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1. Preparation of enzymolysis raw materials Tartary buckwheat bran protein is prepared from buckwheat bran after extraction of flavonoids and is prepared by alkaline extraction and isoelectric precipitation. The protein is mainly composed of albumin and globulin, wherein the amino acid composition is rich and the contents of hydrophobic amino acids, aromatic amino acids, proline and arginine are relatively high, and these amino acids are favorable for obtaining high content of active peptide substances. .
Using this protein as a raw material for enzymatic hydrolysis, it is not only easy to obtain a target product having a certain amino acid composition, but also to make comprehensive use of resources, and at the same time eliminate the assumption that its activity is derived from flavonoids, thereby simplifying the process.
2. Production of Tartary Buckwheat Bran Peptide (1) Pretreatment Before enzymatic hydrolysis, the enzymatically digested raw material should be subjected to the necessary high-temperature pretreatment for the purpose of 3: 1 Denature the protein. The structure of the peptide chain is opened to loosen the molecular structure, increase the action site of the enzyme, and at the same time reduce the viscosity of the solution, so that the molecular motion can be more freely, thereby accelerating the hydrolysis rate. 2 sterilization. Avoid overgrowth of bacteria, and unpredictable hydrolysis or increase the apparent degree of hydrolysis. 3 Purification of trypsin inhibitors. In the later hydrolysis process trypsin can play a normal role.
(2) Selection and application of enzymes In order to obtain peptides with higher content, better activity, and lower cost, enzymes should be selected from the following four aspects: 1 Types of enzymes. The endopeptidase should be selected instead of the terminal peptidase to avoid excessive free amino acids in the hydrolysate, increase the yield and reduce the measurement interference caused by excess amino acids and subsequent isolation difficulties. It is also best to choose according to the specificity of the hydrolysis. 2 The source of the enzyme. Taking into account the safety of food and the normal function of biological activity, try to choose the enzyme system from animal digestive tract, such as pepsin, trypsin. In addition, alkaline protease (Alcalase) is a microbial enzyme with a wide range of sources and low cost, and is suitable for industrial production. It is an ideal industrial enzyme. 3 The optimum conditions of the enzyme. Since the final biological activity is tested by the human digestive system, try to select the enzyme system that is close to the human gastrointestinal tract environment when enzymatically digested, so that high contrast in vivo and in vitro activity can be avoided. 4 Screening of multiple enzyme complexes. When the hydrolysis conditions of the complex enzyme are optimized, the enzymes should not be arbitrarily combined arbitrarily, and it is also not suitable to combine the enzymes with large degree of hydrolysis. Perhaps the two enzymes with high degree of hydrolysis are in the same site of action. Naturally, the combination of the two enzymes will not increase the degree of hydrolysis. On the contrary, the use of an enzyme having a high degree of hydrolysis in combination with an enzyme having a low degree of hydrolysis makes it possible to obtain a better degree of hydrolysis or obtain a more active target peptide.
(3) Indicator Setting At present, the production of active peptides is based on the degree of hydrolysis (degree of hydrolysis refers to the ratio of the number of peptide bonds that are hydrolyzed and the number of peptide bonds of the raw material protein) as a measure. After analyzing a large amount of data, it was found that hydrolysis Degree should not be used as an indicator of active peptide production, but should use the final activity as an indicator. There are four reasons: 1 Free amino acids overemphasize the degree of hydrolysis, causing excessive hydrolysis of the protein, resulting in excessive free amino acids, and polypeptide yield decline. 2 Types and Sources of Enzymes Due to the different sites of action of different enzymes, the structure and length of peptides that are cut off are different, and the contribution to the degree of hydrolysis is naturally different, but the activity may be the same. 3 Pretreatment of bacterial overgrowth can cause unpredictable hydrolysis and increase the apparent degree of hydrolysis, but may not result in highly active products. 4 The degree of hydrolysis itself is difficult to accurately determine the degree of hydrolysis to use a number of test values â€‹â€‹and a variety of reagents, which will inevitably increase the measurement error; is not conducive to obtain an accurate degree of hydrolysis. A rough estimate can be made of the hydrolysis time, the volume of sodium hydroxide consumed during hydrolysis, and soluble nitrogen.
The amount of sodium hydroxide consumed during the hydrolysis process is determined based on the constant change of pH during the hydrolysis process. In order to maintain the pH of the system constant, it is necessary to add sodium hydroxide continuously so that the consumed sodium hydroxide is consumed. The volume can be roughly grasped the degree of hydrolysis.
With the progress of hydrolysis, the soluble nitrogen index is shorter and the solubility is increased accordingly. By measuring the increase in soluble nitrogen or the decrease in turbidity, the degree of hydrolysis can be roughly estimated.
(4) Activity determination When activity is used as the final detection index, it is particularly important to select or establish an efficient, rapid, accurate, sensitive, economical, practical and simple detection method. For example, the determination methods of blood pressure lowering activity include spectrophotometry, fluorescence spectrometry, radiochemical method, high performance liquid chromatography, capillary micellar electrokinetic chromatography, high performance capillary electrophoresis, etc., and different methods can be selected according to their own conditions.
(5) Isolation, purification and characterization of active peptides The active peptides produced by enzymatically hydrolyzing tartary buckwheat bran protein may have completely different physicochemical properties, such as molecular weight distribution, amino acid composition, charge amount, pH value, polarity, and thus have physiological properties. The method of separation and purification of the desired product of the activity may be very different. On the other hand, the separation and purification methods and conditions of the target product, which are often obtained under the conditions of an enzymatic hydrolysis, are difficult to transplant to the product under another condition. Therefore, the separation and purification of active peptides is a very complicated and arduous task.
When separation and purification are performed, it is preferable to use two or more means different in the separation principle so that the target product obtained is more pure. Combinations such as gel chromatography and electrophoresis, ion exchange and partition chromatography, HPLC and ultrafiltration, and the like have been successfully used for the separation and purification of active substances.
3. Directions for Development (1) Problems of Functional Degradation Caused by the Removal of Bitterness In the process of proteolytic production of peptides, the production of bitterness is inevitably accompanied. There are many related research reports, but most of them focus on the speculation of the bitterness mechanism and the removal of bitterness. In the future, we should focus on cutting off or weakening the bitterness from the source and debittering in the production process. From previous reports, debittering was preceded by isolation of active peptides and evaluation of their bitterness. The evaluation of active peptides should focus on efficacy. If no adverse effects on the human body are found, it should not be blindly debittered. The activity should be further measured before and after treatment, and deactivation should be decided based on the decrease in activity. If possible, a separate activity assay should also be performed on the bitterness that is removed.
(2) Differences in activity The activity of the final product must be tested in the human body before it can be truly tested. Many data indicate that active peptides exhibit different activities in experimental animals and humans, in vitro and in vivo. Care should be taken in future studies.
(3) Determination of Multiple Activities of Enzymatic Hydrolysates Natural products often have a variety of biological activities, and most of the current studies have studied an activity. Parallel testing of multiple physiological activities of the same hydrolysate can expand the final product. The scope of the applicable population, so as to prepare for the product to enter the market, provide a better connection for basic research, product development and market operations. Song Jincui extracted from: "Processing of Agricultural Products" 2007.01
Dried Garlic Products,Dried Garlic Flakes,Dried Garlic Puree,Dried Garlic Slice
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