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Novel Method to Mitigate Lactose Intolerance

November 2013

By William Lancaster

Standard Treatment of Lactose Intolerance

Most people with lactose intolerance—formally diagnosed or not—are told to “avoid dairy products.” In many cases, that’s as specific of a “treatment” as they receive.

The alternative is to replace the missing lactase enzyme, either by mixing it with milk ahead of time, or by taking a supplement containing the enzyme right before consuming milk.18

Commercial products have been available for decades that contain a form of lactase that can be taken orally before milk consumption.

But these products, derived from molds in the genus Aspergillus, are stable only at the highly acid pH of the stomach.19

The result is that standard lactase supplements have a very brief window of time during which they can attack the lactose load contained in a milk-containing meal or drink.5 After that, they are not effective.

The average time for that stomach exposure is limited to roughly 15 to 45 minutes, which may not be sufficient time for the entire lactose load to be broken down for absorption.3 Scientists have, therefore, been seeking an alternative approach, one that would allow active lactase enzymes to reach the small intestine—its normal site of action—along with the load of lactose from the stomach.

That would permit much longer contact between the lactose load and the lactase enzyme, allowing more complete digestion of lactose in a more natural and appropriate setting.4,13

Fortunately, just such an enzyme has finally been developed and packaged in a form that can survive the acid environment of the stomach.

FIGURE 4: Neutral Lactase In Action
FIGURE 4: Neutral Lactase In Action

Naturally acquired lactase deficiency can be treated by supplying sufficient neutral lactase to the small intestine, the site of its normal action. This restores the small intestine’s ability to break down lactose into glucose and galactose, which are absorbed. Just as in the normal situation (Figure 2), no intact lactose reaches the bacteria in the large intestine, and no symptoms result.4

New Neutral Lactase Works in the Small Intestine!

Neutral lactase is a novel form of the lactase enzyme that was developed and tested in Europe. It is derived not from the molds in the Aspergillus genus but from a simple yeast commonly used to make cheese, Kluyveromyces lactis.3

Unlike the mold-derived enzyme, which is active only at the acid pH of the stomach, K. lactis-derived lactose is active at the nearly neutral pH of the small intestine.19,20

That range of activity gives neutral lactase a much longer amount of time to work on ingested lactose, so more of that lactose can be broken down and absorbed.13 Neutral lactase, derived from yeast, has been shown to be more effective than mold-derived lactase at digesting lactose in milk.13

This has been evidenced by the significant decrease in the excretion of hydrogen in the breath to near-normal levels, and by the suppression of symptoms when added to milk before consumption.18,21-23

Neutral lactase has passed stringent safety testing, and no safety concerns have been identified.24 It has a long history of use in the food industry to rid milk products of lactose.19,24,25

Lactose Intolerance or Milk Allergy?

There’s a world of difference between the very common condition of lactose intolerance and the much rarer, and more dangerous, true allergy to milk.

Lactose intolerance is caused by low levels of the enzyme lactase that your body uses to break down lactose (milk sugar).3,4 While it can produce many distressing and uncomfortable signals, lactose intolerance is not a true allergy because it does not result in the body developing an antibody-mediated immune reaction.

True milk allergy, on the other hand, involves a potent immune reaction to specific proteins in milk.27 It causes an elevation in various markers of inflammation and heightened immunity. Though rare, some life-threatening allergic reactions to milk proteins have been reported.27 Lactose intolerance causes symptoms of bloating, flatulence, abdominal pain, and watery diarrhea.13 Milk protein allergy generally afflicts children and produces symptoms more commonly associated with allergic reactions, including itching, rash, and wheezing.27

Lactose intolerance is common, but a true milk allergy is rare in adults.27 While neutral lactase has been shown to be effective in decreasing the symptoms of lactose intolerance,3 it will have no effect on milk allergy.

Originally, the major barrier to the use of neutral lactase was the highly acidic, protein-digesting environment of the stomach. Unprotected, neutral lactase would simply be digested itself in the stomach, leaving no activity for the small intestine.

But scientists in Europe have developed a means of protecting neutral lactase by incorporating it into tiny acid-resistant pellets.4

The pellets are packaged in a vegetarian capsule that dissolves in the stomach within minutes of swallowing. Once released in the stomach, the pellets are transferred—without digestion—into the small intestine.3 There, the acid-resistant covering of the pellet is dissolved, releasing 100% of the enzyme for breakdown of lactose, working in the small intestine—just like your body’s own natural lactase enzyme.4

The result?

As shown in Figure 4, the complete digestion of lactose occurs within the small intestine, as neutral lactase immediately releases its glucose and galactose components for rapid absorption. This leaves no intact lactose to pass into the large intestine and trigger the painful and often embarrassing symptoms of lactose intolerance.

A human study of the new formulation showed it to be easily acceptable to patients, and highly effective.3 Among 64 individuals with lactose intolerance, scientists observed that 58% had reduction in abdominal pain, 75% had reduced bloating, 67% had less diarrhea, and nausea was reduced in 58% of subjects.3

The results of a laboratory study graphically demonstrate the difference in performance between traditional acid lactase and the new acid-stable, neutral lactase. You can see the difference for yourself in Figure 5, which illustrates the short duration of action of the acid lactase in the stomach, compared with the much longer period of time the neutral lactase has to work in the small intestine.4

What You Need to Know
FIGURE 2: Normal Absorption of Glucose and Galactose

Next Generation Support for Lactose-Induced Digestive Disturbance

  • Lactose intolerance—the inability to digest milk sugar—afflicts more than 50 million Americans with gas, cramps, bloating, and diarrhea following ingestion of milk products. Its cause is the loss of the lactase enzyme, responsible for breaking down lactose for absorption in the intestine.
  • Standard treatment for lactose intolerance includes either avoidance of milk products—which raises the risk of serious nutritional deficiencies—or supplementation with a short-acting lactase enzyme derived from molds.
  • Mold-derived lactase works only in the stomach, limiting the amount of time the enzyme has to work on ingested lactose.
  • Neutral lactase, derived from a common yeast, can work in the small intestine—the natural site of lactase activity—resulting in a large increase in the amount of time available for the lactase to digest lactose and help prevent symptoms.
  • Neutral lactase is manufactured in a novel, acid-resistant form that rapidly passes through the stomach to deliver the active enzyme to the small intestine, the natural site of lactose metabolism.
  • Studies show that neutral lactase is more effective than mold-derived acid lactase at reducing signs and symptoms of lactose intolerance.