Protein hydrolysis technology: exploring the main production process of active peptide
Proteolysis is a process that uses specific means to decompose macromolecular proteins into small molecule peptides with different biological activities. It occupies a dominant position in the field of peptide production.
Its characteristics includes strong controllability, the ability to produce specific peptides in a targeted manner, high product safety and economical cost.
Chemical hydrolysis method
The chemical hydrolysis method is based on the principle of acid-base hydrolysis. Although it is simple to operate and low in cost, it may cause non-specific destruction of protein and peptide structures due to the intense reaction conditions.
For example, the transformation of the three-dimensional configuration of amino acids and the generation of toxic by-products. In view of the difficulty in accurately controlling the degree of hydrolysis and potential side effects, this method is currently rarely used in actual production.
Enzymatic hydrolysis
Enzymatic hydrolysis has emerged as the most prevalent peptide preparation technology in laboratories and industrial production, attributed to its gentle reaction conditions, superior product purity, absence of amino acid racemization, non-toxic side effects, and its environmentally friendly nature.
In the enzymatic hydrolysis process, the choice of protease is crucial, mainly derived from microorganisms, plants and animals.
Plant-derived proteases, such as bromelain, are widely used in industrial production because of their rich sources and lower cost;
Animal-derived proteases, such as trypsin and pepsin, have strong specificity, but their costs are usually high due to source limitations and high extraction technology requirements;
Microbial proteases have excellent solubility, high activity and strong action,above all they are well suited for a wide range of applications.
The enzymatic hydrolysis method can not only effectively retain the nutritional value of protein, but also optimize its physical and chemical properties and functions.Furthermore,the advantages of enzymatic hydrolysis are efficient, easy to be control, and can produce high-quality, high-purity peptide products. It is especially suitable for the large-scale production of biologically active peptides.
Synthesis method: Design and create specific active peptides
The synthesis of polypeptides mainly includes three pathways: chemical synthesis, enzyme-catalyzed synthesis, and genetic recombinant synthesis.
Chemical synthesis method
Chemical synthesis of peptides mainly relies on solid-phase or liquid-phase synthesis technology. The solid-phase synthesis method is suitable for laboratory research and has the characteristics of high product purity but high cost and low yield. It has certain limitations especially for the synthesis of short-chain and small molecular weight peptides. .
In contrast, the liquid phase synthesis method is more suitable for industrial production needs and can provide high-purity and high-yield products, but it is more suitable for longer chain or high value-added short/medium chain active peptides.
Chemical synthesis methods generally have problems such as high cost, environmental pollution risks, many side reactions, and some products may be toxic, which restrict their application in large-scale production.
Enzyme synthesis method
Enzyme-catalyzed synthesis is mainly used for the synthesis of shorter peptide chains. It is environmentally friendly and has low toxicity of by-products, but it has many side reactions and low yields.
Gene recombination method
The genetic recombination method is suitable for the synthesis of longer peptide chains, especially polypeptides containing hundreds of amino acids. This method introduces the gene sequence encoding the polypeptide into a microorganism or other host organism for expression.
The genetic recombination method can significantly reduce the production cost of peptides that are difficult to obtain naturally or have high production costs and ensure safety, but its technical threshold is high and it has not yet been widely used in the industrial production stage.
Microbial fermentation: a new way to discover bioactive peptide
The principle of microbial fermentation is to use the protease secreted during microbial fermentation to enzymatically hydrolyze proteins to obtain biologically active peptides.
The key part of this method lies in the selection of strains and the optimization of culture conditions, including culture medium formula, strain type, fermentation temperature, time and bacterial age.
The preparation of active peptides by microbial fermentation has the advantages of low production cost, no bitter taste of the peptides produced, and simplified process flow. Common strains include Bacillus subtilis and Aspergillus niger.
The challenges faced by this method mainly include: safety issues, many fermentation strains have toxicity or adverse effects; fermentation conditions are complex to control, intermediate metabolites may inhibit enzyme synthesis, and the protease system produced during the fermentation process is difficult to accurately regulate to meet the target active peptide Preparation requirements make it more difficult to separate and purify target polypeptides.
How to screen safe and effective strains and optimize the fermentation process are key issues that need to be solved urgently when preparing active peptides through microbial fermentation.