Formulated with CereCalase enzyme blend. 90 capsules per bottle

Sometimes your body lacks the enzymes needed for proper digestion. Nu-Zymes™ helps ease your body's digestive burden, lightening the load with all-natural enzymes that work to break down fats, proteins, sugars, carbohydrates, fibers, starches and lactose into small particles. Enzymes also work to release fiber-bound nutrients (nutrients that are "stuck to fiber"), allowing minerals to be more available to your body.

Taken before, after or between meals, this special blend of enzymes can help head off heartburn, bloating and other symptoms of indigestion.

What is different about Nu-Zymes?

Nu-Zymes is specially formulated with our own CereCalase blend, which combines 3 types of enzymes for high-level support of healthy digestion. In addition, NuZymes is economical too, more enzymes per capsule allows you to use fewer capsules per meal, saving you money! There is no corn, wheat, dairy, gluten, soy, sugar, salicylates or casein in Nu-Zymes. Each all-natural capsule is fortified with a unique blend of maylase, protease, lactase, lipase, cellulase, acidophilus and CereCalse™. These plant- and fungi-derived enzymes perform specific functions to help your digestive system.

• Amylase: digests carbohydrates, sugars and starches

• Protease: breaks down proteins in the body

• Lactase: digests the milk sugar lactose

• Lipase: digests fats

• Cellulase: breaks down fibers

• Acidophilus: is a "friendly" bacteria

• CereCalase™: is a special blend of 3 enzymes-phytase, hemicellulase and beta-glucanase

Streamlining fat

While many people believe reducing their fat intake is a healthy choice, this vital nutrient is essential to providing energy, building cell membranes and protecting vital organs and nerve cells. Fat binding supplements may inhibit the intake of fat-soluble vitamins such as A, E, D and K. However, by breaking down fat more effectively with the lipase present in Nu-Zymes™, your body will reap the benefits of its nutritional value. This special enzyme formula helps digest the triglycerides present in fats, thereby supporting your body's use of fat.

Here's what they're saying

"I've tried many, many enzyme products, none of which suggested taking one or two between meals and I'll have to say, I've only been taking these 3-4 days and I am digesting my food much better. I've been fighting digestive problems for years… and I pray you never change this product!" D.T. - Ethridge, MT

These statements have not been evaluated by the FDA. This product is not intended to diagnose, treat, cure or prevent any disease.

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More Information About Digestive Enzymes (referenced from wikipedia.com)

Digestive Enzymes
From Wikipedia, the free encyclopedia


Digestive enzymes are enzymes in the alimentary tract with a purpose of breaking down components of food so that they can be taken up by the organism. The main sites of action are the oral cavity, the stomach, the duodenum and the jejunum. They are secreted by different glands: the salivary glands, the glands in the stomach, the pancreas, and the glands in the small intestines.

Oral Cavity
In the oral cavity, salivary glands secrete ptyalin. It is a type of α-amylase, which digests starch into small segments of multiple sugars and into individual soluble sugars. Secreted by small and large salivary glands.

Salivary glands also secrete lysozyme, which kills bacteria but is not classified as a digestive enzyme.

Stomach
The enzymes that get secreted in the stomach are called gastric enzymes. These are the following:
* Pepsin is the main gastric enzyme. As it breaks proteins into smaller peptide fragments, it is a peptidase.
* Gelatinase, degrades type I and type V gelatin and type IV and V collagen, which are proteoglycans in meat.
* Gastric amylase degrades starch, but is of minor significance.
* Gastric lipase is a tributyrase by its biochemical activity, as it acts almost exclusively on tributyrin, a butter fat.

Acidophilus (Lactobacillus acidophilus)
Acidophilus is a general name for a group of probiotics, often added to milk or sold as a capsule, which contains one or more of the following bacteria which aid in digestion.

Lactobacillus acidophilus is one of several bacteria in the genus Lactobacillus. It is in some countries sometimes used commercially together with Streptococcus salivarius and Lactobacillus delbrueckii ssp. bulgaricus in the production of acidophilus-type yogurt.

Lactobacillus acidophilus gets its name from lacto- meaning milk, -bacillus meaning rod-like in shape, and acidophilus meaning acid-loving. This bacterium thrives in more acidic environments than most related microorganisms (pH 4-5 or lower) and grows best at 45 degrees Celsius. L. acidophilus occurs naturally in the human (and animal) intestine, mouth, and vagina [1]. L. acidophilus ferments lactose into lactic acid, like many (but not all) lactic acid bacteria. Certain related species (known as heterofermentive) also produce ethanol, carbon dioxide, and acetic acid this way. L. acidophilus itself (a homofermentative microorganism) produces only lactic acid. Like many bacteria, L. acidophilus can be killed by excess heat, moisture, or direct sunlight.

Health benefits
Some strains of L. acidophilus may be considered a probiotic or "friendly" bacteria.[1] These types of healthy bacteria inhabit the intestines and vagina and protect against some unhealthy organisms. The breakdown of nutrients by L. acidophilus produces lactic acid, hydrogen peroxide, and other byproducts that make the environment hostile for undesired organisms. L. acidophilus also tends to consume the nutrients many other microorganisms depend on, thus outcompeting possibly harmful bacteria in the digestive tract. During digestion, L. acidophilus also assists in the production of niacin, folic acid, and pyridoxine. L. acidophilus can assist in bile deconjugation, separating amino acids from bile acids, which can then be recycled by the body.

Some research has indicated L. acidophilus may provide additional health benefits, including improved gastrointestinal function, a boosted immune system, and a decrease in the frequency of vaginal yeast infections. Some people report L. acidophilus provides relief from indigestion and diarrhea. A University of Nebraska study found that feed supplemented with L. acidophilus and fed to cattle resulted in a 61% reduction of Escherichia coli 0157:H7. Research has indicated L. acidophilus may be helpful reducing serum cholesterol levels.

L. acidophilus is part of the normal vaginal flora.[5] The acid produced by L. acidophilus in the vagina helps to control the growth of the fungus Candida albicans, helping to prevent vaginal yeast infections. The same beneficial effect has been observed in cases of oral or gastrointestinal Candidiasis infections. Certain spermicides and contraceptive creams can kill L. acidophilus in the vagina, clearing the path to possible yeast infections.

Antibiotics taken orally will also kill beneficial bacteria like L. acidophilus. After a course of antibiotic therapy, patients are occasionally instructed to take an L. acidophilus treatment in order to recolonize the gastrointestinal tract.

L. acidophilus is often sold in health stores in pill or powder form as a nutritional supplement. Research on the nutritional benefits of taking L. acidophilus supplements is inconsistent and inconclusive. Most such claims boil down to a link between L. acidophilus and a possible decrease in the incidence of certain diseases, including yeast infections, gastrointestinal disorders, and a weakened immune system. Most researchers agree further study is needed before substantiating many of these claims.

Amylase
Amylase is the name given to glycoside hydrolase enzymes that break down starch into glucose molecules. Although the amylases are designated by different Greek letters, they all act on α-1,4-glycosidic bonds. Under the original name of diastase, amylase was the first enzyme to be found and isolated (by Anselme Payen in 1833).

Amylase in human physiology
Although found in many tissues, amylase is most prominent in pancreatic juice and urine which each have their own isoform of human α-amylase. They behave differently on isoelectric focusing, and can also be separated in testing by using specific monoclonal antibodies. In humans, all amylase isoforms link to chromosome.

Lipase
water-soluble enzyme that catalyzes the hydrolysis of ester bonds in water–insoluble, lipid substrates.

Lipases are ubiquitous throughout living organisms, and genes encoding lipases are even present in certain viruses.

Function
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)[4], 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.

Myriad other lipase activities exist in nature, especially when the phospholipases and sphingomyelinases are considered.

Structure
While a diverse array of genetically distinct lipase enzymes are found in nature, and represent distinct types of protein folds and catalytic mechanisms, 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.

Location of action
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 signaling and inflammation.

Protease
A protease is any enzyme that conducts proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in the polypeptide chain.

Classification
There are six classes of proteases currently known to science:
* Serine proteases
* Threonine proteases
* Cysteine proteases
* Aspartic acid proteases (e. g., plasmepsin)
* Metalloproteases
* Glutamic acid proteases
The threonine and glutamic acid proteases were not described until 1995 and 2004, respectively. The mechanism used to cleave a peptide bond involves making an amino acid residue that has the cysteine and threonine (peptidases) or a water molecule (aspartic acid, metallo- and glutamic acid peptidases) nucleophilic so that it can attack the peptide carbonyl group. One way to make a nucleophile is by a catalytic triad, where a histidine residue is used to activate serine, cysteine or threonine as a nucleophile.

Occurrence
Proteases occur naturally in all organisms and constitute 1-5% of the gene content. These enzymes are involved in a multitude of physiological reactions from simple digestion of food proteins to highly regulated cascades (e.g., the blood clotting cascade, the complement system, apoptosis pathways, and the invertebrate prophenoloxidase activating cascade). 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; it can be an activation of a function or it can be a signal in a signalling pathway.

Proteases are also a type of exotoxin, which is a virulence factor in bacteria pathogenesis. Bacteria exotoxic proteases destroy extracellular structures. Protease enzymes are also found used extensively in the bread industry in Bread improver.

PROTEASES (proteinases) are large group of ENZYMES - enzymes are the protein molecules which play the role of biocatalysts in the organism, they catalyse the reactions of all metabolic processes. Enzymes are divided into classes, one of which is the class of HYDROLASES - these enzymes catalyse the reaction of hydrolysis of various bonds (peptide bonds, ester bonds etc.) with the participation of a water molecule. PROTEOLYTIC ENZYMES (PROTEASES) belong to the class of HYDROLASES.

Proteases are involved in splitting the peptide bonds which link the amino acid residues (elementar units of PROTEINS). Thus proteins are the SUBSTRATES for proteases. These enzymes "digest" long protein chain to shorter fragments. Some of them can detach the terminal amino acids from the protein chain (EXOPEPTIDASES - like aminopeptidases, carboxipeptidase A), the others "attack" internal peptide bonds of a protein (ENDOPEPTIDASES - like trypsin, chymotrypsin, pepsin, papain, elastase).

Proteases are divided into four major groups according to the character of their active site (catalytic site) and conditions of action: serine proteinases, cysteine (thiol) proteinases, aspartic proteinases and METALLOPROTEINASES. Attachment of a protease to a certain group depends on the structure of catalytic site and the amino acid (as one of the consituents) essential for its activity.

Proteases are everywhere and they are involved in various metabolic processes. Acid proteases secreted into the stomach (such as PEPSIN) and serine proteases present in duodeum (TRYPSIN, CHYMOTRYPSIN), enable us to digest the protein in food, proteases present in blood serum (THROMBIN, PLASMIN, HAGEMAN FACTOR etc.) play important role in blood clotting, as well as lysis of the clots, and the correct action of the immune system. Other proteases are present in leukocytes (ELASTASE, CATHEPSIN G) and play several different roles in metabolic control. Proteases determine the lifetime of other proteins playing important physiological role like hormones, antibodies, or other enzymes - this is one of the fastest "switching on" and "switching off" regulatory mechanisms in the physiology of an organism. By complex cooperative action the proteases may proceed as "cascade" reactions which result in amplification of the organism response to the physiological signal, and make this response very fast.

Inhibitors
The function of peptidases is inhibited by protease inhibitor enzymes. Examples of protease inhibitors are the class of serpins (serine protease or peptidase inhibitors), incorporating alpha 1-antitrypsin. Other serpins are complement 1-inhibitor, antithrombin, alpha 1-antichymotrypsin, plasminogen activator inhibitor 1 (coagulation, fibrinolysis) and the recently discovered neuroserpin.

Natural protease inhibitors include the family of lipocalin proteins, which play a role in cell regulation and differentiation. Lipophilic ligands, attached to lipocalin proteins, have been found to possess tumor protease inhibiting properties. The natural protease inhibitors are not to be confused with the protease inhibitors used in antiretroviral therapy. Some viruses, with HIV among them, depend on proteases in their reproductive cycle. Thus, protease inhibitors are developed as antiviral means.

Degradation
Proteases, being themselves proteins, are known to be cleaved by other protease molecules, sometimes of the same variety. This may be an important method of regulation of peptidase activity.

Lactase
Lactase (LCT), a member of the β-galactosidase family of enzymes, is a glycoside hydrolase 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.

Industrial use
Lactase produced commercially can be extracted both from yeasts such as Kluyveromyces fragilis and Kluyveromyces lactis and from fungi, such as Aspergillus niger and Aspergillus oryzae.[1] Its primary commercial use is to break down lactose in milk to make it suitable for people with lactose intolerance. Lactase is also used in the manufacture of ice cream. Because glucose and galactose are sweeter than lactose, lactase produces a more pleasant taste. Lactose also crystallises at the low temperatures of ice cream; however, its constituent products stay liquid and contribute to a smoother texture. Lactase is used in the conversion of whey into syrup.

Lipase
A lipase is a water-soluble enzyme that catalyzes the hydrolysis of ester bonds in water–insoluble, lipid substrates.

Lipases are ubiquitous throughout living organisms, and genes encoding lipases are even present in certain viruses.

Function
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.

Myriad other lipase activities exist in nature, especially when the phospholipases and sphingomyelinases are considered.

Structure
While a diverse array of genetically distinct lipase enzymes are found in nature, and represent distinct types of protein folds and catalytic mechanisms, 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.

Location of action
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 signaling and inflammation.

References -- Please visit http://en.wikipedia.org/wiki/B_vitamins for full list of references
http://en.wikipedia.org/wiki/Digestive_enzyme http://en.wikipedia.org/wiki/Alpha-Amylase http://en.wikipedia.org/wiki/Lipase http://en.wikipedia.org/wiki/Protease http://en.wikipedia.org/wiki/Lactase http://en.wikipedia.org/wiki/Lipase http://en.wikipedia.org/wiki/Lactobacillus_acidophilus