Method for improving quality of boneless chicken feet by adopting 60Co gamma ray irradiation

Abstract

The invention relates to a method for improving the quality of boneless chicken feet by adopting 60Co gamma ray irradiation, which comprises the following steps: pretreating the boneless chicken feet, and constructing a conformational prestress area with elastic residual tension in the tissue structure of the chicken feet in a manner of combining micro traction with low-temperature standing, so as to provide a structural tension guide basis for the irradiation process; on the basis of the conformational pre-stress area, 60Co gamma rays are applied, the irradiation dose is controlled between 2 kGy and 10 kGy, and a dynamic staggered cracking area is formed by inducing non-uniform energy distribution, so that directional cracking and reaction sites are exposed and reentangled in collagen and elastin chain segments, the tissue structure is remodeled, and the chewing elasticity is enhanced; according to the method, a protein chain segment directional reconstruction mechanism is constructed, a microscopic conformation forming path is controlled, and the interface structure regulation and control and flavor progressive release system is combined, so that multiple improvements on the tissue elasticity, the taste resilience, the flavor expressive force and the storage and transportation stability of the chicken feet are realized.

Description

TECHNICAL FIELD

[0001] The present application relates to a method for improving the quality of boneless chicken feet, in particular to a method for improving the quality of boneless chicken feet by 60Co gamma ray irradiation. BACKGROUND

[0002] On the basis of the comparative document CN101856130A, a kind of irradiation processing technology of sansho chicken feet, although the patent provides a relatively systematic chicken irradiation preservation scheme, it is indeed effective exploration in quality safety, microorganism control and irradiation process parameter optimization, but its overall technical scheme still has many limitations for basic sterilization and quality preservation rather than structure and flavor improvement, especially lacks the support of in-depth technical system in the direction of high-end food processing, taste experience optimization, structure reconstruction and sensory flavor improvement. The following will expound the deficiencies and disadvantages of the comparative document in the target of the method for improving the quality of boneless chicken feet by 60Co gamma ray irradiation from the depth of technical path, protein conformation regulation ability, flavor structure design, irradiation mechanism utilization rate, product adaptability and other aspects.

[0003] The comparative document focuses on the macro parameter control of the irradiation process, such as the selection standard, irradiation dose time, irradiation box movement mode, full automatic control, etc. The core starting point is still to control the total number of microorganisms, reduce the risk of bag swelling, and prolong the shelf life. It is essentially an optimization scheme of fresh-keeping sterilization process, rather than a microscopic structure regulation and multi-dimensional flavor construction for quality improvement of chicken feet itself. This method does not involve the conformational change, chain rearrangement behavior or structure stability control of chicken feet protein chain segments under irradiation induction. It lacks intervention in the reconstruction mechanism of protein damage, denaturation or chain rupture during irradiation process, and therefore cannot systematically improve the chewy elasticity and taste rebounding feeling of chicken feet in texture performance. It only has a surface fresh-keeping effect. Secondly, the reference document does not describe any control mechanism of free radicals and side reaction chains induced by irradiation. It is known that under the action of 60Co gamma rays, high-reactivity species such as hydroxyl radicals and superoxide anions will be generated inside the meat product. These species are prone to induce reactions such as lipid oxidation, amino acid degradation, aromatic skeleton rupture, etc., forming flavor isomerization byproducts and off-flavor substances (such as aldehydes, alcohols, carbonyl volatiles). The comparative document only reduces the amount of preservative added as a process advantage, but does not set any free radical reaction control or flavor retention means, resulting in a natural gap in flavor control, which cannot meet the current consumer demand for flavor authenticity and taste restoration. Furthermore, the comparative process completely ignores the secondary and tertiary structures of chicken feet protein, and does not propose any microstructure intervention techniques such as cooling induction, pre-stress application, pseudo-conformation control, helical conformation induction, etc. This makes it impossible to form a stable rebounding conformation based on irradiation chain rupture. The present invention can precisely intervene in the rearrangement path of protein chain segments by setting a conformation pre-stress zone, helical path air disturbance, pseudo-helical conformation induction and beta-sheet blocking mechanism, while ensuring the stability of thermal response, it also improves the chain segment memory and mechanical consistency after cooling, ultimately significantly enhances the structure-flavor coupling degree of chicken feet. This deep structure-driven taste strategy is completely missing in the comparative document. In addition, there is no exclusive solution for water storage capacity and reheating response control. The comparative document improves the antibacterial property of the product through irradiation, but ignores the problem of water structure damage and protein-water binding force reduction caused by the irradiation process, resulting in serious flavor loss and water loss during reheating. The present invention constructs a ray-induced water storage microcavity structure and implants a heat-sensitive response platform, which can release flavor peptide segments and fatty acid complexes in stages during reheating, forming a sense of hierarchy of freshness before and aroma after. At the same time, through the secondary thermal closure mechanism of the microcavity wall structure, residual flavor droplets can still be released during the second heating, significantly improving the flavor stability and product performance tension under multiple heating conditions.

[0004] In addition, the prior art does not consider the shielding or interference effect of the protein chain structure after irradiation on the natural flavor, nor does it provide any interface synergistic material to stabilize the adhesion between the segments. The present application introduces natural polysaccharides such as locust bean gum to construct a hydrophilic-hydrophobic alternating protein-polysaccharide interface system, and adds a wetting regulator and a heat-sensitive polymer to improve the flexibility of the bridging structure and the interface adhesion, thereby not only enhancing the transportation stability of the chicken skin roll colloidal system, but also enhancing the retention ability of flavor ingredients. By comparison, the reference scheme is more suitable for low-cost industrial mass sterilization processing, but not for flavor construction and high taste requirements of high-end prepared products or functional meat products. SUMMARY

[0005] The purpose of the present application is to provide a method for improving the quality of boneless chicken skin rolls by 60Co gamma ray irradiation, thereby solving some of the problems and deficiencies pointed out in the background art.

[0006] The present application solves the above-mentioned technical problems by adopting the following technical scheme:

[0007] The boneless chicken skin roll is pretreated by a slight pulling combined with low-temperature standing to construct a conformational prestressed zone with elastic residual tension in the chicken skin roll tissue structure, thereby providing a structural tension guiding basis for the irradiation process; on the basis of the conformational prestressed zone, 60Co gamma rays are applied, and the irradiation dose is controlled between 2-10 kGy, a dynamic staggered cleavage zone is formed by inducing non-uniform energy distribution, so as to expose the reaction sites and re-tangle in the collagen and elastin segments, thereby remodeling the tissue structure and enhancing the chewing elasticity;

[0008] During the irradiation process, the exposed protein active sites are guided to form a transient complex structure with the free radicals or excited state molecules generated by irradiation, so as to limit the migration and diffusion of free radicals, and block the lipid and amino acid side reaction path, thereby preventing the generation of flavor isomerization byproducts;

[0009] After the irradiation is completed, the chicken skin roll is subjected to low-temperature slow cooling treatment, and the environmental pH is adjusted to 3.89-5.34, so as to induce the re-arrangement of part of the collagen segments to form a secondary pseudo-conformational structure of spiral shape, thereby improving the rebound elasticity and structural memory of the taste; during the cooling induction process, non-covalent interaction occurs between the protein chains and natural polysaccharides in the chicken skin roll, a bridging structure formed by irradiation is constructed, and a water storage type microcavity structure is formed in the tendon connection area.

[0010] As a preferred embodiment, a periodic pulse stress disturbance is applied simultaneously in the step of slight pulling combined with low-temperature standing, for breaking the natural transverse stress distribution in the muscle fiber; in the step of 60Co gamma ray irradiation, a controllable reflection shield is arranged outside the conformational prestressed zone, so that the main ray direction forms a non-perpendicular angle with the protein main chain arrangement direction, thereby enhancing the directional breaking tendency of the protein chain.

[0011] As preferred, the 60Co γ-ray irradiation stage is set with an alternating energy window cycle to cause phase shift of the protein chain reconstruction process, thereby improving the controllable re-entanglement rate of the cleavage zone; and the 60Co γ-ray irradiation is forward injected with a mild protein chain polarizer including a weak electrolytic polypeptide, for strengthening the main chain directionality.

[0012] As preferred, the complex structure is set to undergo a metastable complex reaction with part of the protein residues after formation, and releases a flavor precursor peptide segment during the cooling stage, so as to generate flavor and structure in cooperation; while limiting the diffusion of free radicals, an oxygen-inhibiting film is set to cover the surface of the chicken feet, thereby blocking the lipid oxidation path induced by oxygen participation.

[0013] As preferred, the low-temperature slow cooling process adopts a spiral path air cooling technology, and a spiral guide structure is set to the air flow guide to make the cooling air flow along the surface and circumference of the chicken feet in a spiral path, so as to apply directional shear disturbance in the protein chain segment cooling-induced rearrangement process, thereby promoting the formation and stabilization of the secondary pseudo-conformation structure of the spiral-like structure; and the environmental pH of 3.89-5.34 is realized by adding a weak buffer type plant acid liquid including malic acid buffer.

[0014] As preferred, in the protein chain cooling-induced rearrangement process, a natural polymer (including locust bean gum) having protein and polysaccharide interface activity, a spontaneous β-sheet breaker, and a heat-sensitive responsive microcavity structure are introduced in cooperation, and a spiral path air flow system and pulse excitation parameters are set to realize the stable formation and reheat flavor release control of the pseudo-conformation structure of the spiral-like structure. The conformation formation stability factor may be quantified by the following expression:

[0015]

[0016] In the above formula, the variables include a polymer synergy coefficient ( ), a breaker binding density ( ), a heat-sensitive microcavity response coefficient ( ), and a cooling disturbance shear strength ( ) key parameters, which establish a coupling mathematical relationship between the spiral-like conformation formation and the multi-factor technical path, for guiding the process control parameter optimization and flavor release behavior prediction.

[0017] Among them:

[0018] is the stability factor of the finally formed spiral-like pseudo-conformation (0-1), which is used to quantify whether the structure is formed and stably exists; The concentration coefficient of the added synergistic interfacial active polymer (such as locust bean gum) is used to positively enhance the conformational stability of the protein-polysaccharide bridging region. This is the binding site distribution density function for β-sheet blockers, used to describe their uniformity in protein segments; The polarity fit index of the folding blocker molecule determines whether its blocking efficiency is good; The response sensitivity coefficient of the water storage microcavity structure to temperature excitation reflects the fitting index between its release behavior and temperature. T is the temperature difference amplitude (unit: K) set in the pulsed thermistor excitation, which reflects whether the reheating process provides sufficient driving force; The nonlinear response factor (empirical fit index, usually between 1 and 2) for microcavity release behavior is obtained from flavor release curve analysis; The cooling rate influence factor is defined as the reciprocal of the cooling rate (the slower the better). The intensity of spiral shear disturbance during the cooling process (e.g., spiral path airflow velocity × angular momentum factor). This is the structural response amplification factor for shear perturbation, used to fit how the perturbation exacerbates the formation of chain segment cyclotron conformations; This is the entropy term or the uncontrollable perturbation error term (system noise factor), used to prevent the denominator from being 0, and also reflects the uncertainty of natural thermal motion.

[0019] The above The derivation of the function:

[0020] Set the objective function , used to measure the stability (range 0~1) of the final helical pseudoconformation, is defined as the expected value of the product of the success rate of structure construction and the stability rate. First, the prerequisite for conformation formation is that the chain segment folding direction is effectively controlled, rather than resulting in disordered stacking (such as β-fold aggregation). Therefore, the following is introduced:

[0021] β-sheet blocking agent binding density: set as ,

[0022] The polarity matching degree of the blocking molecules is set as exponential weight. Then, the conformational protective contribution of blocking behavior can be expressed as:

[0023] Meanwhile, protein-polysaccharide interfacial synergistic polymers (such as locust bean gum) enhance the adhesion stability between protein segments and domains. Let its influencing factor be... The structural support of the conformation is then: .

[0024] Moreover, after the structure is induced by cooling, the flavor release behavior in the microcavity should be realized by reheating, which cannot destroy the conformation, so the impulse heat response function term is introduced. Assuming that the response of the microcavity structure to the impulse heat is in accordance with the behavior of monotonic increase but tends to saturation, the 1-exponential decay function form can be used, which is written as:

[0025]

[0026] wherein, is the response sensitivity coefficient of the microcavity to temperature change, represents the nonlinear temperature-sensitive curve characteristics of the release behavior. At this point, the forward factor of the entire conformation construction success can be expressed as:

[0027]

[0028] On the other hand, if the cooling is too fast, the protein chain has no time to rearrange fully, and then invalid conformations such as broken and irregular entanglement are formed, so the reciprocal of the cooling rate is set as the forward factor, denoted as , which is a negative term into the denominator. In addition, the conformation formation needs to be applied with directional disturbance by means of spiral path air flow cooling technology, the disturbance strength is set as , the influence of conformation folding behavior degree is set as the exponential , which is used to fit the cooperative relationship between disturbance and folding. Therefore, the total term of disturbance type energy interference is . Finally, considering the physical noise (such as thermal motion, spontaneous entanglement, error) in the system which cannot be eliminated, it is set as a constant offset term , which avoids the denominator approaching 0 causing discontinuity. The final target stability function is .

[0029] As preferred, the interface structure formed by the locust bean gum and the protein chain is a weak non-covalent hydrophilic and hydrophobic alternating interface, and the interface can maintain colloidal stability for not less than 72 hours in cold chain transportation; wherein the hydrophilic small molecule polysaccharide is introduced as a wetting regulator at the same time as the locust bean gum is added, so as to enhance the flexible bonding property of the protein and polysaccharide interface.

[0030] As preferred, the addition amount of the locust bean gum is controlled to be 0.2%-0.8% of the dry weight of the chicken claw protein, so as to ensure the formation of the bridging structure without causing gelation retention effect; the impulse heat-sensitive excitation treatment includes 3-5 cycles of short-time heating and intermittent cooling cycle, so that the water in the microcavity structure forms a multi-stage release platform; the heat-sensitive excitation treatment temperature is controlled between 60-75°C, so as to prevent the collapse of the microcavity wall structure while activating the opening of the hydrophobic channel.

[0031] ​As preferred, the flavor peptide segment and short-chain fatty acid complex in the water storage type microcavity release the sensory path of fresh first and then fragrant after thermal stimulation; wherein the microcavity structure after thermal stimulation can self-close part of the pore, realizing the release of residual flavor droplets again after the second heating; the spontaneous beta-sheet blocker is a natural plant polysaccharide with a molecular weight less than 5kDa, which blocks the accumulation of disordered beta layers by spatial embedding.

[0032] As preferred, the blocker preferentially binds to non-polar amino acid residues, avoiding premature beta-turn structure formation during cooling induction; wherein the blocker has a self-limited release behavior and gradually degrades after cooling; the introduction of the blocker is supplemented by a molecular hydration-induced slow-release system, so that the action stage is concentrated within 40 seconds before the protein chain cooling; the beta-sheet blocker is derived from natural plant extracts of roxburgh rose, cassia seed or black soybean skin, and is loaded into the protein chain reaction area after microencapsulation treatment.

[0033] The present application realizes multiple improvements of the organization elasticity, mouthfeel resilience, flavor performance and storage stability of chicken feet by constructing a protein segment directional reconstruction mechanism, controlling the micro-conformation formation path, combining interface structure regulation and flavor progressive release system, which has the following beneficial effects:

[0034] By constructing a conformational prestress zone before irradiation and applying 60Co gamma rays in a non-vertical main chain direction, directional slip and local re-entanglement of protein segments are induced, significantly enhancing the mechanical stability of the spiral-like structure formed after cooling of the chicken feet, so that the final product exhibits stronger chewiness and structure "memory" resilience after reheating. The spiral path type air cooling system combined with beta-sheet blocker intervention technology effectively suppresses the tendency of disordered aggregation during cooling, improves the directionality and uniformity of the spiral-like structure formation, and provides a basis for high-quality taste and high structural consistency.

[0035] By inducing transient complex structures of free radicals and active sites during the irradiation stage, and covering the surface of the chicken feet with a microparticle oxygen barrier film, lipid oxidation and amino acid flavor isomerization pathways are effectively blocked, reducing adverse flavors caused by irradiation from the source, so that the product maintains the original flavor and has less off-flavor. The flavor peptide segment and short-chain fatty acid complex are encapsulated in the water storage type microcavity structure induced by radiation, supplemented by pulse thermal stimulation technology, forming a "fresh first and then fragrant" flavor release rhythm, significantly enhancing the consumer's sensory experience; the microcavity structure can release residual flavor again after repeated heating, realizing stable flavor output under multiple reheating. By synergistically constructing protein-polysaccharide alternating hydrophilic and hydrophobic interfaces with locust bean gum and small molecule polysaccharides, the interfacial adhesion and anti-phase separation ability of the colloidal structure of chicken feet protein at low temperature are effectively enhanced, so that the product still maintains high-quality structure and taste consistency within 72 hours of cold chain. BRIEF DESCRIPTION OF DRAWINGS

[0036] Figure 1 Process flow diagram for improving the quality of boneless chicken feet irradiated by 60Co gamma rays according to the present application.

[0037] Figure 2 Multi-dimensional mechanism interaction diagram for improving the quality of chicken feet irradiated by 60Co gamma rays according to the present application.

[0038] Figure 3 Diagram of the synergistic mechanism of the spiral conformation and flavor release of boneless chicken feet according to the present application.

[0039] Figure 4 Layered relationship diagram for the 60Co gamma ray improvement experiment of functional chicken feet according to the present application.

[0040] Figure 5 Functional relationship diagram of the locust bean gum-microcavity multi-synergistic system for improving the quality of chicken feet according to the present application.

[0041] Figure 6 Diagram of the influence of different irradiation doses on the pH value of boneless chicken feet according to the present application.

[0042] Figure 7 Diagram of the influence of different irradiation doses on the water retention of boneless chicken feet according to the present application.

[0043] Figure 8 Diagram of the influence of different irradiation doses on the protein content of boneless chicken feet according to the present application. DETAILED DESCRIPTION

[0044] The present application will be further described below in conjunction with the accompanying drawings and examples, but it is not intended to be limited by them.

[0045] In conjunction with the accompanying drawings Figure 1As shown, in the specific embodiment of the present application, a method for improving the quality of boneless chicken feet using 60Co γ-ray irradiation is provided. The method first performs a pretreatment step on the boneless chicken feet. Fresh boneless chicken feet are preferably selected as raw materials and are kept at 0-4°C to maintain the original tissue tension characteristics. A tension regulator is used to apply a slight pulling force of 0.05-0.2 N / cm2 to the chicken foot tissue, and the chicken feet are placed in a cold and static environment for low-temperature static treatment. The static treatment time is controlled to be 30-60 minutes. The muscle fibers and collagen matrix in the chicken foot tissue form a conformational pre-stress zone without destroying the original elastic structure. The pre-stress zone can guide the directional response of the tissue protein structure during subsequent energy input, thereby constructing an elastic residual tension network and providing a structural tension guide for the irradiation process. Based on the formation of the conformational pre-stress zone, 60Co γ-ray irradiation is performed on the chicken foot samples. The irradiation process is carried out in a closed and humidity-controlled environment. The irradiation dose is controlled to be 2-10 kGy, and the irradiation rate is 0.5-1.5 kGy / h. A pre-set spatial energy control structure or shielding adjustment mechanism is used to make the 60Co γ-ray present a non-uniform spatial distribution during the action process, thereby inducing a directional molecular cleavage reaction in the collagen and elastin segments in the chicken muscle tissue. This reaction can effectively expose specific sites, including hydrophilic side chains, hydrophobic blocks, or α-helix broken structures. The exposed reaction sites after cleavage further undergo re-entanglement and recrosslinking behavior within or between molecules, allowing the protein molecules to be reconstructed into a more dense and elastic three-dimensional tissue network. Finally, the microstructure of the chicken foot tissue is remodeled, and the chewing elasticity and overall taste experience during consumption are enhanced.

[0046] Further control and optimization of possible adverse reactions during irradiation, focusing on the free radicals (including hydroxyl radicals, peroxide radicals, etc.) generated by high-energy dissociation reactions under the action of 60Co gamma rays during irradiation, as well as short-lived excited-state molecules. These highly active species will undergo chain oxidation reactions with lipids in the chicken feet under uncontrolled conditions, or irreversible cross-linking, cleavage, or carbamide condensation reactions with free amino acids and soluble small peptides, resulting in flavor deterioration, abnormal color, or decreased tissue elasticity. Therefore, a transient complexation induction strategy is introduced during irradiation, i.e. while applying 60Co gamma rays, specific protein active sites in the chicken feet tissue, such as hydrophobic residue exposure sites or broken chain structure regions, are actively induced to form non-covalent complex structures or micro-zone association states with generated free radicals or excited-state molecules in a very short time scale. This reaction process is mainly driven by the nucleophilic adsorption behavior between the polar targets with amino, hydroxyl, or carboxyl functional groups in the protein backbone and the highly active species, supplemented with trace amounts of natural polyphenols, chitosan oligosaccharides, etc. as electron transfer media to enhance the stability and spatial selectivity of the complex. The transient complex structure can capture and consume the initial reaction ability of active free radicals on one hand, and block the migration and diffusion path of free radicals in the tissue on the other hand, inhibiting their reaction with fatty acids and aromatic compounds in the chicken feet, and reducing the generation of harmful aldehydes and other volatile substances. At the same time, the complexation process can also effectively inhibit the cross-linking and cleavage of free amino acids and small peptides, and reduce the generation of Maillard reaction products, thereby improving the flavor and color of the chicken feet during storage.

[0047] Further improve the sensory quality and storage performance of the product, the cooling process adopts low-temperature slow-speed mode, preferably the cooling rate is controlled to be not higher than 1.5℃ / min at 0~4℃, to avoid protein chain shrinkage or helix preconformation collapse caused by sudden cooling. At the same time, a weak acid environment regulation mechanism is introduced during the cooling process to regulate the pH value of the surface and internal tissue environment of the chicken feet to about 3.89~5.34, preferably by injecting slightly acidic buffer or using natural fermented lactic acid solution to adjust. The pH value regulation to this critical value interval is mainly used to stimulate the reversible arrangement transformation of the α-helix residual segment or disordered segment in the collagen chain segment at low temperature. Under the condition of reduced intermolecular electrostatic shielding, hydrogen bonding and hydrophobic force drive the chain segment to reassemble into stable helix-like secondary pseudo-conformation structure. This structure has spatial resilience and strong network rigidity, which helps the chicken feet to exhibit good chewy elasticity and tissue recovery during consumption, thereby improving the resilience and structure memory of the overall mouthfeel;

[0048] In addition, in the above cooling induction stage, at the same time, the chicken claw protein chain is prompted to have non-covalent interaction with the previously added natural polysaccharide, especially the plant polymer with interfacial activity (such as locust bean gum, guar gum, konjac polysaccharide, etc.), including electrostatic adsorption, hydrogen bond association and van der Waals interaction, to form a protein-polysaccharide complex network, which is affected by the previously irradiation-induced segment break point and free site distribution, and presents a bridging structure distribution in three-dimensional space, especially forming a microscopic crosslinking bridge area in the junction area of the chicken claw tendon and fascia, further gathering part of the interstitial water and flavor small molecules in the bridge area, and finally constructing a water storage type microcavity structure with slow release ability and water locking performance, which can maintain the moisture of the tissue, reduce the loss of juice in the subsequent cold chain circulation and terminal reheating process, and release flavor substances under heating excitation conditions, significantly enhancing the reheating adaptability and flavor level of the product.

[0049] Combining the Figure 2 To further improve the directional response efficiency of the conformational prestressed structure and the directional breaking effect of the protein chain after 60Co γ-ray irradiation, a periodic pulse stress disturbance mechanism is introduced in the step of slight pulling combined with low-temperature standing, that is, a micro-control force loading module is set during the standing of the chicken claw, and a slight pulse stress in the range of 0.1-0.3 N / cm² is periodically applied in the pulling direction at a rhythm of 5-10 seconds, the disturbance direction is consistent with the pulling main axis direction, but the stress change is intermittent, this operation is used to destroy the residual stress network distributed transversely in the original muscle tissue, especially the transverse tension coordination area between muscle fiber bundles, so as to break the original stress balance state of the muscle fibers and form a more significant and stable conformational prestressed area in the pulling direction, providing a uniform and predictable stress response basis for subsequent energy input; then in the 60Co γ-ray irradiation step, a controllable reflection shield is set in the outer space of the conformational prestressed area, which is composed of a semi-closed shielding wall made of high-density metal material and has an adjustable angle of reflection inner wall, by adjusting the space projection angle between the ray source and the chicken claw tissue, the 60Co γ-ray irradiation path is shielded or deflected in part of the area, so that the main ray direction entering the prestressed area forms a non-perpendicular angle with the arrangement direction of the chicken claw protein main chain, and the angle range is preferably 15-45°, this irradiation design deviating from the vertical angle can significantly enhance the propagation trend of the ray energy along the main axis of the protein chain, prompting the molecular bond breaking behavior to occur along the chain direction, thereby forming a directional cleavage trend, which is easier than the traditional vertical irradiation which leads to random breaking mode.

[0050] The controllable reflection shielder can be supported by Chengdu Fangda Carbon Carbon Composite Material Co., Ltd. in a ready-to-use manner, and the company support includes: rear collimator + additional tungsten alloy shielding block (replaceable and adjustable angle) whole machine attached; the device parameters include: rear collimator: 4 cm tungsten alloy; source container: 14 cm tungsten alloy + 2 cm stainless steel; the angle is adjusted through the plug-in plate / wedge.

[0051] In the specific embodiment of the present application, in order to improve the spatial effect efficiency of 60Co γ rays in the protein segment structure reconstruction process and the molecular response accuracy, an alternating energy window period regulation strategy is introduced in the ray irradiation stage, that is, by setting the output power or shielding frequency of the irradiation system, a high-low alternating ray intensity mode is formed in the whole irradiation cycle. The specific operation is to set the duration of each high-energy window to 5-10 seconds, the duration of the low-energy window to 3-6 seconds, and the whole cycle control to be less than 1 minute. The window frequency and duration ratio are automatically adjusted according to the sample thickness and pre-stressed structure distribution density. During the alternating irradiation process, the discontinuity of energy input will cause a time sequence deviation between protein segment rupture and conformation contraction, that is, the segment is ruptured and the site is exposed after the first energy peak, but the low-energy period that follows cannot complete the complete inter-chain entanglement, and then the segment slip and contraction are activated again under the excitation of the next round of high-energy input. The conformation rearrangement behavior thus appears phase shift phenomenon. The shift causes the entanglement path between the chain segments to change from the original symmetrical entanglement to the off-center asymmetric entanglement state, which improves the spatial interlacing degree between the protein chain segments, thereby constructing a stable structure network with higher re-entanglement density in the cracking region, improving the overall organizational elasticity and microstructure density;

[0052] In addition, before 60Co γ ray irradiation, a mild protein chain polarizer is injected into the chicken foot tissue to enhance the response characteristics of the protein main chain to the energy field direction. The polarizer is a weak electrolytic polypeptide with a molecular weight of less than 5 kDa, which has weakly charged groups and short-chain hydrophilic side groups in its structure. After being injected into the chicken foot tissue under immersion or low-pressure vacuum tumbling conditions, it can preferentially adsorb or chimeric with the myofibril surface charge zone site, forming a kind of polar guiding layer that can maintain the chain segment conformation stable under the action of rays. The introduction of the polarizer establishes a directional microfield at the protein chain molecular level, which is conducive to the energy conduction and the arrangement of the broken chain segments along the main chain axis during ray irradiation.

[0053] To further enhance the depth regulation effect on the quality of chicken feet during 60Co gamma irradiation process, metastable complex reaction and microenvironment barrier mechanism are introduced in the free radical control and flavor optimization stage. Among them, the active sites exposed by protein chain rupture and the free radicals or excited state molecules induced by irradiation have formed a transient complex structure during the irradiation stage. This complex structure not only has the function of capturing free radicals and blocking side reaction paths, but also has certain chemical reaction potential. Therefore, in the subsequent low-temperature slow cooling stage, with the help of the dynamic background of the gradual decrease of system temperature and the decrease of molecular thermal motion energy, part of the high-energy state free radicals in the complex structure are stably absorbed or neutralized, and the rest are turned to react with the functional groups (such as lysine, glutamic acid, histidine, etc.) in the adjacent protein chain residues with reactive activity. The metastable complex reaction is non-covalent bond combination, which has low energy but strong directionality. In the complex process, the space of the chain segment is untangled and the tension is released, so that part of the short chain peptide, especially the flavor-related precursor peptide, is released to the surface layer of the chicken feet tissue or the bridged microcavity structure. This process realizes the local enrichment of flavor peptides and the timing coordination of conformational stability process, so that the chicken feet product is structurally enhanced while obtaining natural flavor enhancement, avoiding the risk of flavor dilution or oxidative off-flavor caused by traditional irradiation.

[0054] As a preferred, while limiting the diffusion of free radicals, to block the participation of external oxygen in lipid auto-oxidation reaction after irradiation and trigger the degradation of unsaturated fatty acids, the present application sets a micro-particle oxygen barrier film on the surface of chicken feet, which is composed of edible polymer materials with oxygen barrier properties (such as chitosan, gelatin / alginic acid composite film) and nanoscale inorganic particles (such as montmorillonite, silicon dioxide) to form an oxygen barrier that closely adheres to the surface of chicken feet. Its microstructure can significantly delay the penetration and diffusion rate of oxygen molecules, and has certain water regulation ability, which helps to maintain the tissue moisture state and regulate the release rhythm of water storage microcavity. The setting of the oxygen barrier film makes the chicken feet maintain a low-oxygen microenvironment during cold chain circulation and storage.

[0055] To further enhance the spatial consistency and structural forming efficiency of protein segment conformational rearrangement in the cooling induction stage, a spiral path air cooling technology is introduced during the low-temperature slow cooling process. This technology constructs a spiral guide structure air flow guide, which allows constant temperature cooling gas to enter the cooling cavity through the tangential guide channel and flow along the surface of the chicken claw and its circumference in a spiral trajectory. The spiral path is composed of multiple ring-shaped turbulence plates, inclined guide grooves, and central axis wind pressure structures, which form a directional rotational shear force field in different parts of the chicken claw. This shear force continuously acts on the peripheral environment of the protein segment during the cooling induction process, effectively breaking the static cooling mode during the cooling of the segment, promoting the spatial slip, spin, and convolution aggregation tendency of the protein main chain, enhancing the conformational deflection ability of the segment in the low-temperature state, and further promoting the stable transformation of α-helix or random segment to pseudo-helical secondary conformation. Through shear disturbance, the energy potential barrier between segments is reduced, the structural packing density and network density are increased, and a protein organization system with elastic rebound force and microstructure memory is constructed.

[0056] The above-mentioned air flow guide can be provided by Shanghai Yien Intelligent Equipment Co., Ltd.: (website: https: / / www.yienzn.com / ); technical parameters include: mesh width 200-1300 mm; automatic cleaning; support 20-120 min slow cooling (0-4°C).

[0057] In addition, during the cooling induction process, the molecular cooperativity of conformational rearrangement is further enhanced by precise control of the environmental pH. In this embodiment, the pH value of the cooling medium or wrapping liquid is adjusted to about 3.89-5.34. This pH adjustment is achieved by adding weak buffered plant acid liquid including malic acid buffer. This type of buffer is composed of natural organic acid and its conjugate base, and has the characteristics of mildness, non-destructiveness, and certain flavor synergy. During the adjustment process, the buffer is uniformly sprayed onto the surface of the chicken claw or injected into the vicinity of the fascia layer under low pressure to ensure that the local pH environment is stable within the target range. This pH level is close to the isoelectric point interval of structural proteins such as collagen, which helps to reduce the electrostatic repulsion between protein chains, enhance hydrogen bonding and hydrophobic interaction, and drive protein segments to aggregate into spatially ordered pseudo-helical conformational structures under the combined action of air flow shear disturbance. Ultimately, a cooling induction-pH regulation-air flow disturbance triple synergy conformational fine shaping mechanism is formed, providing a solid molecular foundation for the structural memory, chewy elasticity, and cold chain adaptability of the chicken claw organization.

[0058] Combined with the attached Figure 3As shown, to realize the stable construction and controllable flavor release of pseudo-spiral conformation structure in boneless chicken feet, various functional ingredients and physical intervention mechanisms are introduced during the cooling-induced rearrangement of protein chains, including natural polymers with synergistic activity at the interface of protein and polysaccharide, beta-sheet blockers, heat-sensitive microcavity structures, a spiral path air flow cooling system, and a pulse heat stimulation strategy to form a systematic conformation construction path. The natural polymers are preferably plant polysaccharides such as locust bean gum, konjac glucomannan, or guar gum, which have non-covalent association ability. During the cooling-induced stage, the natural polymers form bridging regions with protein segments to enhance the spatial bridging strength and water retention performance between the segments.

[0059] The beta-sheet blockers are low-molecular-weight polypeptides or amino-oligosaccharides with polar end groups, which have the ability to preferentially embed protein disordered segments and block the spontaneous stacking of beta-sheet aggregates, thereby ensuring the chain segments to maintain the space for convective sliding in the low-temperature shear field. Meanwhile, heat-sensitive microcavity structures are introduced when the protein segments tend to be stable during cooling to 5-10℃. The structures can be constructed by implanting polysaccharide-protein composite microparticles (particle size 100-300 nm) in the interstitial space in the early stage, have the ability to store water and load flavor precursor peptide segments, and release small molecule peptides under the condition of reheating due to temperature stimulation, thereby realizing the delayed release of flavor and structure-sensory synchronization. On the physical intervention level, a spiral path air flow system is set up to form a shear disturbance in the spiral direction, making the protein segments form a directional sliding and spatial folding trend during cooling. The system is composed of a wind guide structure with a ring-shaped guide blade and a central negative pressure aspirator, which can adjust the wind speed to 0.5-2 m / s and set the rotational angular momentum factor to form a continuous rotational shear force field. In addition, an intermittent pulse heat stimulation mechanism (such as microwave, infrared, or steam pulse) is set up to form a rapid temperature difference of 5-15℃ in the initial stage of reheating , which stimulates the release of flavor peptides from the microcavity structure and induces the spatial locking of pseudo-spiral conformation, thereby improving the flavor intensity and structural integrity of the reheated chicken feet. The above multi-parameter system can be evaluated for structural stability and optimized for process parameters by the following mathematical model, i.e., the conformation formation stability factor S, which is expressed as:

[0060]

[0061] where S is the stability factor of the pseudo-spiral conformation (value range 0 to 1), which is used to quantify whether the structure is formed and maintained stable; is the synergistic coefficient of natural polymers, representing the enhancement weight of conformation stability in the bridging network; is the binding site distribution density of the blocker, which is used to characterize its uniformity in the chain segment; is the molecular polarity adaptation index of the blocker, which reflects the synergy of its interaction with the protein backbone. is the response sensitivity coefficient of the heat-sensitive microcavity structure to the temperature difference excitation, is the set pulse excitation temperature difference, unit: K, is the nonlinear release response factor of the microcavity system, obtained by fitting the flavor release curve, and the empirical value range is 1-2; is the inverse factor of the cooling rate, the slower the cooling is, the larger the value is, which helps the structure forming; is the spiral airflow disturbance intensity, which is calculated by combining wind speed and rotation angle momentum; is the amplification response index of the disturbance to the conformation formation, is the system error correction term of uncontrollable disturbance such as thermal motion and irregular fluctuations of chain segments; the formula comprehensively expresses that the formation process of the spiral-like conformation is controlled by multiple coupling of biochemical material addition, temperature gradient change, shear disturbance and molecular structure self-stabilization mechanism, which can provide quantitative reference for process parameter optimization and guide to obtain optimal protein structure configuration and reheat release behavior under specific temperature, time, wind speed and component concentration conditions.

[0062] To further improve the stability of the interface structure and the flavor retention ability of boneless chicken feet during cold chain transportation and reheating process, during the cooling induction of protein chain and the rearrangement process of spiral-like conformation, a natural polysaccharide locust bean gum with interface synergistic conformation regulation ability is specially introduced, which has excellent hydrophilic-hydrophobic segmented structure, its main chain is composed of galactomannan, and the branched chain has a small amount of side chain residues, which presents alternating hydrophilic and hydrophobic blocks. When contacting with protein segments, it can form an interface bonding area through weak non-covalent interaction (such as hydrogen bond, van der Waals force, hydrophobic association, etc.). Especially in the stage of partial unfolding or incomplete locking of protein segments, the hydrophilic block of locust bean gum can be actively adsorbed to the polar side chain region exposed on the protein main chain, while the hydrophobic region is inserted into the hydrophobic folding core or the cross-linking entangled area of the protein chain. Finally, a weak non-covalent hydrophilic and hydrophobic alternating interface structure is formed between protein-polysaccharide complex. This structure not only has colloidal dispersion stability, but also has strong structural flexibility, which is conducive to maintaining the high wet stability of chicken tissue structure during cooling and cold storage without interface phase separation or surface adhesion phenomenon. Experiments show that the interface system can maintain a colloidal uniform dispersion state for more than 72 hours without phase change or flocculation under 4±1℃ cold chain conditions. At the same time, on the basis of the introduction of the above locust bean gum.

[0063] The present embodiment further adds a hydrophilic small molecule polysaccharide as a wetness regulator, which is preferably an oligofructose, chitooligosaccharide, algal oligosaccharide or other natural oligosaccharide ingredient, and has a molecular structure containing multiple hydrophilic groups capable of forming stable hydrogen bonds with water, high wetting and high diffusion, and synergistically acts with locust bean gum on the periphery of the protein chain during the addition process, adjusts the hydration ability of the local microenvironment, enhances the interfacial flexible bonding between the protein and the polysaccharide, and makes the entire protein-polysaccharide complex interface still maintain strong viscoelastic response when disturbed by low temperature, shear or reheating, preventing the structure layer from peeling off or the tissue water from rapidly losing.

[0064] To ensure that locust bean gum can efficiently participate in interface bridging during protein chain rearrangement and cooling induction without causing colloid retention or texture abnormalities, the addition amount is preferably controlled in the range of 0.2% to 0.8% of the dry weight of the chicken feet protein. Within this range, the addition amount can provide sufficient interfacial support under the premise of ensuring uniform dispersion of the colloid, form a flexible and reversible non-covalent bridging structure between the protein segments, and at the same time avoid gel shrinkage, sticky texture or water release caused by excessive locust bean gum, ensuring good tissue recoverability and flavor release ability of the chicken feet during subsequent cold chain transportation or reheating; on this basis, the flavor release mechanism is fully activated and the release rhythm of the microcavity structure is regulated.

[0065] The present application sets up a pulse heat-sensitive excitation program in the post-processing process, which includes 3-5 cycles of short-time heating and intermittent cooling treatment, the heating time of each cycle is controlled between 15-30 seconds, and the intermittent cooling time is 20-40 seconds. In each excitation, the core temperature of the chicken feet is quickly raised to the target temperature zone by steam injection, infrared radiation or microwave pulse, and then the heating is quickly stopped for natural temperature recovery. This pulse treatment strategy can promote the graded release of internal water and flavor small molecules in the heat-sensitive microcavity structure distributed in the subcutaneous layer and the junction area of the tendon of the chicken feet, i.e. the release of free water, bound water and flavor precursor peptide segments at different temperature platforms, to construct a multi-stage release behavior responding at different times, thereby enhancing the flavor layering and moistness of the chicken feet during reheating consumption. To prevent the microcavity structure from collapsing due to overheating or the protein bridging system from being damaged, the temperature in the pulse heat-sensitive excitation process is controlled between 60-75°C. This temperature range is sufficient to induce reversible structural tension response of the heat-sensitive polymer in the microcavity structure, activate the opening of the hydrophobic channel and release the flavor ingredients, and effectively avoid the degradation of the microcavity wall structure, protein unzipping or irreversible water loss above 80°C, to ensure the integrity and controllable release ability of the microcavity.

[0066] To further optimize the flavor presentation level and release control ability of boneless chicken feet during the reheating process, a water storage type microcavity structure is designed and formed during the cooling induction and structure building stage. The microcavity is mainly distributed in the tendon junction area and the surface collagen tissue of the chicken feet, and its structure is supported and stabilized by the protein-polysaccharide bridging network formed by irradiation induction, which encapsulates water-soluble flavor peptide segments and short-chain fatty acid complexes. The flavor peptide segments are small molecular peptides (molecular weight between 800-3000 Da) formed after directional cleavage of protein chains, which have high hydrophilicity and freshening effect. The short-chain fatty acid complex (including butyric acid, valeric acid and their flavor esters) is combined in the form of hydrophobic micelles in the microcavity inner wall or the gelatinous bound area. During the pulse heat-sensitive excitation process, the microcavity is expanded by tension due to heating, and the hydrophilic flavor peptide segments are released into the surrounding chicken tissue to form a pre-fresh sensory perception path. Subsequently, in the temperature further rising or delayed release stage, the short-chain fatty acid components are released with the swelling of hydrophobic micelles and the opening of channels, and the after-flavor release peak is constructed, thereby realizing a multi-stage flavor release mode of fresh-sense leading and fat-flavor extending, and significantly improving the richness and recognition of flavor during eating.

[0067] In addition, the microcavity structure has heat-sensitive closure, that is, after the excitation heat source is removed, the cavity wall structure can be self-closed part of the channel during the cooling contraction process due to the reversible winding characteristics between protein-polysaccharide segments, so that the flavor droplets not released at one time are temporarily stored and activated for release again in the secondary reheating process, realizing the synergistic control of flavor progression response and retention intensity, effectively prolonging the release persistence and aftertaste performance of chicken flavor; at the same time, in order to ensure the formation of stable helix-like pseudo-conformation instead of disordered aggregate state during protein chain reconstruction, the present application introduces a spontaneous beta-sheet breaker, which is a natural plant polysaccharide (preferably derived from konjac oligosaccharide, seaweed oligosaccharide, etc.) with a molecular weight less than 5 kDa. The polysaccharide molecule can actively enter the hydrophobic accumulation area of the protein segment where the beta-sheet is formed and embed between them due to its flexible main chain and multiple hydrophilic side groups during the cooling induction stage, destroying the excessive pairing and layered accumulation trend between the chain segments.

[0068] To effectively control the conformational trajectory of protein segments during cooling induction and avoid the spontaneous formation of stable, high-structural-density beta-turn or beta-sheet structures, a beta-sheet blocking agent with conformational selectivity and self-limiting release characteristics is used. The blocking agent is derived from natural plant extracts, preferably including low molecular weight polyphenols in rose hips, cassia seed or black soybean skin, and has high affinity for specific residues of protein chains after purification. Further microencapsulation encapsulation treatment is carried out by spray drying or electrostatic condensation method, and is loaded into the active region of protein chain reconstruction, especially in the segment break site and slip cross region formed after 60Co gamma ray irradiation. The blocking agent selectively binds to non-polar amino acid residues (such as valine, isoleucine, phenylalanine, etc.) in the early stage of structure construction, effectively occupying the hydrophobic packing site required for beta-turn formation, inhibiting the premature folding of the segment and the incorrect entry into the beta-sheet path, and further promoting the segment to maintain the spatial freedom of convolute slip, providing structural precondition for the generation of pseudo-conformation of helix-like.

[0069] At the same time, to prevent the blocking agent from interfering with the formation of stable conformation of protein chain in the later stage, self-limiting release behavior is introduced in the microencapsulation design of the blocking agent, i.e. the blocking agent is quickly released and enters the active state at the beginning of protein chain cooling, and is degraded by itself due to the gradual hydrolysis of the shell or pH response disintegration within 40 seconds to 1 minute after cooling induction, eliminating its influence on the system, so that its action stage is concentrated in the early stage of cooling and the key period of conformation error, rather than the whole process interference, so as to realize the precise intervention-exit type segment regulation strategy. In addition, on the basis of the above blocking agent design, a molecular hydration induction slow-release system is further supplemented, which is composed of hydrophilic small molecule sugar alcohol or organic acid sodium salt (such as sodium lactate, erythritol), which has the ability to form a transient hydration shell on the surface of protein chain. By adjusting the distribution of free water in the system, the blocking agent microcapsule releases quantitatively within the first 40 seconds after contacting the protein chain, rather than releasing all effective components at once, so as to realize the dynamic matching of the release rate of the blocking agent and the cooling process of the segment, and finally ensure that the protein segment avoids entering the beta conformation trap in the cooling induction path, but is rearranged into a pseudo-helical conformation along the helix shear disturbance direction, realizing the organic unity of elastic enhancement, flavor carrier integration and cold chain stability control of the microstructure of the spring roll organization.

[0070] Example 1: combined with Figure 4As shown, the example background is set as a functional chicken drumstick pre-product research and development project, aiming to improve the tissue elasticity and flavor release control of chicken drumsticks by 60Co γ-ray treatment. 150g boneless chicken drumstick samples are selected, 40 samples per batch, after uniform saline pre-permeation treatment, they enter the micro-pulling and low-temperature standing pretreatment stage. The tension control system is used for the tension control system, and 0.3N of micro-pulling force is applied to each chicken drumstick, and the direction is slowly extended along the tendon degradation axis, while standing in a 4°C environment for 40 minutes; The experimental group superimposes periodic pulse stress disturbance on this basis, and applies a low-frequency shear force of 5Hz frequency and 0.1N amplitude through a gas pressure driven vibration module, with a cycle of 2 seconds action 2 seconds intermittent, continuous action for 30 minutes, the measured results show that compared with the undisturbed group, the uniformity index (CV value) of the tissue transverse muscle fiber arrangement of the experimental group decreases by 18%, which proves that the stress disturbance effectively breaks the original transverse tension distribution, and lays a foundation for the establishment of conformational prestress.

[0071] After the construction of the conformational prestress area, enter the 60Co γ-ray irradiation stage, the irradiation source is 60 Co, energy 1.17-1.33MeV, a special reflection shield is used to adjust the irradiation path, among which a controllable reflection sheet is set at 45° behind the sample side, so that the main ray direction and the protein main chain (original collagen fiber) arrangement direction form an about 60° non-vertical included angle, in order to enhance the tangential energy transfer efficiency of the ray and the chain segment. Compared with the normal sample, the protein fracture site in the non-vertical angle irradiation group shows more obvious chain segment slip marks in the structure scanning electron microscope, and the directional fracture rate increases by about 22%, which shows that the reflection angle adjustment system indeed enhances the conformational directional reconstruction trend.

[0072] In order to further improve the spatial synchronization of protein chain structure reconstruction after fracture, the technical path of setting alternating energy window period is adopted during irradiation, that is, the intensity of the rays in the irradiation chamber is adjusted to change with time period, and the period is set to 10 seconds a band, and the dose density is floated ± 0.5kGy from 6.0kGy during this period, so as to construct a low-high energy alternating time window. This alternating treatment makes the chain fracture time staggered, avoids the simultaneous activation of chain ends and the occurrence of disordered entanglement, and promotes the re-entanglement rate through the stagger effect. Based on the scanning peptide chain reconstruction map, the entanglement positioning overlap degree of the alternating group is 72%, which is obviously higher than that of the constant energy group (entanglement positioning overlap degree 55%), which supports the assumption of improving the controllable entanglement efficiency.

[0073] In the pre-irradiation treatment stage, to further strengthen the consistency of protein main chain arrangement and the directionality of response, a mild protein chain polarizer is injected into the sample tissue 30 minutes before irradiation. The polarizer is a small-molecule polypeptide solution containing weak electrolytic properties (such as a complex solution of glutathione and glycine oligopeptide), with a concentration controlled at 0.4 mg / mL. It is injected into the surface layer and tendon transition zone of the chicken drumstick through micro-injection. After 20 minutes of standing to promote the consistency of main chain polarization arrangement, electrophoresis detection shows that this treatment can increase the change amplitude of collagen protein mobility by 17%, indicating that the polarization effect is significant. The subsequent irradiation enhances the concentration of fracture point distribution, and the main chain fracture trend is more concentrated in the atomic sequence axis direction, enhancing the coupling degree of the chain segments after cleavage.

[0074] Next, in this embodiment, 180g size boneless chicken drumsticks are selected, 40 per batch. The micro-pulling-conformation pre-stress establishment and 60Co γ-ray irradiation (dose 6.5 kGy) steps have been completed in the early stage. Now it enters the cooling induction and structure shaping and flavor synergistic release stage.

[0075] First, to achieve synchronization of structure rearrangement and flavor release, a protein free radical activation window is designed in the irradiation stage in this scheme. Through spatial restriction and induced complexation, short-lived complex structures are formed. Mainly, π-π complex bodies are formed by irradiation-activated aromatic residues (such as tyrosine, phenylalanine) and transiently excited state free radicals on the chain segment. Part of the complex structure undergoes metastable complexation with small-molecule flavor precursor peptides during the cooling induction process, causing the temporary binding of flavor components to local protein domains. When the cooling temperature drops below 8°C, the complex structure releases flavor peptides due to the tension disturbance caused by the contraction of the main chain. The total release amount is 1.9 mg / g protein on average. The flavor precursor release peak appears after about 36 seconds of cooling. Mass spectrometry analysis detects 5 main peptide segments (molecular weight 300-700 Da). At the same time, DSC analysis shows that the protein microdomain structure transition temperature overlaps with the flavor release peak, indicating that flavor release and structure transformation show a coupling trend.

[0076] To inhibit the oxidation of flavor components and the migration reaction of free radicals during cooling, a layer of food-grade microparticle oxygen-inhibiting film is covered on the surface of the chicken drumstick. The film is prepared by complexing β-cyclodextrin, chitosan and sodium citrate (coating thickness about 25 µm). It has weak hydrophobicity and free radical capturing ability. The measured oxygen diffusion rate of the chicken drumstick sample surface is reduced by about 63%. The content of fatty acid oxidation products (MDA) is reduced from 0.41 µmol / g in the control group to 0.27 µmol / g in the treatment group, effectively reducing the generation of flavor isomerization byproducts and preserving the original meat aroma characteristics.

[0077] Then enter the cooling-induced rearrangement stage, by setting a spiral path airflow system, the cooling airflow is guided by the wind cavity device equipped with a ring guide vane, so that it forms a spiral path flow around the long axis direction along the surface of the chicken feet, the wind speed is set to 1.4 m / s, the spiral rotation angular velocity is 0.8 rad / s, and the total cooling time is controlled to gradually reduce the temperature to 5℃ within 90 seconds. Under this condition, the protein segment occurs directional slip and segmented convolution under shear disturbance, and induces the formation of a helix-like secondary pseudo-conformation structure. The structure scanning electron microscope image shows that the surface collagen layer of the processing group forms regular parallel fiber bundles, the tensile direction consistency index (AFI) is improved by 28%, the chewing elasticity test is improved from 0.69N to 0.93N, and the rebound rate is improved to 87%.

[0078] At the same time, in order to regulate the pH of the cooling environment to further promote the conformational rearrangement and the stability of the collagen network, the present application adds a weak buffer type plant acid liquid to the cooling liquid system, which is mainly composed of 0.3 mol / L malic acid and 0.1 mol / L sodium citrate, and the system pH is stabilized at (3.89-5.34)±0.1, which effectively triggers the helix-like rearrangement of collagen segments, forming intramolecular hydrogen bond bridging structure, IR spectrum shows that the Amide I region absorption peak shifts from the original 840 cm⁻¹ to 853 cm⁻¹, indicating that the proportion of helix-like conformation increases significantly. In summary, the flavor release curve of the experimental group chicken feet after reheating appears two platforms: a fresh peptide release peak appears in the heating temperature range of 35℃-45℃, and a secondary aroma of short-chain fatty acids is released in the temperature range of 65℃-72℃, and the sensory score is improved to 8.7 (full score 10), while the average of the control group is 7.1, which shows that the flavor and structure are highly coupled and optimized under the above scheme, verifying the practical feasibility and synergistic effect of each technical link of the present application.

[0079] Example 2:

[0080] In combination with the Figure 5 As shown in the accompanying drawings, based on a joint project of a certain food research unit, 30 chicken feet (each weighing about 160g) per batch are selected for comparative study, among which 0.45% (protein dry weight ratio) locust bean gum is introduced as a synergistic interfacial polymer in the cooling induction stage of the experimental group, and microencapsulated natural plant polysaccharide blockers (molecular weight <5kDa, distribution density θ=0.62) and microencapsulated heat-sensitive water storage microcavities (response sensitivity λ=0.21) are injected, the cooling system is set to slow cooling (1.2℃ / min), at the same time, the shear disturbance intensity Ω=2.3 (unit complex factor) is applied through the spiral airflow system, and a pulse heating-cold cycle (ΔT=22K) is applied; according to the previous experiment and literature fitting, the polarity adaptation index of the blocker is set to =1.6, the nonlinear response index of the microcavity is =1.5, the cooling rate factor is =1 / v=0.83, and the disturbance response amplification coefficient is = 1.7, system noise = 0.05, interfacial polymer synergy factor = 0.91. Substituting the data into the formula:

[0081]

[0082] Substituting the values:

[0083]

[0084] The calculation steps are as follows:

[0085]

[0086]

[0087]

[0088] Therefore

[0089] The molecule is approximately

[0090] , multiplied by 0.83 to get , and The denominator is

[0091] Finally

[0092] The stability factor value is about 0.106, indicating that the pseudo-conformation formation under this condition has moderate stability and has obvious effect on resilience and flavor carrier construction. By increasing µ to 1.1 (such as adding more locust bean gum) or appropriately increasing ΔT (increasing the pulse excitation amplitude), the S value can be increased to > 0.15, representing enhanced pseudo-conformation formation and retention ability.

[0093] In actual evaluation, the increase of S value is positively correlated with the resilience of chicken claw tissue (r = 0.88), and the resilience of the experimental group is increased from 0.71 N of the control group to 0.93 N, the flavor release duration is increased to 42 seconds, and the flavor intensity score is increased by 22%; and the tomographic structure scanning shows that the tissue chain segments are arranged in a spiral shape, and the flavor release after heat stimulation shows obvious double peaks, matching the microcavity controlled release characteristics, verifying that the mathematical model has a predictive and guiding effect on actual process regulation.

[0094] To further improve the colloidal stability of the product during cold chain transportation, the flavor level release during reheating, and the flexibility of the protein structure, the research team introduced locust bean gum and hydrophilic small molecule polysaccharide synergistic interface regulation system during the cooling-induced conformation formation stage of the protein chain, and combined with the heat-sensitive excitation controlled release strategy for comprehensive verification. This research was completed by a pre-prepared food processing enterprise in cooperation with the Food Science Research Institute. 50 batches (140g each) of boneless chicken feet were selected for the experiment, irradiated with 60Co gamma rays (6.2kGy) in the early stage, and then entered the cooling-induced and interface construction stage.

[0095] Firstly, based on the previous research that locust bean gum has excellent non-covalent interface binding capacity of protein chain, locust bean gum was used as a conformation bridging agent in this experiment, with the addition amount set at 0.2%, 0.5%, and 0.8% of the dry weight of chicken feet protein, with 0.5% as the main experimental group. At the same time, all samples were added with 30% hydrophilic small molecule polysaccharide (mainly glucose oligomer and mannose oligomer complex) as a wetting regulator, which enhances the uniformity of the distribution of locust bean gum on the protein chain segment and improves the flexibility of the attachment strength. The results of structural spectral analysis show that compared with the group with only locust bean gum added, the uniformity of the interface binding area is improved by about 23% after the introduction of small molecule polysaccharide, and the peak shift reflecting the flexibility of the protein secondary structure in the Raman spectrum also tends to be stable.

[0096] The interface microstructure was observed by cryogenic transmission electron microscopy, and an obvious "hydrophilic-hydrophobic" alternating layered coating structure was formed on the protein chain segment, with the hydrophilic region being wrapped outside the polysaccharide segment and the hydrophobic region being formed by π-stacking between the locust bean gum molecules and the aromatic amino acid residues. This weak non-covalent alternating interface structure was confirmed to significantly enhance the structural stability of the chicken feet protein-gel system during cold chain transportation. In actual cold chain simulation transportation tests, the above products were stored and transported at 4°C for 72 hours, and the dynamic rheological test was used to analyze the change of colloidal viscoelasticity. The results showed that the Tanδ change rate of the experimental group after storage was only +7.6%, which was much lower than the +21.3% of the group without adding the regulator, and the stability was significantly maintained.

[0097] To further realize the controllability of flavor release in reheating, the study designed three different rounds of "pulse heat-sensitive excitation treatment" strategies, namely 3 rounds (70°C x 30s / cooling 30s), 4 rounds (65°C x 40s / cooling 20s) and 5 rounds (60°C x 45s / cooling 20s), and analyzed the release path of water and flavor peptide segments in the microcavity structure. In the main experimental group using the 4-round / 65°C excitation strategy, the microcavity structure maintained an intact proportion of 92%, and after thermal profiling, the release behavior showed three stepwise platforms: the first interval 35°C-42°C was the free water release period, with a release peak of 1.8µg / mg; the second interval 50°C-60°C was the flavor peptide segment activation release zone, with a release concentration of 2.3µg / mg; the third interval 65°C-72°C was the fatty acid volatile release platform, with a subsequent release concentration of 0.9µg / mg, forming a "fresh before and fragrant after" flavor progression path. If the temperature exceeds 75°C, partial collapse of the microcavity wall occurs (collapse rate >28%), and at the same time, there are adverse feedbacks such as astringent taste and flavor burst in sensory evaluation, confirming that the heat-sensitive excitation temperature control window of 60-75°C proposed in this invention is scientific and effective.

[0098] In the final sensory evaluation, a professional evaluation team (n=12) evaluated the elasticity, flavor richness and flavor delayed release characteristics during the instant stage after reheating. The overall score of the experimental group was 8.8 (full score 10), which was 1.7 points higher than that of the traditional processing group, and the score of flavor aftertaste was improved significantly (+31%). Combined with the detection of texture analyzer, the elasticity rebound was improved (from 0.71N to 0.95N), which verified the synergistic effect of locust bean gum-polymer interface system combined with microcavity release platform in actual product optimization.

[0099] This embodiment relies on the chimeric loading structure of flavor peptide segments and short-chain fatty acid complexes in water storage type microcavities, and introduces a spontaneous beta-sheet breaker to inhibit the disordered accumulation of protein segments during cooling induction, ensuring the synchronous realization of ordered construction of pseudo-helical conformation and flavor progression release behavior.

[0100] The experiment adopts 120 de-boned chicken feet and divides them into two groups. In the experimental group, microencapsulated flavor complexes (the encapsulated core is a flavor peptide segment + complex fatty acids of caprylic acid and butyric acid, and the content ratio is 3:2) are added in the cooling induction stage after irradiation (the dose is controlled to be 6.0 kGy). The initial release starting temperature of the gelatin-sodium alginate double-layer wall material is controlled to be 60 DEG C, and the terminal temperature is about 75 DEG C. The heat-sensitive pulse excitation is set to be 65 DEG C x 30 seconds x 2 rounds. The release monitoring results show that, in the first excitation process, the total amount of microcavity release is about 71.4% of the encapsulation amount, and the flavor organoleptic is dominated by the fresh feeling of peptides, showing a fresh and bright front note characteristic. When heated to 72 DEG C for the second time, the microcavity part of the channel is opened again due to the heat-induced closure, and the remaining 28.6% of the flavor lipid components are released, and the sensory performance is a long-lasting aftertaste. The overall construction forms a multi-level sensory path of "fresh front and fragrance back". Compared with the traditional non-staged release processing group, the flavor lingering time is prolonged by 39 seconds, and the main flavor intensity score is increased by 1.9 points (10 points).

[0101] To ensure the smooth construction of the pseudo-helix structure in the protein chain cooling induction process, the team simultaneously introduces a natural plant-derived polysaccharide blocker with a molecular weight controlled in the range of <5 kDa, which includes acaiberry pectin oligomers, cassia low oligogalactose, and black soybean skin acidic polysaccharide extract, and is loaded into chitosan-dextran composite microcapsules by spray drying, so as to be accurately positioned around the protein chain breakage zone in the 60Co gamma ray action area. 40 seconds before cooling induction, the molecular hydration induction slow-release system (based on oligomannose to regulate hydration kinetics) is used, the blocker is quickly released and forms a spatial chimeric with non-polar amino acid residues (such as valine, phenylalanine, and isoleucine) in the protein chain, blocks the formation of hydrophobic accumulation nucleus, and then inhibits the early appearance of beta-turn structure; molecular simulation data shows that the beta-turn formation probability in the blocker group is reduced by about 41.7%, while the consistency of helix rotation angle (RMSD variation) is increased by 23.4%, indicating that the conformation tends to be ordered and stable. After cooling, the blocker begins to enter the self-limiting degradation stage, the wall material responds to the environmental acidity of pH 3.89-5.34, gradually disintegrates and releases the internal active sites, and is completely removed within 60 minutes to avoid affecting the final resilience. In the final texture analysis, the elasticity of the experimental group is increased by 0.98 N, and the elasticity of the contrast group is 0.72 N. In the flavor recognition multi-channel analysis, the staged release nodes can be clearly distinguished; the re-heating test results after 72 hours of cold chain storage also show that the microcavity structure stability is maintained above 91%, and the flavor re-release integrity reaches 86%, proving that the structure-flavor integrated construction path in the present application, with the help of water storage type flavor complex microcavities and natural beta blockers, has the advantages of stability, flavor performance and quality retention in actual industrial applications.

[0102] The relevant embodiment evaluation data are as follows:

[0103] According to the sensory requirements in GB 2707-2016 "National Food Safety Standard Fresh (Frozen) Livestock and Poultry Products", the 100-point evaluation method is used. Ten members are selected to form a sensory evaluation team (5 males and 5 females), and the samples are scored from color, taste, aroma, shape and texture. The following is the sensory evaluation table:

[0104]

[0105] As shown in Figure 6 , the pH values of samples in different treatment groups showed a trend of first decreasing, then increasing and then decreasing during storage.

[0106] During storage, the pH value of the sample group without irradiation treatment was 5.24 at the maximum and 4.69 at the minimum. In the irradiation treated sample group, the maximum value was 5.34 measured at 60d for 4kGy, and the minimum value was 3.89 measured at 15d for 2kGy. At 0d, the pH value of the 4kGy irradiation group was the largest, and there was a significant difference between it and the 2, 6, and 8kGy irradiation groups (p<0.05). At 15d, the pH of each irradiation treated test group was at the lowest value during the storage period, among which the pH value of the 6kGy irradiation group was the largest, and there was a significant difference between it and the 0 and 2kGy irradiation groups, but no significant difference between it and the 4 and 8kGy irradiation treatment groups (p>0.05). At 30d, the pH of the test group without irradiation treatment was at its lowest value during the storage period, while the pH of the different irradiation dose groups increased with the increase of irradiation dose, and the pH of the 8kGy irradiation group was the largest, and there was a significant difference between it and the other irradiation dose groups. At 60d, the 4kGy irradiation group had the largest pH value, and there was a significant difference between it and the 0, 2, and 8kGy treatment groups, and no significant difference between it and the 6kGy treatment group. At 90d, the pH values of each irradiation dose group decreased, and the pH value of the 4kGy irradiation group was the largest, and there was a significant difference between it and the other treatment groups.

[0107] By Figure 7It can be seen that the water retention of the five treatment groups increased with the extension of storage time. The water retention of the sample group without irradiation treatment was the largest, 96.26%, and the smallest, 90.02%. In the sample group with irradiation treatment, the maximum value was 97.05% obtained by 4 kGy at 90 d, and the minimum value was 92.13% obtained by 6 kGy at 0 d. The water retention of the sample groups treated by 0 and 2 kGy had significant difference at 0-15 d. The water retention of the sample group treated by 4 kGy had significant difference at 0-30 d and 60-90 d, and the water retention was the largest at 90 d. The water retention of the sample group treated by 6 kGy had significant difference at 0-15 d. The water retention of the sample group treated by 8 kGy had significant difference at 0-15 d. After treatment by different irradiation doses, there was no significant difference between the sample groups treated by 0 and 2 kGy at each storage period, indicating that the effect of low-dose irradiation on the change of water retention was not obvious. At 0, 30 and 60 d, there was no significant difference in water retention between the sample groups treated by different irradiation doses. At 15 d, there was significant difference between the sample groups treated by 8 kGy and 0, 2 and 6 kGy, and there was no significant difference between the sample groups treated by 4 kGy. At 90 d, the water retention obtained by the sample group treated by 4 kGy was the largest, and there was significant difference between the sample groups treated by 0 and 4 kGy, but there was no significant difference between the sample groups treated by other irradiation doses.

[0108] The detection results of protein content are as follows Figure 8The maximum value of protein content in the non-irradiated sample group was 18.63% and the minimum value was 16.45%. The maximum value of protein content in the irradiated sample group was 21.81% in the 0d sample of the 8kGy treatment group and the minimum value was 14.58% in the 0d sample of the 2kGy treatment group. The protein content of the 0, 2, and 4kGy irradiation treatment groups increased first and then decreased with the extension of storage time, while the protein content of the 6 and 8kGy irradiation treatment groups showed a jagged downward trend. The protein content of the 0kGy treatment group at each time period during storage showed no significant difference. The protein content of the 2kGy treatment group reached the maximum value during storage at 30d and showed significant differences with the 0d and 90d samples. The protein content of the 4kGy treatment group reached the maximum value during storage at 15d and showed significant differences with the 0d and 90d samples. The protein content of the 6kGy treatment group reached the maximum value at 0d and showed significant differences with the 30d and 90d samples. After treatment with different irradiation doses, the protein content of the 8kGy irradiation group reached the maximum value at 0d and showed significant differences with the 0, 2, and 4kGy irradiation groups, but no significant difference with the 6kGy irradiation group. The protein content of the 6kGy irradiation group reached the maximum value at 15d, but showed no significant difference with the other treatment groups. The protein content of the 2kGy irradiation group reached the maximum value at 30d, but showed no significant difference with the other treatment groups. The protein content of the 6kGy irradiation group reached the maximum value at 60d and showed significant differences with the 0, 4, and 8kGy irradiation groups, but no significant difference with the 4kGy irradiation group. The protein content of the 0kGy irradiation group reached the maximum value at 90d and showed no significant difference with the other treatment groups.

[0109] The maximum value of the shear force of the sample group without irradiation treatment was 1123.4 gf, and the minimum value was 998.5 gf during the storage process. The maximum value of the protein content of the sample group with irradiation treatment was 1775.7 gf measured at 60 d of the 2 kGy treatment group, and the minimum value was 487.4 gf measured at 90 d of the 2 kGy treatment group. At 0 d, the shear force of the 2 kGy irradiation group was the maximum, and there was a significant difference between the 2 kGy irradiation group and the 6 kGy and 8 kGy irradiation groups. There was a significant difference between the 0 kGy and 4 kGy irradiation groups and the 8 kGy irradiation group. At 15 d, the shear force of the 6 kGy treatment group was the maximum, and there was a significant difference between the 6 kGy treatment group and each treatment group. At 30 d, there was no significant difference between each treatment group. At 60 d, the maximum value of the shear force was measured in the 2 kGy irradiation group, but there was no significant difference between each treatment group. At 90 d, the shear force of the 0 kGy group was the maximum, and there was a significant difference between the 0 kGy group and the 2 kGy and 4 kGy groups. There was a significant difference between the 2 kGy group and the 4 kGy, 6 kGy, and 8 kGy treatment groups. There was no significant difference between the 0 kGy treatment group at each time period during the storage period. The 2 kGy reached the maximum value at 60 d, and there was a significant difference between the 2 kGy and the other time points. There was no significant difference between 0 d, 15 d, and 30 d, but there was a significant difference between 0 d, 15 d, and 30 d and 90 d. The shear force of the 4 kGy was the maximum at 60 d, and there was a significant difference between the 4 kGy and 90 d. There was no significant difference between the 0 kGy, 15 kGy, and 30 kGy. There was no significant difference between 0 kGy, 15 kGy, 30 kGy, and 90 kGy. The shear force of the 6 kGy and 8 kGy treatment groups was the maximum at 15 d, but there was no significant difference between each time period. The following table shows the effect of different irradiation doses on the shear force of boneless chicken feet:

[0110]

[0111] The above shows and describes the basic principles, main features, and advantages of the present application. Those skilled in the art should understand that the present application is not limited to the above examples, and the above examples and descriptions in the specification are only to illustrate the principles of the present application. Without departing from the spirit and scope of the present application, various changes and improvements can be made to the present application, and these changes and improvements all fall within the scope of the claimed present application. The scope of protection of the present application is defined by the appended claims and their equivalents.

Claims

1. A method for improving the quality of boneless chicken feet by 60Co γ-ray irradiation, characterized in that: The method comprises the following steps: pretreating the chicken feet after bone removal, constructing a conformational pre-stress area with elastic residual tension in the tissue structure of the chicken feet by means of micro-pulling and low-temperature standing, providing a structural tension guide basis for the irradiation process; on the basis of the conformational pre-stress area, 60Co gamma rays are applied, the irradiation dose is controlled to be between 2-10 kGy, a dynamic staggered cleavage area is formed by inducing non-uniform energy distribution, so that directional cleavage, reaction site exposure and re-entanglement are realized in the collagen and elastin chain segments, the tissue structure is reshaped and the chewiness is enhanced; During the irradiation process, the exposed protein active sites are guided to form a transient complex structure with the free radicals or excited-state molecules generated by irradiation, so as to limit the migration and diffusion of free radicals, block the lipid and amino acid side reaction paths, and prevent the generation of flavor isomerization by-products; After the irradiation is completed, the chicken feet are subjected to low-temperature slow cooling treatment, and the environmental pH is regulated to 3.89-5.34, so as to induce the re-arrangement of part of the collagen chain segments to form a secondary pseudo-conformational structure of a spiral shape, and improve the resilience and structural memory of the taste; During the cooling induction process, non-covalent interaction between the protein chains and natural polysaccharides in the chicken feet is promoted, a bridging structure formed by irradiation is constructed, and a water storage type microcavity structure is formed in the tendon connection area.

2. The method for improving the quality of boneless chicken feet by 60Co γ-ray irradiation according to claim 1, characterized in that: During the steps of micro-pulling and low-temperature standing, periodic pulse stress disturbance is applied at the same time, which is used to break the natural transverse stress distribution in the muscle fibers; during the 60Co gamma ray irradiation step, a controllable reflection shield is arranged outside the conformational pre-stress area, so that the main ray direction and the protein main chain arrangement direction form a non-perpendicular included angle, and the directional breaking tendency of the protein chain is enhanced.

3. The method for improving the quality of boneless chicken feet using 60Co γ-ray irradiation according to claim 1, characterized in that: During the 60Co gamma ray irradiation stage, an alternating energy window period is set, so that the protein chain reconstruction process is phase-shifted, and the controllable re-entanglement rate of the cleavage area is improved; before the 60Co gamma ray irradiation, a mild protein chain polarizer including a weak electrolytic polypeptide is injected into the chicken feet, which is used to strengthen the main chain directionality.

4. The method of claim 1, wherein the 60Co gamma ray irradiation is performed at a dose of 10 kGy. After the complex structure is formed, a metastable complex reaction occurs with part of the protein residues, flavor precursor peptide segments are released during the cooling stage, and the synergistic generation of flavor and structure is realized; while limiting the diffusion of free radicals, a microparticle oxygen inhibition film is arranged on the surface of the chicken feet to block the lipid oxidation path induced by oxygen. ​ 5. The method for improving the quality of boneless chicken feet by irradiation with 60Co γ-rays according to claim 1, characterized in that: During the low-temperature slow cooling treatment, a spiral path air cooling technology is adopted, a spiral guide structure air flow guide is arranged, the cooling air flows along the surface and the circumference of the chicken feet in a spiral path, directional shear disturbance is applied in the protein chain segment cooling induction rearrangement process, and the formation and stability of the secondary pseudo-conformational structure of a spiral shape are promoted; the regulation of the environmental pH to 3.89-5.34 is realized by adding a weak buffering type plant acid liquid including malic acid buffer.

6. The method of claim 5, wherein the 60Co gamma ray irradiation is performed at a dose of 10 kGy. The cooling induction process adds natural polymers including locust bean gum with protein and polysaccharide synergistic interface activity to improve the interface adhesion stability of the bridging structure; the water storage type microcavity structure is treated by pulse heat sensitive excitation after formation, so as to have a controllable release curve in the reheating process; the self-induced β folding blocker is introduced in the protein chain reconstruction process to prevent unordered folding from interfering with the stable formation of pseudo-helical conformation.

7. The method of claim 6, wherein the 60Co gamma ray irradiation is performed at a dose of 10 kGy. The interface structure formed by the locust bean gum and the protein chain is a weak non-covalent hydrophilic and hydrophobic alternating interface, which can maintain colloidal stability for not less than 72 hours in cold chain transportation; wherein the hydrophilic small molecule polysaccharide is introduced as a wetting regulator at the same time as the addition of locust bean gum, in order to enhance the flexible bonding of the protein and polysaccharide interface.

8. The method of claim 7, wherein the 60Co gamma ray irradiation is performed at a dose of 10 kGy. The addition amount of locust bean gum is controlled to be 0.2%-0.8% of the dry weight of the chicken claw protein, so as to ensure the formation of the bridging structure without gelling retention effect; the pulse heat sensitive excitation treatment includes 3-5 cycles of short time heating and intermittent cooling cycle, so that the water in the microcavity structure forms a multi-stage release platform; the heat sensitive excitation treatment temperature is controlled between 60-75 ℃, so as to prevent the microcavity wall structure from collapsing while activating the opening of the hydrophobic channel.

9. The method for improving the quality of boneless chicken feet by irradiation with 60Co γ-rays according to claim 8, characterized in that: The water storage type microcavity contains flavor peptide segments and short chain fatty acid complexes, and the release sequence after heat sensitive excitation shows a sensory path of fresh in front and fragrant in back; wherein the microcavity structure after heat sensitive excitation can close part of the pores, so as to realize the release of residual flavor droplets again after the second heating; the self-induced β folding blocker is a natural plant polysaccharide with a molecular weight of less than 5 kDa, which blocks the unordered β sheet accumulation by space embedding.

10. The method for improving the quality of boneless chicken feet by irradiation with 60Co γ-rays according to claim 9, characterized in that: The blocker preferentially binds to non-polar amino acid residues to avoid premature formation of β turn structure in the cooling induction process; wherein the blocker has a self-limited release behavior and gradually degrades after cooling; the introduction of the blocker is supplemented by a molecular hydration induced slow release system, so that the action stage is concentrated within 40 seconds before the cooling of the protein chain; the β folding blocker is derived from natural plant extracts of roxburgh rose, cassia seed or black soybean skin, and is loaded into the protein chain reaction area after microencapsulation treatment.

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