Acid Lactase- Why Are More and More Lactase Products Switching to "Acid-Resistant" Types?

In recent years, with the growing popularity of lactase, a variety of lactase products with different labeled activities, diverse sources, and various formulations have rapidly flooded the market. From tablets, formulated milk powders, and chewable candies to drops, and from "high-activity" and "fast-acting" to "compound" types, lactase is becoming increasingly familiar and accepted by consumers.

In practical application, many consumers find that even after choosing a lactase product, the experience and effectiveness can still vary significantly.

This variation is not solely due to individual constitution but is closely related to the source and physicochemical properties of the lactase itself. Currently, when labeling their products, many lactase manufacturers focus on presenting the enzyme activity index, while providing relatively limited information about the source of the lactase, its optimal pH range, and its adaptability to the gastric acid environment.

However, for an enzyme preparation that needs to be taken orally and function within the digestive tract, these enzymatic characteristics often directly influence its actual performance in the body.

I. Where Do the Differences Among Lactase from Different Sources Come From?

Currently, commercial lactase mainly comes from three types of microbial systems: filamentous fungi, yeast, and bacteria. Generally, the lactase produced by these three sources exhibits significant differences.

• Lactase from Filamentous Fungi

Represented by the Aspergillus genus, especially Aspergillus oryzae, lactase from filamentous fungi is mostly acidic. A notable characteristic of this type of enzyme is that its optimal reaction pH leans towards the acidic range, allowing it to maintain relatively stable spatial structure and catalytic capability even under low pH conditions. Precisely because of this, lactase derived from filamentous fungi possesses a natural physiological adaptation advantage in application scenarios involving direct oral intake and passage through the gastric environment.

• Lactase from Yeast

Although yeast also belongs to the fungal category, lactase produced by its typical representative—Kluyveromyces spp.—usually has an optimal pH close to neutral. This characteristic makes it very suitable for use in the processing stage of dairy products, such as pre-hydrolysis treatment in milk or dairy beverages. However, in the strongly acidic environment of the human stomach, this type of lactase is more prone to conformational changes or even inactivation, making it unsuitable for relying on it to perform digestive functions within the body.

• Lactase from Bacteria

Lactase from bacterial sources (such as Bacillus subtilis and Lactobacillus delbrueckii subsp. bulgaricus) typically has a high reaction rate, but its stability window is relatively narrow, with an optimal pH mostly in the neutral to weakly alkaline range. Therefore, this type of lactase is more commonly used in industrial, research, or specific fermentation systems, rather than for the complex, strongly acidic, and highly variable gastrointestinal environment.

Due to its acidic nature and gastric acid resistance, Aspergillus-sourced lactase can begin breaking down lactose in the stomach, while also offering high safety and stable production, making it the preferred source for oral lactase supplements. In fact, almost all internationally renowned lactase manufacturers currently use Aspergillus oryzae as their strain, which also confirms its broad recognition in terms of technology and safety.

II. pH Adaptability Is More Important Than Mere "High Activity"

The human stomach is a typically low-pH environment. Under fasting conditions, gastric acid pH can be as low as 1.5. After eating, the stomach pH temporarily rises but remains significantly below neutral.

This means:

• Neutral lactase is highly prone to inactivation in the stomach.

• No matter how high the activity is, if it cannot survive the gastric acid phase, it is difficult to be effective.

• Acidic lactase has better gastric acid tolerance and can begin decomposing lactose within the stomach acid.

If lactose is not broken down in the stomach, it enters the small intestine as a whole. For individuals with lactose intolerance, who have insufficient secretion of their own lactase in the small intestine, the undigested lactose is fermented by gut flora, leading to discomfort such as bloating and diarrhea.

III. Why Acidic Lactase Is Increasingly Becoming the Mainstream

With a deeper understanding of the mechanism of lactose intolerance, the evaluation criteria for lactase are shifting from "how high is the activity" to "whether it can function in the real digestive environment." Compared to neutral lactase, which needs to be added to milk in advance for reaction, acidic lactase has better stability under gastric acid conditions and can complete pre-hydrolysis before lactose enters the small intestine, significantly reducing the subsequent fermentation burden.

This high degree of adaptation to the gastrointestinal environment makes it more reliable and reproducible in practical applications. Precisely for this reason, an increasing number of lactase products are turning to acidic lactase as the solution.

Zancheng Life Sciences: Your Reliable Supplier of High-Quality Acid Lactase

• Powder: 100000ALU/g; 160000ALU/g

• Liquid: 20000ALU/g; 30000ALU/g

• Package: Aluminum foil bag; Drum, etc.

  
  

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