What Is Unique About Bactose?

1. The Science What Is Unique About Bactose? It’s a genetically enhanced bacteria that’s able to colonize the human intestine and actively produce human lactase enzyme (lactose-phlorizin hydrolase or LPH), it’s the same enzyme that people who are Lactose Intolerant are missing, it also happens to be the same enzyme that people take in the pill form for their LI symptoms. This lactose-digesting enzyme is stable and active under the conditions normally found in the human small intestine. This means that with just one 7 day supply, Bactose will continue to work for months like little factories in the gut, digesting the lactose that typically will cause all those uncomfortable and embarrassing symptoms. US AS BABIES & OUR GROWTH INTO ADULTS

2. In infancy, mammals have a high level of lactase activity in the lining of the upper intestinal tract, because they depend on lactose as the primary carbohydrate in their diet of mother’s milk. However, in humans, the lactase expression is diminished by about 90% between ages two and five. This condition is called primary lactase deficiency. Many Northern Europeans, some Western Europeans, some Mediterranean’s, and their descendants carry a mutation that prevents this natural decrease in lactase production. These individuals are able to consume milk as adults. However, large portions of the world population (70% globally), such as Southern Europeans, East Asians, and Sub-Saharan Africans have primary lactase deficiency. Other ways lactose intolerance forms

3. Secondary lactase deficiency results from injury or disease of the Small intestine. For example, celiac disease, inflammatory bowel syndrome (IBS) and Crohn’s disease are often accompanied by lactase deficiency. These diseases affect people in all ethnic groups. WHAT IS LACTOSE AND HOW DOES LACTOSE INTOLERANCE CAUSE ISSUES?

4. Lactose is a disaccharide (a sugar made up of two smaller sugars) the two sugars it is made up of are glucose and galactose they are linked by a beta-D-glycosidic bond. Ideally, lactose is broken down into its individual sugars by the enzyme lactase(an enzyme is a protein that facilitates a chemical reaction in living beings) (beta-Dgalactosidase) in the small intestine by the cells of the intestinal brush border microvilli (very tiny hairs on the walls of the intestine that produce enzymes for digesting carbohydrates, this is where most

5. carbohydrates get digested). Thus these intestinal brush border microvilli breakdown the lactose into glucose and galactose, afterward these two components can be absorbed in the small intestine and provide us with energy. When lactase is absent from the brush border microvilli, usually because we are genetically programmed to reduce producing lactase as toddlers as we move from a diet of milk to one made of other food. Problems arise when there is none or not enough lactase produced and the undigested lactose reach the large intestine. There in the large intestine, the resident bacteria metabolize lactose through fermentation which generates gas. The gas is responsible for symptoms such as pain, pressure, cramps, and flatulence. In addition, the undigested lactose increases osmotic pressure (more water being needed to allow passage of the solution) in the large intestine, causing increased excretion of water which then leads to diarrhea and dehydration. Lactose is hiding in many foods… Secondary lactase deficiency results from injury or disease of the Small intestine. For example, celiac disease, inflammatory bowel syndrome (IBS) and Crohn’s disease are often accompanied by lactase deficiency. These diseases occur in all ethnic groups.

6. WHAT OTHER WAYS CAN SOMEONE BREAKDOWN LACTOSE TO REMEDY THEIR LACTOSE INTOLERANCE? Easiest is to take a lactase enzyme pill. Pros are the convenience and perceived low cost. Cons are that it only lasts a little while, not even 1 hour, and must be taken with every single dairy meal. In addition, many lactase enzyme pills actually contain lactase produced for other types of organisms and they do not function ideally in humans. This is simply a cost and ease of manufacturing issue, where those unscrupulous manufacturers do not care and rather produce a cheaper lactase to get better margins. Lowest price, shortest duration, least convenient. Another option is the most extreme and risky and that is gene therapy. This means people who suffer from lactose intolerance get the cells of their intestine genetically altered to produce lactase. This is a very costly procedure (many thousands of dollars) and the effects do not last more than 12-18 months because the cells of the intestine are constantly

7. splitting and dying. In addition, there is still unknown potential risks involved with gene therapy as it is a new therapy. Most expensive, longest-lasting, highest risk. Then there is our solution… We genetically engineer the lactobacillus acidophilus bacteria that are able to colonize the mammalian intestine and actively produce the human form of lactase enzymes to effectively digest lactose in our small intestine before it reaches the large intestine. The lactose-digesting enzymes are stable and active under the conditions normally found in the human small intestine. HOW DID WE ACCOMPLISH THIS INCREDIBLE FEAT?

8. The bacteria we use, Lactobacillus acidophilus is already found in the intestinal tract of children and adults, as well as in that of other mammals. The gene we use is the one for producing LPH (Lactase-Phlorizin hydrolase), which is what is found in the small intestine of human newborns. The method of gene insertion is by utilizing plasmid vector pRLU61 which can replicate bacteria, then the mRNA sequence of human Lactase phlorizin hydrolase in plasmid pS1234T was constructed by inserting the LPH into the unique EcoRI site of pRLU61.