Necessity of adding protease in feed

Necessity of adding protease in feed

Improving the protein digestion and utilization rate of feed can promote the full utilization of other nutrients, thereby improving the growth performance of livestock and poultry and reducing environmental pollution. pepsin, trypsin and chymotrypsin are the most important endogenous proteases in animals, and the digestion efficiency of feed protein is about 80 %. Therefore, the addition of exogenous proteases can play a supplementary role and further improve the digestion rate of protein. In addition to the contribution to protein nutrition, proteases can also help to release other nutrients ( such as starch, fat and minerals ) and degrade protein-based anti-nutritional factors and antigens ( such as plant lectins, co-soybean globulin and trypsin inhibitor ). Inhibiting the unnecessary energy-consuming immune response induced by the above antigens and reducing the nutrient levels not digested by animals. Moreover, by increasing protein digestibility, proteases can also reduce the protein content reaching the posterior segment of the gastrointestinal tract ( GIT ), thereby reducing the fermentation substrate of harmful microorganisms.

Characteristics and shortcomings of pepsin :

The first protease to hydrolyze feed protein in gastrointestinal tract ( also known as digestive tract ) is pepsin. pepsin is secreted by the stomach ( pig ) or glandular stomach ( poultry ). It belongs to acidic protease, which is activated and shows activity below pH 5.0 after secretion, and has the highest activity in low pH environment. pepsin has a wide range of substrate specificity. However, studies have shown that compared with alkaline protease, it has low hydrolysis efficiency for peptide bonds adjacent to three alkaline amino acids ( lysine, arginine and histidine ) . In addition, although pepsin has a wide range of substrate specificity, due to the limited residence time of feed protein in the stomach, and at low pH values, not all proteins can effectively hydrate and be dissolved, therefore, feed protein is not well hydrolyzed here.

Characteristics and deficiency of endogenous protease in small intestine :

In the small intestine, the pH value changed from acidic to neutral and alkaline. Unlike pepsin, the substrate specificity of these proteases secreted by the pancreas is relatively narrow. It is well known that trypsin only hydrolyzes peptide bonds adjacent to basic amino acids lysine and arginine. Chymotrypsin was more focused on the hydrolysis of peptide bonds near hydrophobic amino acids of macromolecules, such as phenylalanine, tyrosine, tryptophan and leucine ; trypsin prefers to hydrolyze peptide bonds near amino acids with small hydrophobic side chains, such as alanine, valine and leucine. It is worth noting that trypsin is the main protease secreted by the pancreas. The secretion of chymotrypsin is only about 50 % of it, and the amount of elastase is less. In other words, proteases secreted by the pancreas tend to hydrolyze peptide bonds adjacent to lysine and arginine, rather than all peptide bonds in the hydrolysate.

Alkaline protease advantage 1 : Adapt to a wide range of PH.

Alkaline protease is a single-component endo-digested feed protease with wide substrate specificity and bacterial origin. It can work efficiently at the pH value of the small intestine, and has the highest activity in the neutral and alkaline pH ranges. It still has a high enzyme activity level at the pH value of 3 – 4.5 in the anterior segment of the gastrointestinal tract.

Advantage 2 of alkaline protease : Wide substrate range. 

Alkaline proteases can hydrolyze not only peptide bonds that pepsin, trypsin, chymotrypsin and elastase can hydrolyze, but also peptide bonds that are less easily hydrolyzed by the four proteases. Plant-derived proteins are often rich in acidic amino acids, namely aspartic acid and glutamic acid, and their amide derivatives, such as as asparagine and glutamine. However, the protease secreted by the pancreas is not easy to hydrolyze the peptide bond composed of these amino acids, and alkaline protease can effectively hydrolyze it. Peptides adjacent to phenylalanine, histidine, leucine, methionine, tryptophan and tyrosine have high activity.

Alkaline protease advantage 3 : Strong complementary effect with endogenous protease.

Unlike other proteases, alkaline proteases play a unique role ; it does not compete with pepsin, trypsin and other endogenous proteases secreted by pancreas in proteolysis, but complements these endogenous proteases. Due to the different substrate specificity of alkaline proteases ( see table 1 ), a group of different small peptides can be produced based on the difference of hydrolysis peptide sites compared with pepsin and pancreatic secretory proteases.

Alkaline protease advantage 4 : Improve the digestibility of other nutrients.

It is well known that phytase has the function of ' exceeding the release of phytate phosphorus ', and feed protease also has the effect of ' exceeding the degradation of protein '. In addition to improving the digestibility of protein amino acids, alkaline protease can also improve the digestibility of starch, fat and structural carbohydrates including fibers in feed. This is because there is a close structural relationship between different nutrients in feed. For example, starch granules in grains are often encapsulated by stored proteins. Taking maize as an example, starch is distributed in two regions of endosperm, keratin region and silty region. Compared with the silty region, the starch granules in the horny region were more tightly bound to the starch-protein matrix. Obviously, the protein ( zein, albumin, globulin, glutenin ) coated with corn starch granules must be degraded first, and amylase can then hydrolyze starch.

YSS PROZYME-PRO is a high-end complex created protease , a complex protein synergist.

Features:

1. Stable during feed processing.
2. Fully compatible with other feed enzymes.
3. Wide selection of raw materials and efficient enzymatic properties.
4. Increase the absorption digestibility of protein and amino acid by 3%-10%.
5. Fast and remarkable effect, stable batch, safe and environmentally friendly.
6. Pure biological fermentation preparation, does not produce drug resistance.
7. Degrades a wide range of feed proteins in conjunction with the animals'own digestive enzymes.
8. Catalyzes the hydrolysis of diet proteins to peptides and amino acids making these nutrients available for uptake and further utilization by the animals.
9. Accelerate nutrition conversion, promote energy and fat absorption, improve intestinal mucosa, reduce intestinal adhesion of harmful bacteria, and achieve animal intestinal health.

       Optimal temperature: 40-70℃. Active temp. range: 20-80℃，.

       Optimum pH: 4-10. The pH range is 2-12.

1. Tolerance feed pelleting high temperature, after 100 °C 90s, enzyme activity kept above 85 %.

2. Protease recovered well in simulated animal intestine in vitro.

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