruminating chambers of herbivores. Aside from ruminants, most animals (including humans) do not produce cellulase in their bodies, and are therefore unable to use most of the energy contained in plant material.

Enzymes that hydrolyse hemicellulose are usually referred to as hemicellulase and are usually classified under cellulase in general. Enzymes that cleave lignin are occasionally classified as cellulase, but this is usually considered erroneous.

Cellulase is an enzyme derived from the fungi Aspergillus niger and Trichoderma longbrachiatum or other sources. Cellulose is an indigestible plant polysaccharide. It is the principal constituent of the cell wall of plants. Cellulase has cellulolytic activity, meaning that it hydrolyses cellulose. Cellulase hydrolyses the beta-D-1, 4-glycosidic bonds of cellulose. Cellulase derived from Trichoderma longbrachiatum is comprised of an enzyme complex consisting of cellulase, a glucosidase, cellobiohydrolase and a glucanase. This complex converts cellulose to beta-dextrins and ultimately to D-glucose. Cellulase is used as a digestive aid, particularly in animals, and for the management of flatulence. The activity of cellulase is expressed in cellulose units or CU.

Cellulase is used for commercial food processing in coffee. It performs hydrolysis of cellulose during drying of beans. Cellulase is used in the fermentation of biomass into bio fuels, although this process is relatively experimental at present. Cellulase is used to address Phytobezoars, a form of cellulose bezoar found in the human stomach.

Sucrase
Sucrase is the enzyme involved in the hydrolysis of sucrose to fructose and glucose. It is secreted by the tips of the villi of the epithelium in the small intestine. Its levels are reduced in response to villi blunting events such as coeliac sprue. Sucrase increases during pregnancy and lactation as villi hypertrophy.

Riboflavin-5-Phosphate (Vitamin B2)
Vitamin B2 is found in liver, dairy products, dark green vegetables and some types of seafood. Vitamin B2 serves as a coenzyme, working with other B vitamins. Vitamin B2 plays a crucial role in turning food into energy as a part of the electron transport chain, driving cellular energy on the micro-level. Vitamin B2 is water-soluble and cannot be stored by the body except in insignificant amounts. It must be replenished daily.

Riboflavin contributes to the normal metabolism of iron in the body, the maintenance of normal red blood cells and the normal function of the nervous system. It contributes to the maintenance of normal skin and mucous membranes, normal vision and contributes to the protection of cell constituents from oxidative stress. Riboflavin contributes to the reduction of tiredness and fatigue and contributes to normal energy metabolism.

Bacillus coagulans - Lactospore®
Bacillus coagulans is a lactic acid bacillus preparation manufactured and distributed by the Sabinsa Corporation. Fermented milks have been a part of the human diet since ancient times. Their efficacy in alleviating gastrointestinal disorders has been exploited in systems of traditional medicine the world over. Lactic acid bacteria, the indigenous microbial flora in fermented milks and natural inhabitants of the human gastrointestinal tract, were thought to be responsible for the longevity of their hosts through their curative and prophylactic actions.

The role of lactic acid bacteria in gastrointestinal microecology has been the subject of extensive research. It is widely believed that these bacteria prevent the growth of putrefactive microorganisms responsible for ill health by competitive inhibition, the generation of a non-conducive acidic environment and/or by the production of bacteriocins. Their metabolites may include B group vitamins.

What are the directions for use for Isotonix Digestive Enzymes?
Directions for use: Pour ½ packet contents into a glass. Add 2 fl. oz./60 ml of water and stir. Each packet contains 2 servings. Maximum benefits occur when taken with or immediately following a meal. Additional servings may be taken if necessary.

What is DigeZyme?
DigeZyme® is a multienzyme complex composed mainly of amylases (starch hydrolysing enzymes), proteases (protein hydrolysing enzymes) and lipases (lipid hydrolysing enzymes). These digestive enzymes collectively support the breakdown of complex macromolecules into energy sources and promote the release of the nutrient content from the foods we eat. The digestive system naturally produces digestive enzymes. DigeZyme supplements the gastrointestinal tract with enzymes to adequately support the body’s ability to digest food. In addition to the amylases, proteases and lipases, DigeZyme contains two additional digestive enzymes including lactase (lactose hydrolysing enzyme) and cellulase (cellulose hydrolysing enzyme).

The enzymes in this complex are of microbial origin (fungal amylase, lipase, lactase, cellulase; and a bacterial neutral protease). The product is, therefore, entirely of non-animal origin.

Why are digestive enzymes important for my health?
Proper digestion is essential for the body to effectively utilise food for use by cells and tissues. Enzymes support the normal breakdown of food into substances that can be used to provide energy to the body. Supplementation with digestive enzymes provides the body with the additional support it needs for proper digestion.

Why is this product great?
Isotonix Digestive Enzymes with Probiotics is more than an occasional digestion aid; it utilises a formula of patented ingredients — including DigeZyme®, an effective probiotic enzyme blend, and Lactospore®, a special probiotics strain — that replenish essential digestive enzymes and probiotics for your health. In addition, Isotonix Digestive Enzymes with Probiotics is formulated using the revolutionary Isotonix delivery system. Our high-quality Isotonix Digestive Enzymes with Probiotics product is a lemon-flavoured, easy-to-take, once-a-day supplement. Also, for those who have difficulty swallowing tablets, Isotonix Digestive Enzymes with Probiotics is the ideal supplement of choice. The packets make it quick and easy to prepare the isotonic solution. Isotonix Digestive Enzymes with Probiotics is vegetarian, naturally flavoured, and also contains no added wheat, soy, yeast, gluten, colouring, salt, preservatives or milk (lactose). For adults, one serving supplies more than 100 mg of key digestive enzymes and 150 million live bacteria. You can’t beat that!

What are digestive enzymes?
Digestive enzymes are special catalytic proteins that help your body break down food to utilise the complete spectrum of nutrients in the food we eat. Unfortunately, food enzymes, which are sensitive to heat, are usually inactivated when food is cooked to serve. This leaves your body with the challenge of trying to break down foods for absorption into your system with no help from the natural enzymes that would otherwise be present in many of the foods we eat. While your body can break down foods with no help, it may put additional strain on your system. Isotonix Digestive Enzymes with Probiotics acts to supplement and maximise the activity of the body’s own enzymes and the "friendly" bacteria our bodies need in an easy-to-take, pleasant-tasting drink.

Our lifestyles and diets are constantly changing. If the last 25 years are any indication, these changes are not usually for the best. Foods that would otherwise offer us their own added enzymes to help our bodies absorb more nutrients are increasingly processed, heated for extended shelf life and stripped of vital elements. The problem is that in making increasing numbers of foods "safe" for ingestion, we are in some cases making foods less healthy for our systems. This means our bodies now need to work harder to absorb the same nutritional content as they may have just a few years ago. Isotonix Digestive Enzymes with Probiotics helps your body replenish all the essential enzymes and "good" bacteria necessary for maximum absorption of nutrients from the food we eat.

What are enzymes?
Enzymes are the workhorses of our cells. They are proteins that catalyse 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 optimise 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 Enzymes with Probiotics supplies natural plant 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.

What are probiotics?
Probiotics are beneficial organisms that promote a healthy intestinal tract environment. Probiotics can help support the body in maintaining proper digestive functions and improving emotional health. Bacillus coagulans bacteria reside mostly in the large intestine and help break down undigested food. These "friendly" bacteria can help the absorption of vitamins and minerals and can actually synthesise some vitamins, such as biotin and vitamin K. In addition, these beneficial bacteria contribute to the breaking down of fibres and undigested starch into simple sugars. These simple sugars then function as fuel for the cells that line the large intestine.

When is the best time to take Isotonix Digestive Enzymes?
It is generally recommended that enzyme supplements be taken at the beginning of or early on in the meal to assure appropriate digestive support, since most food stays in the upper part of the stomach for an hour and a half. However, if the enzymes are not taken before or at the beginning of the meal, they can be supplemented after the meal is started.

What happens when we eat?
Even before we eat, our body‘s digestive action begins to take place. Simply smelling food activates our salivary glands (hence the term "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 basic and specialty enzymes in this product?
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). The specialty enzymes are lactase (for the sugar lactose in dairy products), sucrase (for table sugar and fruit), and cellulase (which helps us digest cellulose fibres).  Each of these enzymes plays a significant part in the body’s overall health by helping to release specific and necessary nutrients into our bodies.

What are the "good" bacteria?
We all know that chlorine in our water supply kills bacteria, making water safe to drink. That’s good, but all bacteria are not harmful. In fact, if it weren’t for "good" bacteria, we would be unable to digest food. Many people, especially women, know the importance of having "good" bacteria in their system, and many actually take supplements like Lactobacillus acidophilus to keep healthy. Isotonix Digestive Enzyme Formula with Probiotics contains probiotic bacteria called Bacillus coagulans, designed to help replenish the "good" bacteria that can be harmed by things like the ingestion of chlorinated water and antibiotics. These "friendly" bacteria help to repopulate the colon, displacing harmful bacteria, and promote an appropriate pH balance.

Are there any allergen warnings for Isotonix Digestive Enzymes?
Isotonix Digestive Enzymes is a vegetarian product and contains no added wheat, soy, yeast, gluten, artificial flavour, starch, salt, preservatives or milk.

• 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, 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. 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. 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.
• Enattah NS, Sahi T, Savilahti E, et al. 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). Thomson Learning, Inc. ISBN 0-03-033503-5
• Southan C. A genomic perspective on human proteases as drug targets. Drug Discov Today 2001;6:681-688.
• 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.
• 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, 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. 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. 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.
• Enattah NS, Sahi T, Savilahti E, et al. 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). Thomson Learning, Inc. ISBN 0-03-033503-5
• Southan C. A genomic perspective on human proteases as drug targets. Drug Discov Today 2001;6:681-688.
• 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.