A meat enzymatic pet food process containing XN2 to measure the oxidation activity of controlled-release substances

Abstract

The present invention belongs to the field of enzymatic hydrolysis technology. The present invention provides a meat enzymatic hydrolysis pet food process containing XN2 to measure the oxidation activity of controlled-release substances, including the process of selecting a certain amount of supernatant to add a certain amount of phosphatidylcholine and stirring evenly for testing, and measuring and controlling the enzymatic hydrolysis process according to the recovery rate of the filtrate and the change in the viscosity value of the controlled-release substance in the enzymatic hydrolysis process. The present invention at least has the functions of improving the cleavage of hydrophobic groups, preventing corruption, assisting in optimizing the anti-infection and digestion of pet food, improving the rapid development effect, and regulating enzymatic hydrolysis and measuring controlled-release substances. The pet food of the present invention has a multiple acceleration of the growth and development of pets compared with ordinary pet food, and the method of the present invention has strong applicability and good scalability.

Description

[0001] The application number of the original case of this application is "202210018526.7", the name is "A meat enzymatic pet food with antioxidant activity and its preparation process", and the application date is "2022.01.08". Technical Field

[0002] The invention belongs to the field of enzymatic hydrolysis technology, and in particular relates to an antioxidant chicken enzymatic hydrolysis pet food and a preparation process thereof Background Art

[0003] Only when the peptide amino acids of proteins are decomposed into the required small molecules can they be beneficial to the digestion of pets. Most of the existing protein decompositions use enzymatic hydrolysis or Maillard reaction. The Maillard reaction is also called non-enzymatic browning reaction, which is a non-enzymatic browning reaction widely used in the food industry. It is a reaction between carbonyl compounds (reducing sugars) and amino compounds (amino acids and proteins), but the process stages are complicated and the reaction process is changeable for pet food. Enzymatic hydrolysis mainly involves proteases acting on specific parts of the protein structure to cut and decompose into small molecule peptides or free amino acids. Most animal and microbial proteins can be hydrolyzed by a single enzyme or multiple enzymes in synergy, but enzymatic hydrolysis is limited in the types and selection of enzymes for hydrolyzing hydrophobic amino acid groups, and it is impossible to complete the good cleavage of hydrophobic groups. Existing pet food also has the defects of slow digestion and rapid deterioration. In this regard, the above-mentioned problems affecting the development of pet food need to be solved urgently. Summary of the invention

[0004] In order to achieve at least one of the above problems, the present invention provides a preparation process of meat enzymatic pet food with antioxidant activity, a method for measuring the enzymatic hydrolysis process of controlled-release substances, comprising the steps of taking a certain amount of supernatant, adding a certain amount of phosphatidylcholine, stirring and evenly testing, adding a controlled-release substance XN2 to the method for testing the copper ion state in the enzymatic hydrolysis of the controlled-release substance according to the recovery rate of the filtrate and the change in viscosity value of the controlled-release substance in the enzymatic hydrolysis process, drying the filtrate after the XN2 filtration test to a constant weight and recording it as XN2SB, taking XN2SB for infrared spectrum testing, combining the method for testing the basic performance of the controlled-release substance, taking the supernatant after the enzymatic hydrolysis of the controlled-release substance, and concentrating to detect the presence of magnesium ions, and judging the controlled release of copper and the participation of magnesium or amino acids in the enzymatic hydrolysis process; the preparation of the controlled-release substance XN2 is based on XN1 The difference from XN1 is that acrylic acid, allylthiourea, and a controlled-release substance containing the component of structural formula I are added to an aqueous solution containing formamide in a mass ratio of 20:3:0.3, and reacted at 40-80 degrees to generate XN2. The beneficial effects of the present invention are: the present invention at least has the effects of improving the cleavage of hydrophobic groups, preventing corruption, helping to optimize the anti-infection and digestion of pet food, and improving the rapid development effect. The pet food of the present invention has a multiple acceleration of the growth and development of pets compared to ordinary pet food. The shelf life and antioxidant properties of the pet food produced by the process of adding different controlled-release substances of the present invention are improved by at least about half a year compared to ordinary pet food. The method of the present invention has strong applicability and good scalability. The present invention further has the effect of regulating the enzymatic hydrolysis corresponding to the controlled-release substance. The controlled-release substance in the overall structure of the present invention further has the function of controlling the release of ions synchronously. BRIEF DESCRIPTION OF THE DRAWINGS

[0005] Figure 1 : Electron microscopic image of the emulsion state of controlled release substances. DETAILED DESCRIPTION

[0006] The technical solutions in the embodiments of the present invention will be described clearly and completely below in conjunction with the drawings in the embodiments of the present invention. Obviously, the described embodiments are only part of the embodiments of the present invention, rather than all the embodiments.

[0007] The invention discloses a preparation process of meat enzymatic pet food with antioxidant activity, comprising the following steps: weighing pre-treated meat or animal offal, adding distilled water at a material ratio of 1:5, crushing and homogenizing with a high-speed crushing homogenizer, adjusting the solution pH to 4-10, controlling the temperature to 40-70°C, and then forming a hydrolyzate by adding 3-5% of the water amount of the enzyme, adding a release-controlling substance and enzyme again during the hydrolysis process, adjusting the hydrolysis conditions to continue the hydrolysis to the required supernatant, taking the supernatant to make powder, and then configuring other nutritional additives as needed to form the pet food, wherein the enzymes include pancreatin, chymotrypsin and histidine decarboxylase to improve the cleavage of hydrophobic groups, prevent corruption, assist in optimizing the anti-infection and digestion-aiding effects of the pet food, and improve the rapid development effect, wherein the enzymes also include methionine adenosyltransferase and methionine degrading enzyme, and the other required substances include ascorbyl palmitate, dihydropyridine and astaxanthin.

[0008] The process of adding the controlled-release substance again includes adding under acidic conditions or adding under alkaline conditions or releasing after the enzymatic hydrolysis reaction or releasing immediately after adding or releasing in another hydrolysis stage after adding, etc., and the controlled-release process is coordinated according to the controlled-release molecular parameters. The controlled-release substance includes allyl thiourea or acrylic acid and its salts, selected long-chain alkanes or amino acids or long-chain pyridines or amino residue pyridines, such as sodium acrylate and amino acids, such as allyl thiourea, acrylic acid, and long-chain alkanes. The reaction is formed to achieve the controlled release of transition metals including copper, and further regulates the enzymatic hydrolysis and the controlled-release substance. The controlled-release substance in the overall structure of the present invention further has the function of a controlled-release regulator that controls the release of ions synchronously. The enzymatic hydrolysis reaction also includes the process of adding substances such as tryptophan, cystine, and cysteine.

[0009] The controlled release substance comprises acrylic acid, allylthiourea, and selenomethionine, or the controlled release substance comprises allylthiourea, acrylic acid, and long-chain alkene pyridine to react to generate a substance comprising the following structural formula I, wherein the long-chain alkene pyridine comprises a pyridine-containing histidine magnesium residue substance, an alkyl methionine ester-containing substance, the long-chain pyridine comprises a pyridine containing a long-chain alkyl, the residual pyridine comprises a pyridine-containing histidine magnesium residue, and the long-chain alkene pyridine-containing substance also comprises a phosphatidylcholine component,

[0010] The following describes the preparation process of the controlled release substance XN.

[0011] The controlled release substance comprises a substance generated by the reaction of acrylic acid, allyl thiourea and selenomethionine. Acrylic acid, allyl thiourea and selenomethionine are added to an aqueous solution at a mass ratio of 20:3:1. Private Pan 60 and Tween 60 at a mass ratio of 3:1 are added to 1.2 times kerosene. The aqueous solution is added to the kerosene and stirred to form an emulsion. When the reaction is deoxidized and ammonium persulfate is added to catalyze the reaction and no heat is released, a polymerized high molecular emulsion is formed. The emulsion sample is observed by electron microscopy. Figure 1 It can be seen that the particle size of the emulsion is more than 1200nm. The emulsion after the reaction is demulsified, and the viscous substance after demulsification is dried and crushed to constant weight, recorded as the controlled release substance XN1. 0.3% XN1 solution is prepared with deionized water, and the viscosity value is 9mPa.s after conversion by capillary test viscosity N. The calculated molecular weight is about 2.3 million. The optimal molecular weight controlled by the test is 2 million, which is conducive to maintaining the filtration particle size.

[0012] Furthermore, the controlled release substance comprises the preparation of a substance comprising the following structural formula I generated by the reaction of allylthiourea, acrylic acid, and long-chain alkene pyridine, or the preparation of a substance comprising a histidine magnesium residue containing pyridine, or a substance containing an alkyl methionine ester,

[0013] Specifically, the first step: preparation of pyridine-containing histidine magnesium residue material, prepare 3% magnesium chloride solution, adjust the pH to 6.9-9 to form a precipitate, add 3-10g ammonium carbonate thereto, and then add histidine at a low temperature of 15-40 degrees until the precipitate dissolves, the volume of magnesium carbonate crystals is smaller than that of magnesium hydroxide micro-precipitate, further, the magnesium carbonate micro-soluble substance and the magnesium hydroxide precipitate form a micro-precipitate equilibrium, the supernatant pH is tested to be 6-7, the supernatant is taken to maintain the pH at 7.1-9, and the color change of magnesium reagent is not obvious, the pH is adjusted to 9.5, and blue turbidity appears. The acid-base change and the salt color change indicate that the above reaction forms a carboxylic acid complex of magnesium ions, which also confirms the amino cation of amino acids under the above conditions. The general EDTA method is used for titration, and red appears. The lack of obvious turbidity further proves that the above-mentioned different carboxyl complexes and different EDTA complexes have different stabilities at different pH values, indicating the formation of magnesium histidine; when acid is added dropwise to the supernatant, gas is released, indicating the presence of magnesium carbonate, and then 5-vinylpyridine formate is added to the supernatant under the conditions of N,N'-diisopropylcarbodiimide dehydration and dichloromethane solvent to heat the reaction, and after the reaction solution is separated and treated, the supernatant is heated and then dried to eliminate the influence of unreacted magnesium carbonate, a small amount of the dried product is prepared into a solution, and magnesium reagent I is added to ammonia monohydrate, and the reaction is not obvious, and another dried product is prepared into a solution, acid is added to adjust the pH to below 6, and the reaction is carried out for several minutes, and magnesium reagent I and ammonia monohydrate are added again, and purple-red appears after heating, and the possible formation of pyridine-containing magnesium histidine residues is tested;

[0014] Step 2: Preparation of alkyl methionine ester-containing substances: selenomethionine and di(hydroxyethyl)methyldodecylammonium chloride can be mixed and then DCC (dicyclohexylcarbodiimide) can be added at low temperature, and then DMAP (4-dimethylaminopyridine) can be prepared into a solution and slowly added drop by drop. After the reaction stops exothermic, solid-liquid separation and purification are performed, and a 1:1 solution is prepared with the purified substance. A small amount of the purified solution is added to an acidic phenolphthalein solution to show colorlessness, and red appears after heating, confirming the presence of an ester group. Furthermore, the present invention protects the group when necessary, such as using Boc to protect the amino group, and an esterification reaction occurs under the action of DCC / DMAP. After the reaction is completed, the product is obtained by removing the protection with trifluoroacetic acid;

[0015] Step 3: Preparation of long-chain alkene pyridine. Add pyridine-containing magnesium histidine residue material and alkyl methionine ester material to a solution containing ethanol and acetone in a mass ratio of 5:1, heat and react under nitrogen sealing regulation until the solution becomes a paste, and remove the solvent by reduced pressure distillation to form a controlled release material containing the component of structural formula I. Add acrylic acid and allyl thiourea to form a controlled release material containing the component of structural formula I in a mass ratio of 20:3:0.3 to an aqueous solution containing formamide, and generate a controlled release material of structural formula I by emulsification reaction at 40-80 degrees in the same manner as the preparation process of controlled release material XN1.

[0016]

[0017] The infrared detection spectrum of the controlled release substance containing structural formula I is shown. The weak peak at 1600cm-1 indicates that the double bond of the olefin is basically opened. The characteristic absorption of carboxyl groups at 3500cm-1, 2690cm-1, and 1690cm-1 indicates the presence of acrylic acid. The strong peak at 1110cm-1 and the sharp and weak peaks at around 700 and 800cm-1 are characteristic of histidine. The characteristic absorption at 1540 is N-substituted pyridine. The thiourea peak appears at 900-1300cm-1, the absorption peak of the amino group of methionine at 3530-3280cm-1, and the absorption peak of hydroxyl at 3600cm-1. Carboxylic acid, pyridine, alkyl and other groups appear in the above formula. It can be seen that the substance containing structural formula I generates long-chain alkane olefin pyridine, and the generation of the corresponding substances in the above preparation process of the controlled release substance is also illustrated in the form of images. It should be noted that the pyridine-containing histidine magnesium residue substance and the alkyl methionine ester substance can be used alone or in combination.

[0018] The fourth step is the preparation of the controlled release substance XN2. Based on XN1, the difference from XN1 is that acrylic acid, allylthiourea, and the controlled release substance containing the component of structural formula I are added to the aqueous solution containing formamide at a mass ratio of 20:3:0.3, and reacted at 40-80 degrees to generate XN2. The emulsion sample was observed by electron microscopy. The electron microscopy data showed that the molecular weight was 1100nm. 0.3% of XN2 was configured into an ionic aqueous solution. The viscosity N was converted by capillary test to obtain a viscosity value of 7mpa.s, and the calculated molecular weight was about 2.28 million. , which is different from the performance of XN1, after adding 0.1% phosphatidylcholine or 0.01% K12 to the solution of 0.3% XN2 substance, the tested viscosity becomes 10mpa.s, while the molecular weight tested by capillary is 2.29 million. The viscosity increases but the molecular weight does not change. The principle of viscosity change is the physical association between phosphatidylcholine and long-chain alkyl and pyridine ring molecules, so that the viscosity changes caused by physical changes while the molecular weight does not change. This effect is beneficial to the control output and testing of enzymatic reaction substances, such as viscosity changes are beneficial to the addition and safe filtration separation of precipitation.

[0019] The following is a basic performance test method for measuring the copper ion catalytic controlled release substance XN involved in this invention.

[0020] First, XN1 is preferably used to test the catalytic decomposition of copper ions. Distilled water is weighed and placed in the same glass beaker SB1 and glass beaker SB2. 10 mg / kg copper oxide is added to SB1 and 100 mg / kg copper oxide is added to SB2. Then, the pH of the solution in each beaker is adjusted to 4.5, and the temperature is controlled at 60°C. Then, 3% of the water is added with equal weight portions of pancreatic enzyme, chymosin, and histidine decarboxylase to hydrolyze for 1 hour to form a hydrolyzate. The supernatants of the hydrolyzates in the two beakers are respectively added with 0.05% XN1 and hydrolyzed for 0.5 hours, and then the pH is adjusted to 8 and hydrolyzed for 0.5 hours. 100 g of the supernatants of SB1 and SB2 are respectively taken and filtered with filter papers with a pore size not exceeding 1 um. The filtrates are weighed. The filtered weight of the supernatant of SB1 is 93.6 g, and the filtered weight of the supernatant of SB2 is 93.7. The recovery rate of the filtered supernatant of SB1 is SB1. The recovery rate of SB2HS was 93.6%, and that of SB2 supernatant filtration was 93.7%. Both recovery rates were above 93%, indicating that SB1 beaker XN1 was basically not degraded into small molecules below 1000 nm, while SB2 beaker XN1 might have been degraded into parts smaller than 1000 nm.

[0021] Secondly, the filter paper after filtering the supernatant of SB1 and SB2 was dehydrated and washed with ethanol, and the filtrate was dried to constant weight and recorded as XN1 SB1 and XN1 SB2. SB1 and XN1SB2 were prepared with 0.3 deionized water solution, and the viscosity N was converted by capillary test to obtain the viscosity values ​​of XN1SB1N as 8.9mpa.s and XN1SB2N as 6mpa.s. The molecular weight values ​​of XN1SB1 and XN1SB2 were calculated as XN1SB1F as 2.26 million and XN1SB2F as 1.32 million, respectively. 10g of XN1SB1 and XN1SB2 samples were taken, placed in a muffle furnace and burned at 500℃ to constant weight, then taken out and cooled to room temperature, and 10g of sulfuric acid solution was added to dissolve them and the pH was adjusted to a neutral solution. 0.5g of ammonia water was added to the solution to produce a blue color. The chromaticity CD value was tested with a handheld intelligent colorimeter. The chromaticity values ​​of XN1SB1CD and XN1SB2CD were 0.05 degrees and 0.43 degrees, respectively.

[0022] Finally, a comparative test was conducted to simulate the baseline amount of copper ions present in the animal body by preparing a solution containing 10 mg / kg of copper ions. After adding sulfuric acid solution to dissolve, the pH was adjusted to 10 g of a neutral solution. 0.5 g of ammonia water was added to the solution to produce a blue color. The CD value tested with a handheld intelligent colorimeter was 0.052 degrees, which is basically close to the lower CD value of 0.05 degrees in the above corresponding case. The comparative test shows that the regression accuracy of the test data is relatively high, and also confirms that copper exists as ions, the binding of the measured controlled-release substance to copper, the amount of copper ions present, and the copper ions in the above environment have an impact on the degradation of the measured controlled-release substance.

[0023] From the above, it can be seen that the supernatant filtration recovery rate of the XN1 substance under the above scheme conditions combined with the above scheme conditions can affect the molecular weight and viscosity of XN1, and then quickly judge whether the enzymatic hydrolysis reaction of the present invention has excessive decomposition of copper ions. When the XN molecular weight is less than 2 million and the supernatant filtration recovery rate is greater than 93.6%, it means that the XN molecules are degraded too quickly, indicating that copper exists more in the ionic state. When the XN molecular weight is greater than 2.26 million and the supernatant filtration recovery rate is less than 93.6%, it means that the XN molecule is degraded within the basic range;

[0024] Further explanation may exist histidine decarboxylase to decompose CuPZn-SOD, judge the ion content. Further, can judge the control of ions including copper under the above conditions and enzymatic reaction according to XN1 molecular weight and viscosity, further, by the above data analysis, combined with percentage quantity conversion, it can be known that under the conditions of the above scheme, XN1 molecular weight and viscosity and copper ion control situation are nearly linear, combined with experimental test evaluation of the proportion of copper ion on molecular weight and viscosity under the above conditions, when the XN1 material supernatant test filtration recovery rate is less than 93.6% and the molecular weight is greater than 200, preferably according to the following formula to predict the control of copper ion value under the above conditions M = (44XN1 SB1 N / 89) + (28XN1 SBF / 113), to achieve the judgment of molecular weight or the judgment of enzymatic reaction or the judgment of molecular weight according to the corresponding parameter formula.

[0025] The following description describes the process of measuring the controlled release substance XN participating in the enzymatic hydrolysis process, using the recovery rate of the supernatant filtrate to judge the protein decomposition situation, and then combining the viscosity value of the substance XN after participating in the enzymatic hydrolysis process, and the molecular parameters including the molecular weight of the substance XN after participating in the enzymatic hydrolysis process to judge the copper ion state in the enzymatic hydrolysis process or the situation of the enzymatic hydrolysis process, such as whether the protein hydrolysis in the enzymatic hydrolysis process is thorough.

[0026] Specifically, the method for testing the copper ion status in enzymatic hydrolysis of the preferred substance XN1 is as follows: weigh the pre-treated meat or animal offal, preferably chicken from a supermarket, add distilled water at a material ratio of 1:5, crush and homogenize with a high-speed crusher, adjust the solution pH to 4.5, control the temperature to 60°C, and then add the following equal weight portions of pancreatic enzyme, chymosin, and histidine decarboxylase at a ratio of 3% of the added water, hydrolyze for 1 hour to form a hydrolyzate, take the supernatant of the hydrolyzate, add 0.05% XN1, hydrolyze for 0.5 hours, adjust the pH to 8, and hydrolyze for 0.5 hours, take 100g of the supernatant, filter with filter paper with a pore size of no more than 1um, weigh the filtrate to weigh 89.2g, and the recovery rate XN1 SBHS is 90.3%. Considering the filtration loss, the recovery rate is above 93%, indicating that most of the chicken protein is completely hydrolyzed, take the filtered filter paper and dehydrate and wash it with ethanol, dry the filtrate to constant weight and record it as XN1 SB, take XN1 SB is prepared with 0.3 deionized water solution, and the viscosity value obtained after conversion by capillary test is XN1 SBN, which is 8.6mpa.s. The molecular weight of XN1 substance in the above process is calculated to be about 2.12 million. According to the following judgment: when the molecular weight of XN is less than 2 million and the recovery rate of supernatant filtration is greater than 93.6%, it means that XN molecules are degraded too quickly, indicating that copper exists more in ionic state, indicating that the hydrolysis of histidine decarboxylase may be strong. When the molecular weight of XN is greater than 2.26 million and the recovery rate of supernatant filtration is less than 93.6%, it means that the degradation of XN molecules is within the basic range; it can be seen that slightly more ionic copper appears in the enzymatic hydrolysis process, which may be caused by the decomposition of CuPZn-SOD by histidine decarboxylase or the process may be caused by too fast oxidation.

[0027] Including the method of testing the copper ion state in enzymatic hydrolysis with substance XN2 or the situation of measuring and controlling the enzymatic hydrolysis process: under the same conditions, based on the test method of measuring the controlled release substance XN1, different from the test of substance XN1, 100g of the supernatant can be selected, 0.1% phosphatidylcholine is added and stirred evenly for testing. The following data are obtained in the absence of phosphatidylcholine. The filtrate recovery rate XN2SBHS of substance XN2 obtained by the test method of substance XN1 is 89.7%, the viscosity value of substance XN2 after participating in the enzymatic hydrolysis process is XN2SBN is 6.5mpa.s, and the molecular weight of substance XN2 after participating in the enzymatic hydrolysis process is about 2.2 million.

[0028] From the above data, it can be seen that the recovery rate of the filtrate of substance XN2 is reduced in the enzymatic hydrolysis process, and the viscosity value of substance XN2 after participating in the enzymatic hydrolysis process decreases slightly, which may be due to incomplete protein decomposition. The small changes in viscosity and molecular weight indicate the presence of copper ions, which further indicates that the results did not reach the corresponding results of the test of substance XN1, and the hydrolysis of histidine decarboxylase may be weak. Therefore, based on the above data, the filtrate of substance XN2 after filtration test in the above test was dried to constant weight and recorded as XN2SB. XN2SB was taken for infrared spectrum test. From the infrared spectrum, it can be seen that the characteristic peaks of pyridine, carboxyl and thiourea appeared, especially the peaks of copper complex appeared between 300-600cm-1, while the strong peak at 1110cm-1, the sharp and weak histidine peaks at about 700 and 800cm-1 and the related peaks of methionine at 3530-3280cm-1 were not obvious, which means It is clear that no histidine magnesium residues and no selenomethionine appear, indicating that at least chymosin does not cleave hydrophobic groups such as alkylpyridine. The molecular structure and the corresponding cationic group combine to have the effect of resisting chymosin cleavage in the above enzymatic environment. In the basic performance test method of XN, XN1 is replaced with XN2 after the enzymatic hydrolysis is completed, and the supernatant is concentrated and tested. The known magnesium ion test shows a display color. The presence of magnesium ions, the absence of histidine magnesium residues and the appearance of magnesium indicate that histidine decarboxylase has taken effect, indicating that there is copper control and magnesium and amino acid control release, which further indicates that the histidine group is decomposed and released in the presence of resistance. The subsequent histidine decarboxylase hydrolysis may be weak or the molecular parameters or structures including the long positively charged alkyl group after the amino acids in the molecular structure are released inhibit the corresponding carrier bacteria of the enzymes such as histidine decarboxylation, thereby causing the weakening of the performance of histidine decarboxylase.

[0029] From the above analysis of the results, it can be seen that the usage of the controlled release substance XN2 in the above enzymatic hydrolysis scheme is to add it in the late stage of pH4.5, which is beneficial to control the thorough enzymatic hydrolysis. Further, the addition of the XN2 substance under alkaline conditions or self-controlled release also has the effect of controlling the adsorption of polar amino acids, and then further combined with the control of copper ions to judge the detection of SOD decomposition by enzymes such as histidine decarboxylation, and the controlled release of magnesium ions is also beneficial to evaluate the performance of methionine adenosyltransferase. The controlled release substance of the present invention includes a process of separating and removing the added controlled release substance after participating in the enzymatic hydrolysis. The controlled release substance of the present invention includes a process of separating and removing the macromolecular part of the added controlled release substance after participating in the enzymatic hydrolysis process, and a process of testing the changes after adding phosphatidylcholine or K12 to a solution of a certain amount of the controlled release substance XN2. In addition, the application examples of the present invention are also reflected in the pet food produced by adding different release-controlling substances to the process of the present invention through actual feeding and feeding results feedback, such as also including the release-controlling substances participating in the enzymatic hydrolysis process without adding the release-controlling substances for comparison. The specific comparison process prepares the following substances according to relevant standard amounts, including selenomethionine, tryptophan, selenocysteine ​​antioxidants, peptide chain small molecules, anti-inflammatory health care produced by enzymatic hydrolysis, beneficial factors or products that promote development, ascorbyl palmitate, dihydropyridine, astaxanthin, fats, sugars, vitamins, tryptophan The pet food containing acid, cystine and cysteine ​​was fed to pets of no less than 5 cats or dogs, and compared with ordinary pet food under the same conditions and the same experimental conditions. The growth rate of the pet food prepared by the process using the controlled-release substance XN1 of the present invention was 0.3 times higher than that of the ordinary pet food, and the growth rate of the pet food prepared by the process using the controlled-release substance XN2 of the present invention was 0.5 times higher than that of the ordinary pet food. The shelf life and antioxidant activity of the pet food produced by the process of adding different controlled-release substances of the present invention were 0.6 years higher than that of the ordinary pet food.

[0030] The invention belongs to the field of enzymatic hydrolysis technology, and particularly relates to an enzymatically hydrolyzed meat pet food with antioxidant activity and a preparation process thereof, comprising weighing pretreated chicken, adding distilled water at a material ratio of 1:5, crushing and homogenizing with a grinder, adjusting the solution pH to 4-10, controlling the temperature to 40-70°C, and then adding 3-5% of the water amount of enzyme to form a hydrolyzate, adding a controlled release substance and enzyme again during the hydrolysis process, adjusting the hydrolysis conditions to continue hydrolysis until the required supernatant, taking the supernatant to make powder, and then preparing the pet food according to the required method. The invention relates to an enzymatically hydrolyzed meat pet food with antioxidant activity, comprising: The invention comprises beneficial products produced after the controlled-release substances participate in the enzymatic hydrolysis process, pancreatic enzymes, chymosin histidine decarboxylase, selenomethionine, selenocysteine ​​antioxidants, peptide chain small molecules, anti-inflammatory health care produced by enzymatic hydrolysis, development-promoting beneficial factors or products, ascorbyl palmitate, dihydropyridine, astaxanthin, fats, sugars, vitamins, tryptophan, cystine, cysteine, etc., beneficial products such as selenomethionine, etc. The shelf life and antioxidant properties of pet food are improved by at least about half a year compared with ordinary pet food. The method of the invention has strong applicability and good popularization.

[0031] The above description is only a preferred specific implementation manner of the present invention, but the protection scope of the present invention is not limited thereto. Any technician familiar with the technical field can make equivalent replacements or changes according to the technical scheme and inventive concept of the present invention within the technical scope disclosed by the present invention, which should be covered by the protection scope of the present invention.

Claims

1. A process for preparing meat enzymatically hydrolyzed pet food with antioxidant activity, characterized in that: The process includes the following steps: weighing the pre-treated meat or animal offal, adding distilled water, crushing and homogenizing, adjusting the solution pH to 4.5, controlling the temperature to 60°C, and then adding the following equal weight portions of pancreatic enzyme, chymotrypsin, and histidine decarboxylase at a ratio of 3% of the added water, hydrolyzing to form a hydrolyzate, taking the supernatant of the hydrolyzate, adding 0.05% XN2, hydrolyzing for 0.5h, adjusting the pH to 8, and hydrolyzing for 0.5h, taking the supernatant, adding 0.1% phosphatidylcholine, filtering with filter paper, taking the filtrate and weighing the weight, and testing the supernatant filtration recovery rate XN2SBH S, take the filter paper after filtration and wash it with ethanol, dry the filtrate to constant weight and record it as XN2SB, prepare deionized water solution with XN2SB, test the viscosity value with capillary tube to get XN2SBN, calculate the molecular weight of XN2 substance, and judge according to the following: when the molecular weight of XN2 is less than 2 million and the recovery rate of supernatant filtration is greater than 93.6%, it indicates that the XN2 molecule is degraded too fast, indicating that copper exists more in ionic state, indicating that the hydrolysis of histidine decarboxylase is strong; when the molecular weight of XN2 is greater than 2.26 million and the recovery rate of supernatant filtration is less than 93.6%, it indicates that the degradation of XN2 molecule is within the basic range; The controlled release substance XN2 is prepared by adding acrylic acid, allylthiourea, and long-chain alkane pyridine to a formamide-containing aqueous solution at a mass ratio of 20:3:0.3, and reacting at 40-80 degrees to generate XN2. The structural formula of XN2 is as follows:

Images