LactoGlutenZyme is scientifically formulated to eliminate genetically altered glutens from grains, lactose sugars from dairy, casein proteins from dairy and high protein foods in your diet. Here is some of the more detailed information and research supporting the science behind LGZ.

LGZ starts off with a revolutionary and proprietary dipeptidyl peptidase IV and protease enzyme blend. These specially cultivated enzyme blends are important in that they have as a primary function the hydrolysis of gluten. In addition, the powerful enzyme blend effectively hydrolyzes the proteins in dairy products, especially casein and other difficult to digest proteins. Thus, the use of LGZ supports the digestion of the protein in gluten-containing cereal grains like wheat as well as casein-containing milk products. This proprietary enzyme blend works in a unique way to specifically break down proline-containing peptides (casomorphin, gluteomorphin and gliadomorphin). The enzyme blend digests these peptides which are generally resistant to being completely broken down by other enzymes. This assists in normalizing the inflammatory response to gluten and casein peptides thus allowing proteins to be properly broken down and absorbed in their digested state. It is not uncommon for some individuals to experience significant digestive discomfort when they eat foods with these difficult to digest proteins. Further, the presence of gluten or casein is not always evident, particularly in highly processed foods. Gluten and Caseinate often found in such things as salad dressings, cold cuts and numerous other food products. This “hidden” gluten and casein are often found in such things as salad dressings, cold cuts and numerous other food products. This “hidden” gluten and casein can cause the discomfort of gas, bloating, indigestion and pain. LGZ features dipeptidyl peptidases and proteases specific to digestion of gluten and casein. Please look at the Stanford research white paper on the lactoglutenzyme.com website homepage to read about the history of this part of our formula.

Department of Chemical engineering, Stanford University, Stanford, California, United States of America. 2Department of chemistry, Stanford University, Stanford, California, United states of America, 3 Department of Biochemistry, Stanford University, Stanford, California, United States of America, 4 Department of Medicine, Stanford University, Stanford, California, United States of America. Citation; Ehren J, Moron B, Martin E, Bethune MT,Gray GM, et al. (2009) a food-grade Enzyme preparation with Modest gluten Detoxification Properties. PLoS ONE 4(7): e6313. Doi:10.1371/journal.pone.0006313 editor Hany A. El-Shemy, Cairo University, Egypt Published July 21, 2009 Bergkvist, R. “The proteolytic enzymes of Aspergillus oryzae II: properties of the proteolytic enzymes.” Acta Chemie Scandanavia 17: 1541-51 (1963).Bergkvist, R.; Svard, P.O. “Studies on the thrombolytic effect of protease from Aspergillus oryzae.” Acta Physiologie Scandanavia 60: 363-71 (1964).Blonstein, J.L. “Oral enzyme tablets in the treatment of boxing injuries.” The Practitioner 198: 547-8 (1967).Boyne, P.S.; Medhurst, H. “Oral anti-inflammatory enzyme therapy in injuries in professional footballers.” The Practioner 198: 543-6 (1967).Cichoke, A.J. “Systemic Enzyme Therapy.” The American Chiropractic 13: 22-3 (1991)Cleeland, R. Proceedings of the Society of Experimental Biological Medicine 112: 913 (1963).Cooper, N.R.; Ziccardi, R.J. “The nature and reactions of complement enzymes.” In Proteolysis and Physiological Regulation, D.W. Ribbons; K. Brew, eds. (New York: Academic Press, 1976).Deitrick, R.E., MD. “Oral Proteolytic enzymes in the treatment of athletic injuries: a double-blind study.” The Pennsylvania Medical Journal 68(10): 35-7 (1965).Donelly, P.K. et al. “The role of protease in immunoregulation.” British Journal of Surgery 70: 614-22, (1983).Effects of an oral enzyme preparation upon serum proteins associated with injury in man.” Journal of Medicine (1974).Fletcher, A.; Alkjaersig, N.K. “Fibrinolytic and Defibrinating Enzymes” in Enzymes as Drugs, J.S. Holcenberg; J. Roberts, eds. (New York: John Wiley& Sons, 1981).Foster, R.L. The Nature of Enzymology (London: Croom Helm, 1980). Pp 299-306.Gsell, O. Barth-Verlag, Leipsig (1964).Hasselberger, F.X. Uses of Enzymes and Immobilized Enzymes. (Chicago: Nelson-Hall, 1978). Pp 117-131Innerfield, I., MD, et al. “Evaluation of an oral proteolytic enzyme in operation upon the hand.” Surgery, Gynecology & Obstetrics 125: 595-7 (1967).Innerfield, I., MD. “Physiological and clinical effects of buccally given proteases.” JAMA 170: 925-9 (1959).Innerfield, I., MD. Enzymes in Clinical Medicine (New York: McGraw-Hall, 1960).Jelsema, C.L., et al. “Enzymatic Alteration of Cell-SurfaceAntigenicity” in Enzymes as Drugs, J.S. Holcenberg; J. Roberts, eds. (New York: John Wiley & Sons, 1981). Kiessling, H.; Svensson, R. “Influence of an enzyme from Aspergillus oryzae, Protease I, on some components of the fibrinolytic system.” Acta Chemie Scandanavia 24: 569-79 (1970).Morrison, W.L.; Neurath, H. “Proteolytic enzymes of the formed elements of human blood.” Journal of Biological Chemistry 20: 39 (1953).Rathgeber, W.F., “The use of proteolytic enzymes in sporting injuries.” South African Medical Journal 45: 181-3 (1971).Stuteville, O.H., DDS, MD; Wallach, S, DDS. “Trypsin in the treatment of swellings of the head and neck.” American Journal of Surgery 96: 787-91 (1958).Tarayre, J.P.; Lauressergues, H. “Advantages of a combination of proteolytic enzymes, flavonoids and ascorbic acid in comparison with non-steroid anti-inflammatory agents.” Arzneimittel-Forschung (Drug Research) 27(I): 1144-9 (1977).Thornes, R.D. “Unblocking or activation of the cellulase immune mechanism by induced proteolys in patients with cancer. Lancet 2: 382-4, (1974).Ulrich, F. “In vitro generation of splenic suppressor cells by trypsin.” Immunology 46: 369-80, (1982).Vanhove, P., etal. “Action of brinase [A. oryzae protease] on human fibrinogen and plasminogen.” Thrombo Haemostas 42: 571-81 (1979).Vischer, T.L. et al. “In vitro stimulation of lymphocytes by neutral proteinases from human polymorphonuclear leukocyte granules. Journal of Experimentasl Medicine 144: 863-72, (1976).Winsor, T. MD. “Inhibition of the response to thermal injury by oral proteolytic enzyme.” Journal of Clinical Pharmacology 12: 325-30 (1972).Witkin, S.S.; Day, N.K. “Reactions, Regulation and Modulation of the Complement System” in Enzymes as Drugs, J.S. Holcenberg; J. Roberts, eds. (New York: John Wiley& Sons, 1981).Wolf, Max, MD; Ransberger, Karl, PhD. Enzyme Therapy (New York: Vantage Press, 1972). Pp.119-34.Woolf, R.M., MD, et al. “Resolution of an artificially induced hematoma and the influence of a proteolytic enzyme.” The Journal of Trauma 5(4): 491-3 (1965).Young, R.E.S. “Evaluation of oral and parenteral proteolytic enzymes as antiinflammatory agents. Clinical Medicine 2461-5 (Nov 1962).

LGZ utilizes a concentrated Lactase produced by the controlled fermentation of Aspergillus oryzae that digests the most processed forms of lactose in dairy. This special lactase is characterized by its ability to hydrolyze lactose over a wide range of temperatures and pH. Lactase catalyzes the hydrolysis of lactose making it useful for the relief from the discomfort of lactose intolerance. Montalto M, Curigliano V, Santoro L, et al. (2006). "Management and treatment of lactose malabsorption". World J. Gastroenterol. 12 (2): 187--91. PMID 16482616. > He M, Yang Y, Bian L, Cui H (1999). "[Effect of exogenous lactase on the absorption of lactose and its intolerance symptoms]". Wei Sheng Yan Jiu (in Chinese) 28 (5): 309--11. PMID 12712706. > O'Connell S, Walsh G (2006). "Physiochemical characteristics of comercial lactases relevant to their application in the alleviation of lactose intolerance". Appl. Biochem. Biotechnol. 134 (2): 179--91. doi:10. 1385/ABAB:134:2:179. PMID 16943638.

A special blend of patented minerals has research showing it can increase the rate of digestion of processed foods.

A method for facilitating digestion of carbohydrates into simple sugars in warm-blooded animals by maintaining and enhancing digestion and absorption in the mucosal cells of the small intestines. Minerals selected from the group consisting of copper, zinc and manganese are provided in the form of amino acid chelates having a ligand to mineral molar ratio of at least 1:1, a molecular weight of no more than 1500 daltons and a stability constant of between about 106 and 1016 and administered orally. The minerals are taken into the mucosal cells lining the small intestine where they are utilized to facilitate the absorption from the intestinal tract.

All minerals are ISO 9001:2008 certified, cGMP certified, Kosher, Halal, EFSA, CAS registered, hypoallergenic, vegetarian friendly, nutritionally functional, of ultimate glycine:mineral molar ratio, BSE free, Non_GMO, pharmaceutically pure, chemically validated (FTIR finger printed), clinically researched guaranteed and patented.

Patented and stabilized probiotics also are utilized that are research proven to help in the digestion of altered grain and dairy. These probiotics colonize in the gut and create enzymes that aid in the digestion of not only dairy and grain proteins but also the dairy sugar lactose.

Fernandes, C. F.,K. M. Shahani.1989.Lactose intolerance and its modulation with Lactobacilli and other microbial supplements. J. Appl. Nutr. 41:50-64. http://www.nebraskacultures.com/htmls/research/pdf/lactoseintolerance.pdf In a 2010 study published in European Review for Medical and Pharmacological Sciences, for instance, researchers assigned 60 people with lactose intolerance to one of three treatments: lactase supplements, supplements containing Lactobacillus reuteri (a type of probiotic), or a placebo. Study results showed that both lactase supplements and Lactobacillus reuteri were more effective than the placebo in reducing gastrointestinal symptoms brought on by consumption of lactose.

CONCLUSION

Each and every ingredient contained in Lacto-Gluten-Zyme is either patented or has University research showing that they digest or aid in the digestion of genetically altered Glutens, Casein and Lactose. The Highly potent nutrients also are research proven to digest high amounts of protein and processed carbohydrates and fats from food.

Toxic effects are real and those that understand the need to eliminate these altered substances from entering the bloodstream deserve a research proven formula. There is no other formula on the market today that has the research, patents and guarantee like Lacto-Gluten-Zyme. Please check out the other write up on this product and the individual details in regards to Gluten, Casein, Lactose and High protein diets.