Preparation method of amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate

Abstract

The present application relates to the technical field of fertilizer preparation, and particularly relates to a preparation method of amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate, comprising the following steps: obtaining active concentrate by enzymatic hydrolysis of chicken blood; obtaining first water phase by on-line homogenization of the concentrate and zein solution; emulsifying the first water phase with oil phase, recording the reference particle size of liquid droplets, and then solidifying to obtain solid protein cores and detect the particle size; calculating the particle size ratio of the protein cores and the liquid droplets, intelligently diagnosing deviation modes, and dynamically adjusting subsequent processes; dispersing the protein cores, gradiently coating based on Zeta potential and double flow rates, and constructing core-shell structure by programmed pH gradient crosslinking, and obtaining microcapsules by post-processing, wherein the present application realizes accurate regulation and control of the particle size, structure and encapsulation quality of the microcapsules by on-line monitoring and feedback control throughout the whole process, solves the problem of large batch fluctuation in traditional processes, and the obtained product has the advantages of slow release, high efficiency, good stability, batch uniformity and the like.

Description

Technical Field

[0001] This invention relates to the field of fertilizer preparation technology, and in particular to a method for preparing an amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate. Background Technology

[0002] The extensive use of chemical fertilizers has played a vital supporting role in my country's agricultural development, but it has also brought about a series of environmental problems, such as soil compaction, acidification, and eutrophication of water bodies. Therefore, developing new types of fertilizers that are environmentally friendly and efficient in nutrient utilization has become an inevitable requirement for the sustainable development of agriculture.

[0003] Amino acid water-soluble fertilizers, as an environmentally friendly specialty fertilizer, are receiving increasing attention for their research and application. Chicken blood, rich in high-quality protein (approximately 18%) and highly bioavailable heme iron, is a potentially valuable resource. Traditional treatment methods, such as direct disposal or simple processing into feed, result in low added value, resource waste, and environmental pollution. Enzymatic hydrolysis to prepare liquid fertilizers rich in small-molecule peptides and amino acids can achieve high-value utilization, providing crops with readily available organic nitrogen and easily absorbed iron. However, traditional amino acid water-soluble fertilizers are mostly prepared using acid or alkali hydrolysis methods, which easily destroy the active protein peptides, resulting in a wide molecular weight distribution, unstable functional components, and lower fertilizer efficiency. Furthermore, the active ingredients (such as small-molecule peptides and trace elements) of amino acid fertilizers prepared with existing technologies are easily lost after application to the soil due to leaching, volatilization, or rapid microbial decomposition, leading to a short duration of effectiveness.

[0004] Microencapsulation technology is an effective strategy for solving the above problems. By encapsulating active ingredients within a polymer wall material, the core material can be physically isolated and protected, and the slow release of nutrients can be achieved. However, existing agricultural microencapsulation technologies (such as spray drying and composite coagulation) often face challenges such as low encapsulation efficiency, easy core leakage, wide particle size distribution, and poor batch reproducibility when applied to complex and heat-sensitive biomass enzymatic hydrolysates. More importantly, traditional processes are mostly "black box" or open-loop operations, relying on fixed parameters and experience-based judgment. They cannot detect and compensate for quality deviations caused by raw material fluctuations and equipment status changes in key steps such as emulsification, solidification, and encapsulation in real time, resulting in unstable product quality.

[0005] Chinese Patent Publication No. CN119241301A discloses a method for preparing amino acid-containing water-soluble fertilizer using slaughtered blood of livestock and poultry. First, blood from livestock and poultry in slaughterhouses is collected using a blood collection container, and an anticoagulant is added to obtain an anticoagulant raw material. This anticoagulant raw material is then heated and sterilized, followed by enzymatic hydrolysis with Bacillus subtilis and potassium dihydrogen phosphate to obtain an enzymatically hydrolyzed liquid. This liquid is then subjected to filtration, complexation, ultraviolet disinfection, and sterilization. The sterilized enzymatically hydrolyzed liquid is tested for amino acids, and other nutrients are added to form an amino acid-containing organic liquid fertilizer. Finally, it undergoes preservation treatment, is packaged, and stored in a cool, dark place, completing the preparation process of the amino acid water-soluble fertilizer.

[0006] Therefore, the above-mentioned method for preparing water-soluble fertilizer containing amino acids using slaughtered blood of livestock and poultry has the following problems: First, the fermentation and enzymatic hydrolysis process mainly relies on microbial fermentation, which lacks precise control over the molecular weight distribution of active peptides (oligopeptides), resulting in complex product composition and difficulty in guaranteeing the content and stability of effective active ingredients (such as oligopeptides of specific molecular weight and heme iron); Second, the final product is in liquid form, in which free amino acids and active ingredients are prone to degradation, aggregation, or rapid reaction with soil components and inactivation during storage and application, lacking a long-term slow-release mechanism, and there is still room for improvement in fertilizer utilization; Finally, although the process steps are clear, there is a lack of real-time monitoring and feedback control of the physical properties (such as particle size and potential) of key intermediate products (such as emulsion droplets and microcapsule precursors), resulting in insufficient consistency of product quality and insufficient controllability and intelligence of the process. Summary of the Invention

[0007] Therefore, this invention provides a method for preparing amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate, in order to overcome the problems in the prior art, such as insufficient extraction and protection of blood-derived active ingredients, lack of long-term slow-release mechanism, low controllability and intelligence of production process, resulting in low product uniformity, stability and fertilizer utilization efficiency.

[0008] To achieve the above objectives, the present invention provides a method for preparing an amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate, comprising:

[0009] Step S1: Obtain chicken blood enzymatic hydrolysis active concentrate and organic acid modified chitosan with pH buffering capacity.

[0010] Step S2: Mix the concentrated active chicken blood enzymatic hydrolysate with the ethanol solution of zein to obtain a mixture, and perform online homogenization on the obtained mixture to obtain the first aqueous phase;

[0011] Step S3: The first aqueous phase is sampled, and the first aqueous phase sample is sheared and emulsified with the oil phase to form a water / oil emulsion sample. The reference particle size is determined based on the droplet particle size distribution data of the emulsion sample. The emulsion sample is then solidified and separated into solid and liquid phases to obtain a solid protein core sample.

[0012] Step S4: Compare the particle size distribution of the solid protein core sample with the reference particle size. Based on the comparison results, dynamically adjust the shear emulsification process parameters and / or solidification process parameters of the first aqueous phase to obtain the solid protein core preform.

[0013] Step S5: The solid protein core preform is redispersed in a buffer solution with a preset pH value and sheared to obtain a protein core suspension;

[0014] Step S6: Add an anionic polyelectrolyte solution to the protein core suspension for surface pretreatment. The pretreatment process is controlled based on the Zeta potential in the reaction system to form a stable negatively charged pre-coating on the protein core surface.

[0015] Step S7: Mix the pretreated protein core with an aqueous solution containing the organic acid-modified chitosan to allow the chitosan to be adsorbed onto the surface of the protein core. Add a crosslinking agent and dynamically adjust the pH of the reaction system based on real-time pH monitoring during the crosslinking process to allow the chitosan to crosslink and solidify on the surface of the protein core, thereby obtaining a core-shell particle slurry.

[0016] Step S8: The above-mentioned core-shell particle slurry is subjected to solid-liquid separation, the solid particles are collected, washed and dried to obtain a microcapsule product with solid protein as the core and cross-linked chitosan network as the shell, which can be used to prepare amino acid water-soluble fertilizer.

[0017] Further, in step S1, a concentrated extract of chicken blood enzymatic hydrolysis activity rich in oligopeptides and heme iron is obtained, comprising:

[0018] Step S11: Collect chicken blood and perform anticoagulation treatment. After breaking the blood cells, use a complex protease for enzymatic hydrolysis. After the enzymatic hydrolysis is completed, inactivate the enzyme to obtain chicken blood hydrolysate.

[0019] Step S12: The chicken blood enzymatic hydrolysate is fractionated and separated using an ultrafiltration membrane system, and active peptide components with molecular weights in the range of 1000 Da to 5000 Da are specifically retained and collected.

[0020] Step S13: The active peptide components are concentrated under reduced pressure to obtain the chicken blood enzymatic hydrolysis active concentrate.

[0021] The complex protease includes trypsin and flavor protease.

[0022] Further, step S2 includes:

[0023] Step S21: The mixture of chicken blood enzymatic hydrolysis active concentrate and zein ethanol solution is circulated between the homogenizer and the mixing tank for homogenization.

[0024] Step S22: During the circulating flow process, the median D50 particle size and span distribution width of the mixture are monitored in real time.

[0025] Step S23: The median D50 particle size and span distribution width of the mixture are compared with the preset D50 target range and span target threshold, respectively. Based on the comparison results, the operating parameters of the online high-shear homogenizer are dynamically adjusted until the median D50 particle size is maintained within the preset D50 target range and the span distribution width is lower than the preset span target threshold, thereby obtaining the first aqueous phase.

[0026] Furthermore, in step S3, the oil phase contains a water-in-oil emulsifier; the droplet size distribution data of the emulsion sample is the D50 particle size.

[0027] Further, step S4 includes:

[0028] The first alignment result is obtained by calculating the ratio of the D50 particle size of the solid protein core to the reference particle size;

[0029] The first comparison result is compared with the stable ratio range, wherein...

[0030] If the first comparison result is within the stable ratio range, the D50 particle size of the solid protein core and the reference particle size do not meet the preset target particle size range, and the particle size distribution Span does not exceed the preset threshold, then adjust the shear rate or homogenization pressure setting value of the shear emulsification process.

[0031] If the first comparison result is greater than the upper limit of the stable ratio range, and the Span value of the particle size distribution of the solid protein core exceeds the preset threshold, then the heating rate or solvent removal rate in the early stage of curing is increased.

[0032] If the first comparison result is less than the lower limit of the stable ratio range, then reduce the temperature of the curing process or increase the system pressure.

[0033] The stable ratio range is determined based on historical process data.

[0034] Further, step S5 includes:

[0035] Step S51: The solid protein core preform is redispersed in a buffer solution with a preset pH value and sheared to form a mixed system to be dispersed.

[0036] Step S52: During the shearing process, the pH value of the mixed system is monitored in real time. When the monitored pH value deviates from the preset pH value range, an acid or alkali addition operation is triggered to perform pH correction until the pH value stabilizes within the preset pH value range.

[0037] Step S53: Monitor the turbidity of the mixture in real time to determine the dispersion uniformity, and dynamically adjust the intensity of shear dispersion based on the turbidity monitoring results to obtain a protein core suspension.

[0038] Further, step S6 includes:

[0039] Step S61: The anionic polyelectrolyte solution is continuously added to the protein core suspension at a first preset flow rate;

[0040] Step S62: Monitor the Zeta potential in the reaction system in real time and calculate the difference between it and the preset target threshold for Zeta potential;

[0041] Step S63: When the difference is less than or equal to a preset switching threshold, it is determined that the added flow rate will be switched from the first preset flow rate to the second preset flow rate, wherein the second preset flow rate is lower than the first preset flow rate.

[0042] Step S64: Continue adding at the second preset flow rate until the Zeta potential reaches the preset Zeta potential target threshold, then determine that the addition of the anionic polyelectrolyte solution is stopped.

[0043] Further, in step S7, the dynamic control includes:

[0044] The first stage involves controlling and maintaining the pH value of the system within the first pH range for a first period of time.

[0045] In the second stage, the pH value of the system is adjusted to and maintained within the second pH range for the second time period.

[0046] Wherein, any pH value within the first pH range is less than any pH value within the second pH range.

[0047] Furthermore, the organic acid-modified chitosan is citric acid-modified chitosan.

[0048] On the other hand, the present invention also provides an amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate, wherein the amino acid water-soluble fertilizer comprises core-shell structured microcapsules;

[0049] The core of the microcapsule is a solid protein containing enzymatically hydrolyzed chicken blood active ingredients, and the shell of the microcapsule is a cross-linked chitosan network.

[0050] Compared with existing technologies, the beneficial effects of this invention are as follows: Using concentrated chicken blood enzymatic hydrolysis solution as raw material, this invention overcomes the technical bottlenecks of traditional amino acid water-soluble fertilizer preparation processes, such as easy destruction of active ingredients, lack of slow-release function, and reliance on experience-based judgment. Through an integrated process of precise enzymatic hydrolysis, intelligent emulsification and solidification, online monitoring and feedback, and controllable core-shell construction, it has for the first time constructed an integrated microcapsule preparation system of "online monitoring - intelligent diagnosis - closed-loop control," producing amino acid water-soluble fertilizer microcapsules with highly uniform particle size, complete structure, and pH-responsive slow-release function. This system upgrades the traditional open-loop process to data-driven intelligent manufacturing, ensuring efficient extraction and stable encapsulation of active ingredients from the source. It fundamentally solves the batch inconsistency problem caused by fluctuations in biomass raw materials, achieving intelligent and controllable release of active ingredients in the soil. This increases fertilizer utilization by more than 50% compared to existing liquid processes, significantly improving product stability and the level of intelligent production processes, and providing a full-chain technical solution for the high-value utilization of slaughter by-products.

[0051] Furthermore, this invention utilizes a combination of enzymatic hydrolysis and ultrafiltration fractionation technology to specifically obtain a concentrated active chicken blood enzymatic hydrolysate rich in small molecule oligopeptides (1000Da-5000Da) and heme iron. This overcomes the damage to active ingredients caused by traditional acid-base methods or microbial fermentation methods, ensuring high content and high activity of functional substances.

[0052] Furthermore, this invention innovatively introduces a real-time comparison and closed-loop feedback control system for "emulsion droplet size" and "solidified protein core size" to dynamically adjust the emulsification and solidification process parameters, ensuring high uniformity of solid protein core size and batch stability, and providing a core carrier with good consistency for subsequent coating processes.

[0053] Furthermore, this invention precisely controls the anionic polyelectrolyte pretreatment process based on online monitoring of Zeta potential to form a stable pre-coating layer; combined with real-time pH monitoring to dynamically regulate the chitosan crosslinking and curing conditions, it achieves uniform, dense, and complete encapsulation of the shell layer on the core surface, significantly improving the encapsulation rate and mechanical strength of the microcapsules.

[0054] Furthermore, the microcapsules constructed in this invention with cross-linked chitosan as the shell are environmentally responsive (e.g., pH sensitive), enabling intelligent and controlled release of active ingredients (oligopeptides, heme iron) in the soil according to crop needs and environmental changes, effectively reducing nutrient loss, extending fertilizer effectiveness, and improving fertilizer utilization.

[0055] Furthermore, the present invention integrates online monitoring and automatic feedback control of multiple key parameters such as particle size, pH, zeta potential, and turbidity throughout the entire process, realizing refined, automated, and intelligent production from raw material processing to microcapsule molding, significantly improving the controllability, reproducibility, and overall efficiency of the process. Attached Figure Description

[0056] Figure 1 This is a flowchart illustrating the method for preparing amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate according to an embodiment of the present invention;

[0057] Figure 2 This is a flowchart of step S1 of the method for preparing amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate according to an embodiment of the present invention;

[0058] Figure 3 This is a flowchart of step S2 in the method for preparing amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate according to an embodiment of the present invention;

[0059] Figure 4 This is a flowchart of step S5 in the method for preparing amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate according to an embodiment of the present invention;

[0060] Figure 5 This is a flowchart of step S6 in the method for preparing amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate according to an embodiment of the present invention. Detailed Implementation

[0061] To make the objectives and advantages of the present invention clearer, the present invention will be further described below with reference to embodiments; it should be understood that the specific embodiments described herein are merely for explaining the present invention and are not intended to limit the present invention.

[0062] Preferred embodiments of the present invention will now be described with reference to the accompanying drawings. Those skilled in the art should understand that these embodiments are merely illustrative of the technical principles of the present invention and are not intended to limit the scope of protection of the present invention.

[0063] Furthermore, it should be noted that, in the description of this invention, unless otherwise explicitly specified and limited, the terms "installation," "connection," and "linking" should be interpreted broadly. For example, they can refer to a fixed connection, a detachable connection, or an integral connection; they can refer to a mechanical connection or an electrical connection; they can refer to a direct connection or an indirect connection through an intermediate medium; and they can refer to the internal connection of two components. Those skilled in the art can understand the specific meaning of the above terms in this invention according to the specific circumstances. Example

[0064] Please see Figure 1The diagram shows a flowchart of the method for preparing amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate according to the present invention. The method for preparing amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate according to an embodiment of the present invention includes:

[0065] Step S1: Obtain chicken blood enzymatic hydrolysis active concentrate and organic acid modified chitosan with pH buffering capacity.

[0066] Step S2: The concentrated active chicken blood enzymatic hydrolysate is mixed with the ethanol solution of zein to obtain a mixture. The obtained mixture is then subjected to online homogenization, and the particle size distribution of the mixture is monitored in real time. The homogenization parameters are dynamically adjusted to obtain the first aqueous phase.

[0067] Step S3: The first aqueous phase is sampled, and the first aqueous phase sample is sheared and emulsified with the oil phase to form a water / oil emulsion sample. The droplet size distribution data of the emulsion sample is monitored and recorded online in real time to determine the reference particle size. The emulsion sample is solidified and solid-liquid separation is completed to obtain a solid protein core sample.

[0068] Step S4: Compare the particle size distribution of the solid protein core sample with the reference particle size. Based on the comparison results, dynamically adjust the shear emulsification process parameters and / or solidification process parameters of the first aqueous phase. After corresponding processing, obtain the solid protein core preform.

[0069] Step S5: The solid protein core preform is redispersed in a buffer solution with a preset pH value and sheared to obtain a protein core suspension;

[0070] Step S6: Add anionic polyelectrolyte solution to the protein core suspension for surface pretreatment. The pretreatment process is controlled by real-time detection and based on the Zeta potential in the reaction system to form a stable negatively charged pre-coating on the protein core surface.

[0071] The anionic polyelectrolyte is one or more of sodium alginate, carrageenan, or polyacrylic acid.

[0072] Step S7: Mix the pretreated protein core with an aqueous solution containing the organic acid-modified chitosan to allow the chitosan to be adsorbed onto the surface of the protein core. Add a crosslinking agent and dynamically adjust the pH of the reaction system based on real-time pH monitoring during the crosslinking process to allow the chitosan to crosslink and solidify on the surface of the protein core, thereby obtaining a core-shell particle slurry.

[0073] Step S8: The above-mentioned core-shell particle slurry is subjected to solid-liquid separation, the solid particles are collected, washed and dried to obtain a microcapsule product with a solid protein core and a cross-linked chitosan network as the shell, which can be used to prepare amino acid water-soluble fertilizer.

[0074] Specifically, in step S1, a concentrated extract of chicken blood enzymatic hydrolysis activity rich in oligopeptides and heme iron is obtained, including:

[0075] Step S11: Collect chicken blood and perform anticoagulation treatment. After breaking the blood cells, use a complex protease for enzymatic hydrolysis. After the enzymatic hydrolysis is completed, inactivate the enzyme to obtain chicken blood hydrolysate.

[0076] Step S12: The chicken blood enzymatic hydrolysate is fractionated and separated using an ultrafiltration membrane system, and active peptide components with molecular weights in the range of 1000 Da to 5000 Da are specifically retained and collected.

[0077] Step S13: The active peptide components are concentrated under reduced pressure to obtain the chicken blood enzymatic hydrolysis active concentrate.

[0078] The complex protease includes trypsin and flavor protease.

[0079] It is understandable that enzymatic hydrolysis of chicken blood produces active peptides with molecular weights concentrated in the 1000-5000 Da range, which have higher absorption efficiency than large protein molecules and single amino acids. At the same time, the heme iron released by enzymatic hydrolysis is a natural organic chelated iron with high bioavailability.

[0080] Specifically, sodium citrate was added at 0.1% (w / v) of the chicken blood volume for anticoagulation. The anticoagulated blood was centrifuged at 4000 rpm for 10 minutes, and the blood cell pellet was collected and washed twice with physiological saline. The washed blood cells were then suspended in an equal volume of deionized water and placed in an ice bath. The blood cells were disrupted using an ultrasonic cell disruptor (600W power, 5 seconds on, 5 seconds off, total time 30 minutes). The pH of the disrupted cell solution was adjusted to 7.5, and a complex protease was added at 2% of the blood cell protein mass. The complex protease consisted of trypsin (enzyme activity ≥2500U / mg) and flavor protease (enzyme activity ≥500U / g) in a 1:1 mass ratio. Hydrolysis was carried out at 50℃ for 4 hours, with stirring every 30 minutes during the process. After hydrolysis, the temperature was raised to 90℃ and held for 10 minutes to inactivate the enzyme. The solution was then cooled to room temperature to obtain the chicken blood hydrolysate. Chicken blood enzymatic hydrolysate was passed through an ultrafiltration membrane system with a molecular weight cutoff of 5000 Da, operating at a pressure of 0.2–0.3 MPa and a temperature of 25°C. The retentate, i.e., the active peptide fraction with a molecular weight range of 1000 Da–5000 Da, was collected. This active peptide fraction was then placed in a rotary evaporator and concentrated under reduced pressure at a water bath of 50°C and a vacuum degree of -0.09 MPa until the solid content reached 30% (w / w), yielding a concentrated chicken blood enzymatic hydrolysate, which was then refrigerated at 4°C for later use.

[0081] Take chitosan powder with a degree of deacetylation ≥85% and viscosity ≤200 mPa·s, and slowly add it to a 1% (v / v) citric acid aqueous solution while stirring to prepare a 2% (w / v) chitosan solution. Continue stirring for 2 hours until completely dissolved, allow to stand to remove bubbles, and you will get a citric acid-modified chitosan solution with pH buffering capacity. Store at 4℃ for later use.

[0082] Specifically, step S2 includes:

[0083] Step S21: The mixture of chicken blood enzymatic hydrolysis active concentrate and zein ethanol solution is circulated between the homogenizer and the mixing tank for homogenization.

[0084] Step S22: During the circulating flow process, the median D50 particle size and span distribution width of the mixture are monitored in real time.

[0085] Step S23: The median D50 particle size and span distribution width of the mixture are compared with the preset D50 target range and span target threshold, respectively. Based on the comparison results, the operating parameters of the online high-shear homogenizer are dynamically adjusted until the median D50 particle size is maintained within the preset D50 target range and the span distribution width is lower than the preset span target threshold, thereby obtaining the first aqueous phase.

[0086] In one specific embodiment, 100g of concentrated chicken blood enzymatic hydrolysis solution was mixed with 300g of 10% (w / v) zein ethanol solution. The mixture was pumped into a circulating homogenization system consisting of an online laser particle size analyzer and a high-pressure homogenizer, the circulating homogenization system being integrated with an automated control unit. The D50 and Span values ​​of the mixture were monitored in real time. The preset target range for D50 in the control unit was D50 = 5 ± 1 μm, and the preset target threshold for Span was Span < 1.5. The standard initial process parameters of the circulating homogenization system were set as follows: feed flow rate 100 L / h, homogenization pressure 60 MPa, and single cycle processing time 2 minutes.

[0087] During the cyclic homogenization process, the control unit performs graded control based on the degree to which the D50 and Span values ​​in the mixing system deviate from the corresponding preset targets:

[0088] If the real-time monitored value is 6μm≤D50≤7μm, it is determined to be a slight exceedance. The control unit will automatically increase the homogenization pressure linearly from the current value by 10% to 20%, preferably by 15%.

[0089] If the real-time monitored D50 is greater than 7μm, it is determined to be seriously out of control. The control unit will automatically increase the homogenization pressure by 30% to 50% under the current pressure, and at the same time automatically extend the processing time of this cycle unit by 30% to 50%. Preferably, the homogenization pressure will be increased to 40%, and the processing time of this cycle unit will be automatically extended by 40%.

[0090] If the real-time monitored Span value is 1.5 ≤ Span ≤ 2.0, it is determined that the particle size distribution is slightly uneven. The control unit reduces the flow rate by 10% to 20% to improve the flow field stability of the two-phase mixture, so that the material undergoes more uniform shearing in the homogenization chamber. Preferably, the flow rate is reduced by 15%.

[0091] If the real-time monitored Span value > 2.0, it is determined that the particle size distribution is severely uneven. The control unit determines that there may be uneven feeding or poor premixing, and immediately reduces the flow rate of the feed pump by 20% to 40% to improve the uniformity of the flow field of the material entering the homogenization zone. It also automatically switches valves to return the material in the current pipeline to the pre-mixing tank and starts the high-shear dispersion device in the tank. Under the original homogenization pressure increased by 20% to 50%, it performs enhanced pre-dispersion for 30 to 90 seconds. After the pretreatment, the material is pumped back into the circulating homogenization system. The control unit temporarily increases the initial pressure setpoint of the homogenization circulation by 10% to 20% and restarts monitoring. If the Span value returns to the target range (< 1.5), the control unit automatically restores the pressure and flow rate to the preset standard initial process parameters. When the monitoring data remains stable within the target range for 30 seconds, the control unit determines that homogenization is complete and the first aqueous phase is obtained.

[0092] In this embodiment, the standard initial process parameters of the circulating homogenization system are set as follows:

[0093] Feed flow rate: 100L / h;

[0094] Homogenization pressure: 60 MPa;

[0095] Single loop processing time: 2 minutes;

[0096] Specifically, the online laser particle size analyzer initially detected a D50 of 8 μm and a Span of 2.0. After receiving the monitoring data, the control unit determined that the D50 was severely out of range and the Span was severely uneven. It then first executed a combined correction procedure for the severely uneven Span, including:

[0097] Flow rate correction: Immediately reduce the feed pump flow rate from 100L / h to 70L / h by 30%.

[0098] Reflux and enhanced pre-dispersion: The automatic switching valve refluxes all material in the pipeline back to the pre-mixing tank. The high-shear dispersion head inside the tank is activated and runs for 60 seconds at an equivalent intensity 40% higher than the current homogenization pressure (60MPa) (i.e., 84MPa).

[0099] Parameter Reset and Restart Monitoring: After pre-dispersion, the material is pumped back into the circulating homogenization system at a flow rate of 70 L / h. The control unit temporarily increases the initial homogenization pressure setpoint of this circulating unit by 15% to 69 MPa and restarts real-time monitoring.

[0100] After completing the Span calibration cycle, the control unit continues to adjust the D50 value:

[0101] After reflux pretreatment, the re-monitored D50 value decreased to 7.2 μm, and the Span value decreased to 1.8. At this point, D50 was still severely out of range, so the system automatically increased the homogenization pressure from 69 MPa by 40% to approximately 97 MPa, and extended the originally planned 2-minute cycle time by 50% to 3 minutes. After increasing the pressure to 100 MPa and running for approximately 1.5 minutes, the monitoring data showed D50 = 4.9 μm and Span = 1.4, and this data remained stable for more than 30 seconds. The control unit determined that homogenization was complete, automatically gradually reduced the homogenization pressure to the standard value of 60 MPa, and restored the feed flow rate to 100 L / h.

[0102] Once the first aqueous phase is obtained, proceed to the next step S3.

[0103] It is understandable that the specific control ratios, timing, and thresholds mentioned above can also be preset based on historical production data or optimized by the control unit through self-learning.

[0104] The first aqueous phase (temperature approximately 25°C) and soybean oil containing 2.0% (w / w) Span-80 (oil phase) were separately pumped into an online high-shear emulsifier (set speed 10000 rpm) via precision metering pumps at a flow rate of water phase:oil phase = 1:9 (volume ratio). During emulsification, the particle size distribution of the emulsion droplets was monitored and recorded in real time using an online laser particle size analyzer integrated into the emulsifier's outlet pipeline. The control unit was set to take the average value of three consecutive samples (5-second intervals) with a D50 value fluctuation of less than ±0.3 μm as the "reference particle size" for that batch.

[0105] In this embodiment, the recorded reference particle size D1 = 7.5 μm.

[0106] Subsequently, the W / O emulsion was transferred to a temperature-controlled vacuum distillation apparatus for solidification. The solidification conditions were set as follows: Stage 1: 40℃, -0.08MPa, heating rate 4℃ / min; Stage 2: 45℃, -0.09MPa, maintained until the endpoint. The solidification progress was monitored using an online viscometer. When the system viscosity ceased to change and entered a plateau phase, the system automatically determined this as the solidification endpoint. A disc centrifuge was then used for solid-liquid separation, and the wet solid protein cores were collected. A small sample of the wet solid protein cores was washed with anhydrous ethanol, and its particle size distribution was analyzed using an offline laser particle size analyzer (Malvin Mastersizer 3000).

[0107] In one specific embodiment, the D50 particle size of the solid protein core was measured to be D2=7.0μm and Span=1.4.

[0108] Specifically, step S4 includes:

[0109] The first alignment result R is obtained by calculating the ratio of the D50 particle size of the solid protein core to the reference particle size;

[0110] The first comparison result is compared with the stable ratio range, wherein...

[0111] If R is within the stable ratio range, the D50 particle size of the solid protein core and the reference particle size do not meet the preset target particle size range, and the particle size distribution Span does not exceed the preset threshold, then adjust the shear rate or homogenization pressure setting value of the shear emulsification process.

[0112] If R is greater than the upper limit of the stable ratio range and the Span value of the solid protein core particle size distribution exceeds the preset threshold, then the heating rate or solvent removal rate in the initial stage of curing is increased.

[0113] If R is less than the lower limit of the stable ratio range, then reduce the curing temperature or increase the system pressure.

[0114] The stable ratio range is determined based on historical process data.

[0115] The target particle size range preset by the control unit is: D0 = 8.0 μm ± 0.1 μm, and the preset threshold of Span is: 1.6;

[0116] In this embodiment, the particle size D2 of the solid protein core sample is compared with the reference particle size D1, and the first alignment result R is calculated:

[0117] R = D2 / D1 = 7.0 / 7.5 ≈ 0.933

[0118] The system queries the historical qualified batch database and finds that the normal fluctuation range of the curing shrinkage coefficient K is 0.94±0.03 (i.e. 0.91-0.97), which is also the stable ratio range. The current R value (0.933) falls within this range.

[0119] Diagnostic results: The curing process was stable (R value normal), Span = 1.4 < 1.6, but D1 and D2 were both below the preset target particle size range D0 = 8.0 μm ± 0.1 μm. The control unit directly generated process instructions and issued them to the emulsification equipment based on internal compensation adjustments. The speed setting of the high-shear emulsifier was increased from the current 10,000 rpm to 11,000 rpm, or the operating pressure setting of the high-pressure homogenizer was increased from 60 MPa to 65 MPa. This adjustment aimed to enhance the shear force to increase the reference particle size D1 of the subsequent emulsion droplets, so that the D2 obtained after curing would approach the total target D0. After adjustment, retesting showed that the solid protein core particle size D2 = 7.9 μm and the reference particle size D1 = 7.95 μm, which was verified as qualified. Using the process parameters, the corresponding shear emulsification and curing treatment in step S3 was performed on all the first aqueous and oil phases to obtain a solid protein core preform with qualified particle size distribution.

[0120] Specifically, step S5 includes:

[0121] Step S51: The solid protein core preform is redispersed in a buffer solution with a preset pH value and sheared to form a mixed system to be dispersed.

[0122] Step S52: During the shearing process, the pH value of the mixed system is monitored in real time. When the monitored pH value deviates from the preset pH value range, an acid or alkali addition operation is triggered to perform pH correction until the pH value stabilizes within the preset pH value range.

[0123] Step S53: Monitor the turbidity of the mixture in real time to determine the dispersion uniformity, and dynamically adjust the intensity of shear dispersion based on the turbidity monitoring results to obtain a protein core suspension.

[0124] In this embodiment, the wet solid protein core preform was added to a 0.1M citrate buffer solution at pH 5.0 at a solid content of 10% (w / v). The stirring and dispersion system equipped with an online pH meter and turbidimeter was started at an initial speed of 800 rpm.

[0125] When the pH value deviates from 5.0 ± 0.1, the linked automatic acid-base metering pump (containing 0.5M citric acid and 0.5M NaOH respectively) will add the corresponding solutions in a pulse manner, usually correcting the pH back to the set range within 10 seconds. In one specific embodiment, the system detected an initial pH of 5.2, and after automatically adding citric acid for 3 seconds, the pH stabilized at 5.0.

[0126] The online turbidimeter (measurement range 0-1000 NTU) showed that the initial turbidity rapidly increased to 250 NTU, then entered a slow increase phase with fluctuations of ±15 NTU. The system determined that the dispersion was not uniform and automatically increased the stirring speed in steps: first, it increased to 1200 rpm for 1 minute, at which point the turbidity rose to 280 NTU, but the fluctuations did not decrease; then it increased to 1500 rpm for 2 minutes, at which point the turbidity stabilized at a plateau of 300 ± 5 NTU. The system determined that the dispersion was now uniform, obtaining a protein core suspension, and automatically adjusted the stirring speed back to the maintenance setting of 1000 rpm, obtaining a homogeneous protein core suspension.

[0127] Specifically, step S6 includes:

[0128] Step S61: The anionic polyelectrolyte solution is continuously added to the protein core suspension at a first preset flow rate;

[0129] Step S62: Monitor the Zeta potential in the reaction system in real time and calculate the difference between it and the preset target threshold for Zeta potential;

[0130] Step S63: When the difference is less than or equal to a preset switching threshold, it is determined that the added flow rate will be switched from the first preset flow rate to the second preset flow rate, wherein the second preset flow rate is lower than the first preset flow rate.

[0131] Step S64: Continue adding at the second preset flow rate until the Zeta potential reaches the preset Zeta potential target threshold, then determine that the addition of the anionic polyelectrolyte solution is stopped.

[0132] Specifically, the anionic polyelectrolyte solution is one or more of sodium alginate, carrageenan, or polyacrylic acid;

[0133] In this embodiment, a 0.5% (w / v) sodium alginate (SA) solution is added to the protein core suspension at a uniform rate. The system's preset key parameters are:

[0134] Target Zeta potential threshold (ζ0): -35mV;

[0135] Switching threshold (ζ): -31.5mV (i.e., 90% of ζ0);

[0136] First preset flow rate (V1): 5 mL / min;

[0137] Second preset flow rate (V2): 1 mL / min;

[0138] Initial stage: SA solution was added at a rate of V1 (5 mL / min), and the online Zeta potentiometer showed that the potential shifted rapidly to negative from +20 mV.

[0139] Flow rate switching: When the potential drops to -31mV (below the switching threshold ζ-30mV), the system automatically switches the feeding flow rate from V1 to V2 (1mL / min).

[0140] Endpoint determination: Continue adding at V2, the potential slowly changes to -35mV and remains stable at this value for 60 seconds. The system automatically stops adding SA solution.

[0141] By controlling the flow rate gradient with "fast approximation and slow fine-tuning", a dense negatively charged pre-coating with a stable zeta potential of -35±1mV is finally formed on the surface of the protein core.

[0142] Specifically, in step S7, the protein core suspension with a stable negatively charged pre-coating is mixed with a pre-prepared 2% (w / v) citric acid-modified chitosan solution at a volume ratio of 1:2. Electrostatic adsorption is then performed at 25°C for 30 minutes with gentle stirring (200 rpm). During this process, positively charged chitosan molecules tightly adhere to the negatively charged protein core surface through electrostatic forces, forming the initial shell.

[0143] After adsorption is complete, 0.5% (w / v) of genipin aqueous solution is slowly added to the system as a crosslinking agent. The amount of genipin added is 20% of the chitosan mass. The crosslinking reaction is initiated, and the core "programmed pH gradient crosslinking control" is executed.

[0144] The control process is as follows:

[0145] Phase 1 (Initial Network Construction):

[0146] The system monitors the pH in real time using an online pH meter and controls an automatic titration pump (containing 0.1M HCl solution) to add micro-volume amounts, precisely stabilizing the pH of the reaction system within the range of 5.2±0.05 for 25 minutes.

[0147] Understandably, in this weakly acidic environment, the chitosan molecular chains are fully extended and have good solubility. The cross-linking agent genipin can fully penetrate and react with the amino groups on the chitosan molecules to form a Schiff base reaction, initially forming a relatively loose and extended three-dimensional network structure, thus ensuring the integrity of the shell.

[0148] Phase Two (Network Contraction Strengthening Period):

[0149] After the first stage, the system automatically switches control programs. A reverse fine-tuning process is performed using an automatic titration pump (containing 0.1M NaOH solution), smoothly raising the system pH from 5.2 to 6.5 within 5 minutes, and then stabilizing it at 6.5 ± 0.1 for 50 minutes.

[0150] Understandably, a near-neutral environment leads to a decrease in the solubility of chitosan molecular chains and an increase in the hydrogen bonding between molecular chains, causing the initially cross-linked network structure to physically shrink and become more compact. This stage further consolidates the cross-linking points, making the shell more dense and increasing its mechanical strength, thereby achieving superior sustained-release performance and physical stability.

[0151] Once the total cross-linking time (75 minutes) is reached, the system automatically stops temperature and pH control, and the resulting product is a core-shell particle slurry with a protein core and a gradient cross-linked chitosan shell.

[0152] The core-shell particle slurry obtained in step S7 was transferred to a tubular high-speed centrifuge and centrifuged at 8000 rpm for 10 minutes to achieve solid-liquid separation. The supernatant was discarded. To remove residual cross-linking agent, salt, and unreacted chitosan, the collected wet filter cake was subjected to a three-stage countercurrent wash with deionized water: three times the volume of deionized water was added each time, and the mixture was redispersed and centrifuged again. The washing endpoint was determined by detecting the conductivity of the washing solution; when the conductivity was below 20 μS / cm, the washing was considered successful. The washed wet microcapsule filter cake was transferred to a tray in a vacuum freeze dryer and spread into a thin layer. The following freeze-drying procedure was performed:

[0153] Prefreeze to -40°C and hold for 2 hours;

[0154] Main drying: With the condenser temperature below -55℃ and the vacuum degree below 10Pa, the shelf temperature is slowly raised from -40℃ to 0℃ over a period of 20 hours.

[0155] Drying: Raise the shelf temperature to 25°C and maintain it for 8 hours;

[0156] The final product is a dry, free-flowing, pale yellow to light brown microcapsule powder with a moisture content of less than 5% (w / w).

[0157] It is understood that the obtained microcapsule product can be used directly as an amino acid water-soluble fertilizer product, or the obtained microcapsule product can be physically mixed with an agriculturally acceptable carrier (including urea, potassium dihydrogen phosphate, potassium sulfate and a small amount of dispersant, wetting agent, etc.) at a mass ratio of 1:9 to obtain the final amino acid water-soluble fertilizer product of the present invention. Example

[0158] Unlike Example 1, in step S3, after emulsifying the first aqueous phase and the oil phase, the D50 reference particle size of the emulsion droplets was recorded online as D1 = 8.0 μm (consistent with the target). Subsequently, a solidification process was performed and the mixture was separated to obtain a solid protein core. A small amount of the wet solid protein core sample was taken, washed with anhydrous ethanol, and its particle size distribution was detected using an offline laser particle size analyzer, yielding: D2 = 9.6 μm, Span = 1.8.

[0159] The calculated ratio R = D2 / D1 = 9.6 / 8.0 = 1.20. According to the historical database, the normal range of the curing shrinkage coefficient K is still 0.91-0.97. The current R value (1.20) is much higher than the upper limit of the range. D2 (9.6μm) > D1 (8.0μm), and Span = 1.8 > 1.6. It can be determined that in the early stage of curing, before the emulsion droplets were completely cured and shaped, collisions and mergers occurred between droplets, resulting in larger and wider particle distribution.

[0160] The control unit will adjust the curing process parameters of the subsequent materials to be cured in real time, increasing the heating rate of the material from room temperature to the first stage curing temperature (40℃) by 30% to a rate of 5.2℃ / min, or instantly increasing the system vacuum from -0.08MPa to -0.095MPa within the first 5 minutes of curing to accelerate the initial evaporation rate of ethanol and promote the rapid formation of a solid skin on the surface of the droplets.

[0161] The adjusted curing procedure was applied to subsequent materials in this batch. The control unit will perform particle size detection and diagnosis again after the subsequent unit completes the curing and separation. After adjustment, the re-detection showed that the solid protein core particle size D2 = 7.95 μm and the reference particle size D1 = 8.0 μm, which was verified as qualified. Example

[0162] Unlike Example 1, in step S3, after emulsifying the first aqueous phase and the oil phase, the D50 reference particle size of the emulsion droplets was recorded online as D1 = 8.0 μm (consistent with the target). Subsequently, a solidification process was performed and the mixture was separated to obtain a solid protein core. A small amount of the wet solid protein core sample was taken, washed with anhydrous ethanol, and its particle size distribution was detected using an offline laser particle size analyzer, yielding: D2 = 6.5 μm, Span = 1.5.

[0163] The calculated ratio R = D2 / D1 = 6.5 / 8.0 = 0.81. A search of the historical database shows that the normal range for the curing shrinkage coefficient K is still 0.91-0.97. The current R value (0.81) < 0.91, and D2 (6.5 μm) < D1 (8.0 μm), indicates that during the curing process, excessive driving force (such as excessively high temperature, excessive vacuum, or excessively long time) caused the solvent (ethanol) to be removed too quickly. This resulted in the zein network experiencing excessive shrinkage stress during curing, ultimately forming particles that are too small.

[0164] The control unit will adjust the curing process parameters of the subsequent materials to be cured in real time, and reduce the curing temperature: lower the constant temperature of the second stage from 45℃ to 40℃, or adjust the system vacuum from -0.09MPa to -0.07MPa, so as to reduce the solvent evaporation rate.

[0165] The adjusted curing procedure was applied to subsequent materials in this batch. The control unit will perform particle size detection and diagnosis again after the subsequent unit completes the curing and separation. After adjustment, the re-detection showed that the solid protein core particle size D2 = 7.96 μm and the reference particle size D1 = 8.0 μm, which was verified as qualified.

[0166] Comparative Example 1:

[0167] The same formulation as in Example 1 was used, but all online monitoring and feedback control were eliminated during the preparation process, and the operation was carried out solely based on fixed process parameters and experience time.

[0168] Step S2: After mixing the chicken blood enzymatic hydrolysate concentrate with the zein ethanol solution, the mixture was homogenized in a high-pressure homogenizer at a fixed pressure of 60 MPa for 5 minutes without any online particle size monitoring or parameter adjustment.

[0169] Step S3: Emulsify the first aqueous phase and the oil phase containing the emulsifier at a constant speed of 10,000 rpm for 3 minutes. Then, fix the emulsion at 45°C and -0.09 MPa for 40 minutes, without monitoring the endpoint using online viscosity or process analysis techniques.

[0170] Step S4: Fix the protein core in pH 5.0 buffer and disperse at 1000 rpm for 5 minutes without online pH and turbidity monitoring.

[0171] Step S5: Add 50 mL of 0.5% sodium alginate solution to the protein core suspension. There is no Zeta potential monitoring. The feeding rate and endpoint are controlled by experience.

[0172] Step S6: After adding the crosslinking agent, crosslink at a fixed pH of 6.0 and a fixed temperature for 60 minutes without programmed pH gradient control.

[0173] Comparative Example 2:

[0174] A water-soluble fertilizer containing amino acids was prepared according to the method described in Example 1 of CN119241301A.

[0175] Parallel comparative tests were conducted on Embodiments 1, 2, and 3 of the present invention and Comparative Examples 1 and 2. The results are shown in Table 1.

[0176] Table 1 Comparison of Performance Test Data

[0177] Test Project Example 1 Example 2 Example 3 Comparative Example 1 (fixed parameters, no feedback) Comparative Example 2 (CN119241301A) Average particle size of microcapsules (μm) 7.9 7.95 7.96 12.5 Liquid products Particle size distribution Span value 1.4 1.5 1.5 2.8 / Encapsulation rate (%) 92.5 91.8 92.1 78.3 / 7-day cumulative release rate (%) 35.2 36.0 34.8 68.5 85.2 (Liquid, no sustained release) 28-day cumulative release rate (%) 85.0 84.5 85.2 95.0 98.0 (Mostly fully released) inter-batch particle size variation coefficient (%) 3.2 3.5 3.4 18.7 / Storage stability (3-month activity retention rate %) 95.6 94.8 95.2 82.1 75.3 Fertilizer utilization rate (pot experiment, %) 68.5 67.9 68.2 45.2 38.5

[0178] As shown in the table above, this invention, through the integration of real-time monitoring, intelligent feedback, and programmed control, achieves the integrity of the microcapsule structure and uniformity of particle size (particle size 7.9–8.0 μm in the examples, Span ≤ 1.5), significantly improving the encapsulation efficiency to over 91%, and possessing ideal sustained-release characteristics (release rate of approximately 35% at 7 days and approximately 85% at 28 days). The batch-to-batch particle size variation coefficient is less than 3.5%, the activity retention rate exceeds 94% after 3 months, and the fertilizer utilization rate reaches approximately 68% in pot experiments, all significantly better than Comparative Example 1 (encapsulation efficiency 78.3%, utilization rate 45.2%) without real-time control and Comparative Example 2 (no sustained release, utilization rate 38.5%) using the existing liquid process. The results indicate that this invention, while improving product uniformity, stability, sustained-release performance, and fertilizer utilization efficiency, achieves intelligent and controllable production throughout the entire process, overcoming the problems of easy loss of active ingredients, poor batch consistency, and low nutrient utilization rate in traditional processes.

[0179] The technical solution of the present invention has been described above with reference to the preferred embodiments shown in the accompanying drawings. However, it will be readily understood by those skilled in the art that the scope of protection of the present invention is obviously not limited to these specific embodiments. Without departing from the principles of the present invention, those skilled in the art can make equivalent changes or substitutions to the relevant technical features, and the technical solutions after these changes or substitutions will all fall within the scope of protection of the present invention.

Claims

1. A method for preparing an amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate, characterized in that, include: Step S1: Obtain chicken blood enzymatic hydrolysis active concentrate and organic acid modified chitosan with pH buffering capacity, wherein the organic acid modified chitosan is citric acid modified chitosan. Step S2: The concentrated active chicken blood enzymatic hydrolysate is mixed with the ethanol solution of zein to obtain a mixture. The obtained mixture is then subjected to online homogenization, and the particle size distribution of the mixture is monitored in real time. The homogenization parameters are dynamically adjusted to obtain the first aqueous phase. Step S3: The first aqueous phase is sampled, and the first aqueous phase sample is sheared and emulsified with the oil phase to form a water / oil emulsion sample. The droplet size distribution data of the emulsion sample is monitored and recorded online in real time to determine the reference particle size. The emulsion sample is solidified and solid-liquid separation is completed to obtain a solid protein core sample. Step S4: Compare the particle size distribution of the solid protein core sample with the reference particle size. Based on the comparison result, dynamically adjust the shear emulsification process parameters and / or solidification process parameters of the first aqueous phase. After corresponding processing, obtain the solid protein core preform, including... The first alignment result R is obtained by calculating the ratio of the D50 particle size of the solid protein core to the reference particle size; The first comparison result R is compared with the stable proportion range, wherein... If R is within the stable ratio range, the D50 particle size of the solid protein core and the reference particle size do not meet the preset target particle size range, and the particle size distribution Span does not exceed the preset threshold, then adjust the shear rate or homogenization pressure setting value of the shear emulsification process. If R is greater than the upper limit of the stable ratio range and the Span value of the solid protein core particle size distribution exceeds the preset threshold, then the heating rate or solvent removal rate in the initial stage of curing is increased. If R is less than the lower limit of the stable ratio range, then reduce the curing temperature or increase the system pressure. The stable ratio range is determined based on historical process data; Step S5: The solid protein core preform is redispersed in a buffer solution with a preset pH value and sheared to obtain a protein core suspension; Step S6: Add an anionic polyelectrolyte solution to the protein core suspension for surface pretreatment. The pretreatment process is controlled by real-time detection and based on the Zeta potential in the reaction system to form a stable negatively charged pre-coating on the protein core surface. The anionic polyelectrolyte solution is one or more of sodium alginate, carrageenan, or polyacrylic acid. Step S7: Mix the pretreated protein core with an aqueous solution containing the organic acid-modified chitosan to allow the chitosan to be adsorbed onto the surface of the protein core. Add a crosslinking agent and dynamically adjust the pH of the reaction system based on real-time pH monitoring during the crosslinking process to allow the chitosan to crosslink and solidify on the surface of the protein core, thereby obtaining a core-shell particle slurry. Step S8: The above-mentioned core-shell particle slurry is subjected to solid-liquid separation, the solid particles are collected, washed and dried to obtain a microcapsule product with a solid protein core and a cross-linked chitosan network as the shell, which can be used to prepare amino acid water-soluble fertilizer.

2. The method for preparing amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate according to claim 1, characterized in that, In step S1, a concentrated enzymatic hydrolysate of chicken blood rich in oligopeptides and heme iron is obtained, comprising: Step S11: Collect chicken blood and perform anticoagulation treatment. After breaking the blood cells, enzymatic hydrolysis is performed using a complex protease. After the enzymatic hydrolysis is completed, the enzyme is inactivated to obtain chicken blood hydrolysate. Step S12: The chicken blood enzymatic hydrolysate is fractionated and separated using an ultrafiltration membrane system, and active peptide components with molecular weights in the range of 1000 Da to 5000 Da are specifically retained and collected. Step S13: The active peptide components are concentrated under reduced pressure to obtain the chicken blood enzymatic hydrolysis active concentrate. The complex protease includes trypsin and flavor protease.

3. The method for preparing amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate according to claim 1, characterized in that, Step S2 includes: Step S21: The mixture of chicken blood enzymatic hydrolysis active concentrate and zein ethanol solution is circulated between the homogenizer and the mixing tank for homogenization. Step S22: During the circulating flow process, the median D50 particle size and span distribution width of the mixture are monitored in real time. Step S23: The median D50 particle size and span distribution width of the mixture are compared with the preset D50 target range and span target threshold, respectively. Based on the comparison results, the operating parameters of the online high-shear homogenizer are dynamically adjusted until the median D50 particle size is maintained within the preset D50 target range and the span distribution width is lower than the preset span target threshold, thereby obtaining the first aqueous phase.

4. The method for preparing amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate according to claim 3, characterized in that, In step S3, the oil phase contains a water-in-oil emulsifier; The droplet size distribution data of the emulsion sample is the D50 particle size.

5. The method for preparing amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate according to claim 1, characterized in that, Step S5 includes: Step S51: The solid protein core preform is redispersed in a buffer solution with a preset pH value and sheared to form a mixed system to be dispersed. Step S52: During the shearing process, the pH value of the mixed system is monitored in real time. When the monitored pH value deviates from the preset pH value range, an acid or alkali addition operation is triggered to perform pH correction until the pH value stabilizes within the preset pH value range. Step S53: Monitor the turbidity of the mixture in real time to determine the dispersion uniformity, and dynamically adjust the intensity of shear dispersion based on the turbidity monitoring results to obtain a protein core suspension.

6. The method for preparing amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate according to claim 1, characterized in that, Step S6 includes: Step S61: The anionic polyelectrolyte solution is continuously added to the protein core suspension at a first preset flow rate; Step S62: Monitor the Zeta potential in the reaction system in real time and calculate the difference between it and the preset target threshold for Zeta potential; Step S63: When the difference is less than or equal to a preset switching threshold, it is determined that the added flow rate will be switched from the first preset flow rate to the second preset flow rate, wherein the second preset flow rate is lower than the first preset flow rate. Step S64: Continue adding at the second preset flow rate until the Zeta potential reaches the preset Zeta potential target threshold, then determine that the addition of the anionic polyelectrolyte solution is stopped.

7. The method for preparing amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate according to claim 1, characterized in that, In step S7, the dynamic control includes: The first stage involves controlling and maintaining the pH value of the system within the first pH range for a first period of time. In the second stage, the pH value of the system is adjusted to and maintained within the second pH range for the second time period. Wherein, any pH value within the first pH range is less than any pH value within the second pH range.

8. An amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate, prepared by the method for preparing amino acid water-soluble fertilizer based on chicken blood enzymatic hydrolysate according to any one of claims 1-7, characterized in that, The amino acid water-soluble fertilizer includes core-shell structured microcapsules; The core of the microcapsule is a solid protein containing enzymatically hydrolyzed chicken blood active ingredients, and the shell of the microcapsule is a cross-linked chitosan network.

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