A milk tea based on synergistic buffering of anserine and carnosine and a preparation method thereof
By using a synergistic buffering system of goose muscle peptide and carnosine in a specific mass ratio, along with β-cyclodextrin encapsulation and low-temperature tea polyphenol complexation, combined with a cross-flow membrane microporous cold sterilization process, the problem of metabolic disorders caused by staying up late was solved, achieving effective metabolic regulation and stability of active ingredients, while avoiding flavor conflicts and thermal degradation.
Patent Information
- Authority / Receiving Office
- CN · China
- Patent Type
- Applications(China)
- Filing Date
- 2026-06-09
- Publication Date
- 2026-07-10
AI Technical Summary
Existing functional foods and beverages cannot effectively target the surge in uric acid synthesis and aggravated anaerobic glycolysis caused by staying up late. Conventional dipeptide compounding cannot reach the effective threshold of the active center of xanthine oxidase in the liver, resulting in a single metabolic regulatory pathway and low comprehensive intervention efficacy.
A specific mass ratio of chemoresine and carnosine synergistic buffer system is used, combined with β-cyclodextrin encapsulation and low-temperature cold extraction of tea polyphenols complexation. Through steric hindrance and hydrogen bond complexation, the uric acid production pathway is blocked and lactic acid is neutralized. Combined with natural adaptogens to regulate the central nervous system, and cross-flow membrane microporous cold sterilization and aseptic cold filling process are used to ensure that the active ingredients are not degraded by heat.
It achieves targeted metabolic intervention for people who stay up late, systematically alleviates delayed acid excretion and tissue oxidative damage, maintains normal sleep cycles, and at the same time maintains the stability of product flavor and active ingredients.
Smart Images

Figure CN122350199A_ABST
Abstract
Description
Technical Field
[0001] This invention relates to the field of food and beverage processing technology, specifically to a milk tea based on the synergistic buffering of goose muscle peptide and carnosine and its preparation method. Background Technology
[0002] With the accelerated pace of modern life, metabolic disorders caused by long-term sleep deprivation and night shift work are becoming increasingly prominent, mainly manifested as abnormal uric acid metabolism, excessive lactic acid accumulation, and tissue glycation caused by oxidative stress. Carnosine (β-alanyl-L-histidine) and anserine (β-alanyl-1-methyl-L-histidine), as naturally occurring histidine dipeptides widely found in the skeletal muscle and brain of vertebrates, play crucial roles in the body due to their unique imidazole ring and free amino groups. They function as key bioactive molecules in functional foods, playing vital roles in proton buffering, antioxidation, and regulation of purine metabolism.
[0003] In existing functional food and beverage processing technologies, interventions targeting fatigue and metabolic stress mainly fall into two categories. On the one hand, traditional energy-boosting drinks typically use water or tea as a base, directly adding central nervous system stimulants such as caffeine and taurine to maintain short-term alertness. On the other hand, in peptide-based nutritional beverage systems containing carnosine or anserine, related products often focus on sports nutrition or general health maintenance. Their formulations typically add free carnosine alone as a lactic acid buffer after exercise, or simply combine carnosine and anserine in a standard 1:1 ratio to prepare liquid oral solutions or solid beverage powders.
[0004] However, conventional dipeptide compound systems in existing technologies cannot achieve targeted metabolic intervention for the specific physiological damage caused by people who stay up late. The specific metabolic disorders caused by staying up late are characterized by a surge in uric acid synthesis and aggravated anaerobic glycolysis. The conventional design of existing products with moderate compounding or carnosine as the main component results in an excessively low absolute concentration of carnosine in the system. Its molecular structure cannot reach the effective threshold required to bind to and saturate the active site of hepatic xanthine oxidase. As a result, the products cannot block the catalytic oxidation pathway of purine to uric acid from the metabolic source. Moreover, in the complex physiological internal environment, they cannot simultaneously address the continuous consumption of free hydrogen ions and reducing sugars. Therefore, conventional formulas exhibit the defects of single metabolic regulatory pathway and low comprehensive intervention efficacy when dealing with the severe delayed uric acid excretion and tissue oxidative damage caused by night shift work. Summary of the Invention
[0005] To address the shortcomings of existing technologies, this invention provides a milk tea based on the synergistic buffering of goose muscle peptide and carnosine, and its preparation method, thus solving the problems mentioned in the background section.
[0006] To achieve the above objectives, the present invention provides the following technical solution: In a first aspect, the present invention provides a milk tea based on the synergistic buffering of chemoresin and carnosine, employing the following technical solution: A milk tea based on the synergistic buffering of chemoresin and carnosine, comprising, by weight percentage, the following components: 0.15% to 0.45% of a core dipeptide complex; 5.0% to 10.0% of a plant-based or A2 milk powder matrix; 0.02% to 0.08% of a natural adaptogen and neuromodulator; 0.05% to 0.15% of an anti-glycation and metabolic cofactor; 1.0% to 5.0% of a sweetener; 0.5% to 2.0% of a flavor modifier; 0.05% to 0.15% of a pH buffering system; the balance being water or cold-brewed tea liquid; wherein, the core dipeptide complex internally encapsulates chemoresin and carnosine, and the mass ratio of chemoresin to carnosine is 3:1 to 4:1.
[0007] By employing the above technical solution, and by using a core dipeptide complex with a specific mass ratio combined with a non-caffeine-based neuromodulation system, targeted intervention for physiological damage during night shifts was achieved. The specific biochemical mechanism and reaction process are as follows: First, metabolic buffering intervention. Anserine and carnosine in a mass ratio of 3:1 to 4:1 enter the body. The 1-methylhistidine group in the anserine molecule binds to the active site of xanthine oxidase in the human liver, blocking the catalytic pathway of xanthine substrate oxidation to uric acid through steric hindrance, thus reducing serum uric acid synthesis. Carnosine uses its imidazole ring to accept free hydrogen ions, neutralizing blood lactate produced by anaerobic glycolysis. The non-equivalent high anserine molecule ratio ensures the binding saturation of the xanthine oxidase reaction site while retaining sufficient carnosine to maintain the system's anti-lactate capacity. Second, blocking non-enzymatic glycation processes. The free amino groups in carnosine preferentially undergo nucleophilic addition reactions with the carbonyl groups of free glucose in the body, consuming the dicarbonyl intermediates of glycosylation and reducing the cross-linking deposition of advanced glycation end products (AGEs) in subcutaneous tissue. The third step involves central nervous system regulation. Natural adaptogens and neuromodulators penetrate the blood-brain barrier, promoting the release of inhibitory neurotransmitters in the brain and regulating the electroencephalogram (EEG) state of the prefrontal cortex. This mechanism replaces the unidirectional excitatory effect of caffeine's competitive binding to adenosine receptors, avoiding compensatory fatigue sluggishness in the central nervous system, maintaining cognitive reaction speed during work hours without interfering with normal sleep cycles after get off work.
[0008] Preferably, the core dipeptide complex is a powder that has undergone dual modification treatment, including β-cyclodextrin encapsulation and low-temperature cold extraction with tea polyphenol complexation. This technical solution resolves the flavor conflict caused by the addition of free dipeptides. The reaction process is as follows: β-cyclodextrin molecules provide a hydrophobic cavity, and the hydrophobic side chain groups of anserine and carnosine molecules enter the cavity to form a host-guest inclusion complex, physically isolating odor molecules from contact with human olfactory receptors. Tea polyphenols contain polyphenolic hydroxyl groups, which, at low temperatures, undergo a weak complexation reaction with the terminal amino groups of the peptide chains exposed outside the inclusion complex via hydrogen bonds and van der Waals forces. This alters the local charge distribution of the peptide segments, neutralizing the metallic astringency produced by the complexation of trace metal ions by histidine residues.
[0009] Preferably, the plant-based or A2 milk powder matrix is selected from one or more combinations of oat protein powder, pea protein powder, and skimmed A2 β-casein milk powder; the natural adaptogens and neuromodulators are selected from one or more combinations of L-theanine, γ-aminobutyric acid, and Rhodiola rosea extract; and the anti-glycation and metabolic cofactors are selected from one or more combinations of vitamin B6, vitamin B12, chromium yeast, and mulberry leaf extract. By adopting the above technical solution, the risk of A1 casein in ordinary milk matrix is eliminated by removing it, thus improving the biochemical compatibility of the mixed system. L-theanine and other substances synergistically regulate neuronal activity, while mulberry leaf extract and chromium yeast participate in glucose and lipid metabolism cycles, helping the dipeptide complex maintain stable nighttime blood glucose levels.
[0010] Preferably, the pH buffer system consists of sodium citrate and dipotassium hydrogen phosphate, and the pH buffer system maintains the pH value of the milk tea system between 6.6 and 6.8. By adopting the above technical solution, the pH of the liquid system is stabilized within the range that avoids the isoelectric points of plant proteins and casein, preventing protein aggregation and laminar flow phenomena in the emulsion during processing and shelf life.
[0011] Preferably, the mass ratio of anserine to carnosine in the core dipeptide complex is 3.5:1; the sweetener is composed of erythritol and mogroside in a mass ratio of 100:1 to 200:1. By adopting the above technical solution, a quantitative balance is achieved between the free amino group consumption rate and the xanthine oxidase inhibition rate, and total sugar intake is controlled, eliminating the risk of tooth decay and additional blood sugar fluctuations.
[0012] Secondly, this invention provides a method for preparing milk tea based on the synergistic buffering of chemoresin and carnosine, employing the following technical solution: A method for preparing milk tea based on the synergistic buffering of chemoresin and carnosine includes the following steps: S1, tea milk base preparation: mixing plant-based or A2 milk powder matrix, flavor modifiers, and a portion of water or cold-brewed tea liquid, followed by emulsification and high-pressure homogenization to obtain a tea milk base; S2, aseptic active solution preparation: dissolving the core dipeptide complex, natural adaptogens and neuromodulators, anti-glycation and metabolic cofactors, and pH buffering system in the remaining water or cold-brewed tea liquid, followed by cross-flow membrane cold sterilization filtration to obtain a sterile active solution; S3, cold mixing and cold filling: after ultra-high temperature instantaneous sterilization and cooling of the tea milk base obtained in step S1, pumping it into a sterile environment, mixing it evenly with the sterile active solution obtained in step S2, and performing aseptic cold filling to obtain the final product.
[0013] By adopting the above technical solution, the problems of thermal degradation and Maillard browning of highly active dipeptides and plant extracts during the traditional hot processing of milk tea are solved. The engineering mechanism is as follows: macromolecular milk protein materials are sterilized separately with heat-sensitive dipeptides and adaptants. The tea milk base is sterilized at high temperature to destroy heat-resistant microorganisms, while the dipeptide and vitamin system containing free amino groups are sterilized separately at room temperature through microporous physical interception. The two groups of sterile materials are combined at low temperature, which prevents the thermally driven carbonyl-amine condensation reaction between free amino groups and reducing sugars in the system, ensuring the concentration of active substances and the pure color of the finished product.
[0014] Preferably, the core dipeptide complex is prepared in advance by the following specific preparation method: A 6% to 10% (w / w) aqueous solution of β-cyclodextrin and a 5% to 8% (w / w) aqueous solution of free dipeptides are prepared, wherein the free dipeptide aqueous solution contains anserine and carnosine in a mass ratio of 3:1 to 4:1; the free dipeptide aqueous solution is added dropwise to the β-cyclodextrin aqueous solution, controlling the mass ratio of the total amount of dipeptides to β-cyclodextrin to be 1:5 to 1:7, and stirred at 35 to 45°C for 1.5 to 2.5 hours to form a primary inclusion complex micelle solution; the primary inclusion complex micelle solution is cooled to 20 to 25°C, and a low-temperature cold-extracted tea polyphenol solution is added dropwise at a ratio of total peptide mass to dry matter of tea extract of 10:1 to 15:1, and the reaction is stirred for 30 to 60 minutes, followed by vacuum freeze-drying to obtain the core dipeptide complex powder. By adopting the above technical solution, the physicochemical parameter boundaries of supramolecular assembly are defined. A mass ratio of 1:5 to 1:7 ensures that β-cyclodextrin is in excess concentration, promoting complete entry of the dipeptide substrate into the cavity. Thermodynamic conditions of 35 to 45°C increase molecular kinetic energy and accelerate the encapsulation process. The dropping environment of 20 to 25°C restricts the thermal motion of molecules, promoting the formation of stable secondary weak bond complexes between the phenolic hydroxyl groups of tea polyphenols and the terminal amino groups of the polypeptide.
[0015] Preferably, in step S1, the high-pressure homogenization process employs a two-stage homogenization process, where the first-stage homogenization pressure is controlled at 15 to 20 MPa, and the second-stage homogenization pressure is controlled at 3 to 5 MPa. By adopting the above technical solution, the first-stage homogenization generates strong shear force and cavitation effect to break down fat globules and protein aggregates, while the second-stage homogenization releases pressure to prevent the broken micro-droplets from re-aggregating due to Brownian motion, thereby improving the long-term physical suspension stability of the plant-based emulsion.
[0016] Preferably, step S2 is implemented as follows: cross-flow membrane cold sterilization filtration uses a filter membrane with a pore size of 0.20 to 0.22 micrometers, and filtration is carried out at an operating pressure of 0.1 to 0.3 MPa and a feed solution temperature of 20 to 25°C. By adopting the above technical solution, the spatial steric hindrance of the filter membrane pore size physically intercepts bacterial vegetative cells, and the operating pressure of 0.1 to 0.3 MPa avoids conformational deformation of water-soluble polypeptide macromolecules due to high shear pressure and membrane surface fouling and clogging.
[0017] Preferably, in step S3, the tea milk base is subjected to ultra-high temperature instantaneous sterilization at 135 to 137°C for 4 to 5 seconds, followed by rapid cooling to below 30°C. During the aseptic mixing process, the stirring speed is controlled at 50 to 100 rpm, and the aseptic cold filling temperature is controlled at 15 to 25°C. By adopting the above technical solution, the extremely short-time heat treatment of the tea milk base preserves the amino acids and flavor lipids of the tea base while achieving commercial aseptic conditions. The extremely low stirring speed of 50 to 100 rpm during the mixing stage provides a lower limit to the shear force required for macroscopic fluid mixing, preventing high-speed mechanical forces from damaging the physical structure of the pre-constructed β-cyclodextrin dipeptide microcapsules.
[0018] This invention provides a milk tea based on the synergistic buffering of chemoresin and carnosine, and its preparation method. It has the following beneficial effects: 1. This invention achieves targeted intervention for physiological metabolic disorders in people who work night shifts by limiting the specific mass ratio of anserine to carnosine in the core dipeptide complex to 3:1 to 4:1. This ratio increases the absolute concentration of anserine to fully bind to the active site of hepatic xanthine oxidase, inhibiting excessive uric acid synthesis caused by night shift work; at the same time, the retained carnosine component plays a role in buffering hydrogen ions and competitively binding free glucose, neutralizing lactic acid produced by anaerobic glycolysis and blocking the non-enzymatic glycation process in the dermis, thereby systematically alleviating the delayed acid excretion and tissue oxidative damage caused by night shift work.
[0019] 2. This invention employs a dual modification process combining β-cyclodextrin encapsulation and low-temperature cold extraction of tea polyphenols to resolve the flavor conflicts and color abnormalities of functional free dipeptides in dairy-based beverages. The hydrophobic cavity provided by β-cyclodextrin physically isolates the animalic odor groups of the dipeptide, while the phenolic hydroxyl groups of tea polyphenols alter the charge distribution at the peptide chain ends through hydrogen bonding, neutralizing the metallic astringency caused by histidine residues. Combined with the optical masking effect of the natural color of tea polyphenols, this effectively masks the dullness that easily occurs when peptides are mixed with milk proteins, maintaining the pure sensory quality of the final product.
[0020] 3. This invention employs a compartmentalized dispensing process combining cross-flow membrane microporous cold sterilization and aseptic cold filling, overcoming the defects of thermal degradation and discoloration of highly active peptides in traditional beverage thermal processing. By separately sterilizing the heat-sensitive dual-peptide active liquid containing free amino groups through room temperature physical filtration, and then mixing it with a tea milk base sterilized at ultra-high temperature in an aseptic low-temperature environment, the conditions for the thermo-induced Maillard reaction between amino groups and reducing sugars are interrupted from the engineering path, ensuring the concentration of core active substances during the product's shelf life and preventing excessive browning of the system. Attached Figure Description
[0021] Figure 1 This is a flowchart of a milk tea preparation method based on the synergistic buffering of goose muscle peptide and carnosine. Detailed Implementation
[0022] The technical solutions in the embodiments of the present invention will be clearly and completely described below with reference to the accompanying drawings. Obviously, the described embodiments are only some embodiments of the present invention, and not all embodiments. Based on the embodiments of the present invention, all other embodiments obtained by those skilled in the art without creative effort are within the scope of protection of the present invention.
[0023] Please see the appendix Figure 1 This invention provides a milk tea based on the synergistic buffering of goose muscle peptide and carnosine and its preparation method. The main raw materials and reagents used in the following examples and comparative examples are as follows. Reagents not specifically mentioned are all commercially available food-grade, analytical grade or higher grade products. Substances that can be identified by their chemical structure characteristics or commercially available common ingredients will not be described in detail.
[0024] Goose muscle peptide (CAS No. 584-85-0), chemical name β-alanyl-1-methyl-L-histidine, molecular formula C10H16N4O3, purity ≥98.0%, is a commercially available food-grade high-purity powder.
[0025] Carnosine (CAS No. 305-84-0), chemical name β-alanyl-L-histidine, molecular formula C9H14N4O3, purity ≥98.0%, is a commercially available food-grade high-purity powder.
[0026] β-Cyclodextrin (CAS No. 7585-39-9), with the molecular formula C42H70O35 and a purity ≥98.0%, is a commercially available food-grade powder.
[0027] The tea polyphenol extract (CAS No. 84650-60-2) contains epigallocatechin gallate as its core active ingredient, with a tea polyphenol mass fraction of ≥98.0%, and is a commercially available food-grade product.
[0028] Oat protein powder with a protein content of ≥80.0% and a fineness of ≥100 mesh is a commercially available food-grade product.
[0029] Pea protein powder, after physical deodorization treatment, has a protein content of ≥80.0% and is a commercially available food-grade product.
[0030] A2β-casein milk powder, skimmed type, in which A2β-casein accounts for ≥99.0% of the total casein protein content, is a commercially available food-grade product.
[0031] L-Theanine (CAS No. 3081-61-6), chemically named N-ethyl-L-glutamine, with the molecular formula C7H14N2O3, has a purity of ≥98.0%, is free of caffeine residue, and is a commercially available food-grade extract.
[0032] γ-Aminobutyric acid (CAS No. 56-12-2), with the molecular formula C4H9NO2 and a purity ≥95.0%, is a commercially available food-grade product derived from biological fermentation.
[0033] Rhodiola rosea extract, with rhodioloside (CAS No. 10338-51-9) as the active ingredient, has a mass fraction of 5.0% and is a commercially available food-grade product.
[0034] Chromium yeast contains 2000 mg / kg of organic trivalent chromium and is a commercially available food-grade product.
[0035] Mulberry leaf extract, with 1-deoxynojirimycin (CAS No. 19130-96-2) as the core active ingredient, has a mass fraction of 2.0% and is a commercially available food-grade product.
[0036] The core component of the monk fruit glycoside extract is monk fruit glycoside V (CAS No. 88901-36-4), with a mass fraction of monk fruit glycoside V ≥ 50.0%, making it a commercially available food-grade product.
[0037] Preparation Example 1: This preparation example provides a dual-modified dipeptide complex supported by a lower parameter limit, comprising the following steps: Deionized water was heated to 50°C, and β-cyclodextrin was added. The mixture was stirred continuously until completely dissolved, preparing a 6% (w / w) β-cyclodextrin aqueous solution. Anserine and carnosine were weighed at a 3:1 mass ratio and dissolved in deionized water to prepare a 5% (w / w) free dipeptide aqueous solution. The free dipeptide aqueous solution was slowly added dropwise to the β-cyclodextrin aqueous solution, maintaining a 1:5 mass ratio of total dipeptide to β-cyclodextrin. The system temperature was adjusted to 35°C, and the mixture was magnetically stirred at a shear rate of 500 rpm for 2.5 hours in the dark to form a primary inclusion complex micelle solution. Green tea raw materials were weighed and added to purified water at 4°C at a tea-to-water mass ratio of 1:20. The mixture was statically cold-extracted in a sealed container for 12 hours. After centrifugation, the supernatant was filtered through a 0.22-micron microporous membrane to obtain a cold-extracted tea polyphenol solution with a defined dry matter content. The primary inclusion complex micelle solution was cooled to 20°C, and low-temperature cold-extracted tea polyphenol solution was slowly added dropwise at a ratio of total peptide mass to dry matter of tea extract of 15:1. The reaction was carried out at a low stirring speed of 150 rpm for 30 minutes to complete the secondary modification. The modified composite solution was then subjected to vacuum freeze-drying at a pre-freezing temperature of -50°C, a sublimation drying vacuum of 10 Pa, and a desorption drying temperature not exceeding 35°C. After grinding through a 100-mesh sieve, the double-modified dipeptide complex powder was obtained.
[0038] Preparation Example 2: This preparation example provides a parameter-upper-level supported dual-modified dipeptide complex, comprising the following steps: Deionized water was heated to 60°C, and β-cyclodextrin was added. The mixture was stirred continuously until completely dissolved, preparing a 10% (w / w) β-cyclodextrin aqueous solution. Anserine and carnosine were weighed at a mass ratio of 4:1 and dissolved in deionized water to prepare an 8% (w / w) free dipeptide aqueous solution. The free dipeptide aqueous solution was slowly added dropwise to the β-cyclodextrin aqueous solution, maintaining a mass ratio of total dipeptide to β-cyclodextrin of 1:7. The system temperature was adjusted to 45°C, and the mixture was magnetically stirred at a shear rate of 300 rpm for 1.5 hours in the dark to form a primary inclusion complex micelle solution. Green tea raw materials were weighed and added to purified water at 10°C, with a tea-to-water mass ratio of 1:15. The mixture was statically cold-extracted at low temperature for 8 hours in a sealed container. After centrifugation, the supernatant was filtered through a 0.22-micron microporous membrane to obtain a cold-extracted tea polyphenol solution with a defined dry matter content. The primary inclusion complex micelle solution was cooled to 25°C, and low-temperature cold-extracted tea polyphenol solution was slowly added dropwise at a ratio of total peptide mass to dry matter of tea extract of 10:1. The reaction was carried out at a low stirring speed of 200 rpm for 60 minutes to complete the secondary modification. The modified composite solution was then subjected to vacuum freeze-drying at a pre-freezing temperature of -40°C, a sublimation drying vacuum of 20 Pa, and a desorption drying temperature not exceeding 35°C. After grinding through a 100-mesh sieve, the double-modified dipeptide complex powder was obtained.
[0039] Preparation Example 3: This preparation example provides a dual-modified dipeptide complex supported by preferred parameters, comprising the following steps: Deionized water was heated to 55°C, and β-cyclodextrin was added. The mixture was stirred continuously until completely dissolved, preparing an 8% (w / w) β-cyclodextrin aqueous solution. Anserine and carnosine were weighed at a mass ratio of 3.5:1 and dissolved in deionized water to prepare a 6% (w / w) free dipeptide aqueous solution. The free dipeptide aqueous solution was slowly added dropwise to the β-cyclodextrin aqueous solution, maintaining a mass ratio of total dipeptide to β-cyclodextrin of 1:6. The system temperature was adjusted to 40°C, and the mixture was magnetically stirred at a shear rate of 400 rpm for 2.0 hours in the dark to form a primary inclusion complex micelle solution. Green tea raw materials were weighed and added to purified water at 7°C, with a tea-to-water mass ratio of 1:18. The mixture was statically cold-extracted at low temperature in a sealed container for 10 hours. After centrifugation, the supernatant was filtered through a 0.22-micron microporous membrane to obtain a cold-extracted tea polyphenol solution with a defined dry matter content. The primary inclusion complex micelle solution was cooled to 22°C, and low-temperature cold-extracted tea polyphenol solution was slowly added dropwise at a ratio of total peptide mass to dry matter of tea extract of 12:1. The reaction was carried out at a low stirring speed of 180 rpm for 45 minutes to complete the secondary modification. The modified composite solution was then subjected to vacuum freeze-drying at a pre-freezing temperature of -45°C, a sublimation drying vacuum of 15 Pa, and a desorption drying temperature not exceeding 35°C. After grinding through a 100-mesh sieve, the double-modified dipeptide complex powder was obtained.
[0040] Example 1: This embodiment provides a roasted oolong tea with a liver-protecting and anti-late-night functional formula. By weight percentage, its formula includes: 0.15% of the core dipeptide complex obtained in Preparation Example 1, 5.0% oat protein powder, 0.08% L-theanine, 0.15% mulberry leaf extract, 0.5% roasted oolong tea powder, 5.0% erythritol, an appropriate amount of pH buffer composed of sodium citrate and dipotassium hydrogen phosphate, and the remainder being purified water; including the following steps: Roasted oolong tea powder was extracted with purified water at 4℃ for an extended period of 10 hours (tea-to-water ratio 1:50). The extracted tea liquor was then filtered to obtain a cold-extracted tea infusion. Oat protein powder was slowly added to purified water preheated to 45℃ and dispersed for 10 minutes at 3000 rpm using a high-shear emulsifier to ensure full protein hydration. The dissolved emulsion was then mixed with the tea liquor, erythritol was added, and the mixture was subjected to two-stage homogenization in a high-pressure homogenizer. The first homogenization pressure was 15 MPa, and the second homogenization pressure was 3 MPa, resulting in a homogenized tea emulsion base. The tea emulsion base was then treated with ultra-high temperature instantaneous sterilization at 135℃ for 4 seconds, followed by rapid cooling to 20℃ via a plate heat exchanger and pumped into a sterile mixing tank for later use. A high-concentration active aqueous solution was prepared by dissolving the core dipeptide complex, L-theanine, mulberry leaf extract, and pH buffer in a small amount of purified water. This solution was then filtered and sterilized at room temperature using a 0.22-micron microporous membrane. The resulting sterile active solution was pumped online into the aforementioned sterile mixing tank. The pH of the system was monitored and adjusted online to stabilize at 6.6. The system was then stirred at a low speed of 50 rpm for 15 minutes until completely homogeneous. The solution was then directly fed into a Class 100 cleanroom-grade aseptic filling machine, where it was cold-filled into sterile packaging bottles at 15°C and sealed to obtain the finished product.
[0041] Example 2: This embodiment provides a rich cocoa anti-glycation repair and anti-late-night functional milk tea. By weight percentage, its formula includes: 0.45% of the core dipeptide complex obtained in Preparation Example 2, 10.0% of skimmed A2 β-casein milk powder, 0.05% γ-aminobutyric acid, 0.10% chromium yeast, 2.0% skimmed cocoa powder, 1.0% of a compound sweetener (erythritol and mogroside in a mass ratio of 100:1), an appropriate amount of a pH buffer composed of sodium citrate and dipotassium hydrogen phosphate, and the remainder being cold-brewed green tea liquid; including the following steps: Green tea leaves were extracted with purified water at 10℃, with a tea-to-water mass ratio of 1:30 and an extraction time of 6 hours. The resulting cold-extracted green tea liquid was obtained after filtration. Skimmed A2 β-casein milk powder and skimmed cocoa powder were slowly added to a portion of the preheated (55℃) cold-extracted green tea liquid. The mixture was dispersed for 15 minutes at 5000 rpm using a high-shear emulsifier. A compound sweetener was added, and the mixture was then subjected to two-stage homogenization in a high-pressure homogenizer. The first homogenization pressure was 20 MPa, and the second homogenization pressure was 5 MPa, yielding a tea milk base. The tea milk base was then subjected to ultra-high temperature sterilization at 137℃ for 5 seconds, cooled to 30℃, and transferred to a sterile mixing tank. The core dipeptide complex, γ-aminobutyric acid, chromium yeast, and pH buffer were dissolved in a small amount of purified water to prepare a solution. After cold filtration and sterilization through a microporous membrane with a pore size of 0.20 micrometers, the solution was aseptically pumped into a sterile mixing tank. The pH of the system was monitored and adjusted online to 6.8, and the mixture was stirred at a low speed of 100 rpm for 20 minutes. The uniformly mixed sterile solution was then cold-filled into packaging bottles at 25°C and sealed to obtain the finished product.
[0042] Example 3: This embodiment provides a vanilla black tea brain-boosting and anti-late-night functional milk tea. By weight percentage, its formula includes: 0.30% of the core dipeptide complex obtained in Preparation Example 3, 8.0% pea protein powder, 0.02% Rhodiola rosea extract (calculated as rhodioloside), 0.05% B vitamin complex, 1.0% natural vanilla pod extract, 3.0% erythritol, an appropriate amount of pH buffer composed of sodium citrate and dipotassium hydrogen phosphate, and the remainder being cold-brewed black tea liquid; including the following steps: Black tea leaves were extracted with purified water at 7°C with a tea-to-water ratio of 1:40 for 8 hours. The extracted tea liquid was then filtered to obtain a cold-extracted black tea liquor. Pea protein powder was slowly added to a portion of the cold-extracted black tea liquor preheated to 50°C, and the mixture was emulsified under high shear for 12 minutes. Natural vanilla pod extract and erythritol were then added, and the mixture was subjected to two-stage homogenization in a high-pressure homogenizer. The first-stage homogenization pressure was 18 MPa, and the second-stage homogenization pressure was 4 MPa, yielding a tea emulsion base. The tea emulsion base was then subjected to ultra-high temperature sterilization at 135°C for 4 seconds, rapidly cooled to 25°C, and stored in a sterile mixing tank. The core dipeptide complex, Rhodiola rosea extract, B vitamins, and pH buffer were dissolved in a small amount of purified water to prepare an active solution. This solution was then sterilized by cold filtration through a 0.22-micron pore size membrane and aseptically added to the mixing tank. The pH was monitored and stabilized at 6.7 online, and the mixture was continuously stirred at 80 rpm for 18 minutes. The fully homogenized liquid enters the aseptic filling machine, where it is cold-filled and sealed at 20°C to obtain the finished product.
[0043] Example 4: This embodiment provides a compound plant-based anti-late-night functional milk tea. By weight percentage, its formula includes: 0.25% of the core dipeptide complex obtained in Preparation Example 3, mixed plant milk powder (4.0% oat protein powder and 3.0% pea protein powder), 0.04% L-theanine, 0.02% γ-aminobutyric acid, 0.10% mulberry leaf extract, 0.8% roasted oolong tea powder, 2.0% erythritol, an appropriate amount of pH buffer composed of sodium citrate and dipotassium hydrogen phosphate, and the remainder being purified water; including the following steps: Low-temperature cold-extracted tea liquor was obtained by extracting roasted oolong tea powder with purified water at 5℃. Mixed plant milk powder was slowly added to purified water preheated to 48℃ for 10 minutes for dispersion and emulsification. This emulsion was then mixed with the tea liquor and erythritol and subjected to two-stage homogenization: a first-stage homogenization pressure of 16 MPa and a second-stage homogenization pressure of 3.5 MPa, yielding a tea milk base. This tea milk base was subjected to ultra-high temperature sterilization at 135℃ for 4 seconds, followed by rapid cooling to 22℃ and placed in a sterile environment. A solution was prepared by dissolving the core dipeptide complex, L-theanine, γ-aminobutyric acid, mulberry leaf extract, and pH buffer in water. This solution was then cold-filtered using a 0.20-micron microporous membrane for sterilization and aseptically pumped into a mixing tank containing the tea milk base. The pH of the system was adjusted to 6.7, and the mixture was stirred at 60 rpm for 15 minutes. The mixed solution was then aseptically cold-filled and sealed at 18℃ to obtain the finished product.
[0044] Comparative Example 1: Compared with Example 3, the difference is that β-cyclodextrin was not used for host-guest encapsulation modification. Instead, the aqueous solutions of chemoresine and carnosine were directly mixed with the low-temperature cold-extracted tea polyphenol solution and then freeze-dried to obtain the dipeptide powder. All other aspects were the same.
[0045] Comparative Example 2: Compared with Example 3, the difference is that the low-temperature cold extraction of tea polyphenols was not used for secondary complexation modification. Instead, the primary inclusion complex micelles formed by β-cyclodextrin encapsulation were directly freeze-dried to obtain the dipeptide powder. All other aspects are the same.
[0046] Comparative Example 3: Compared with Example 3, the difference is that the core dipeptide complex was not subjected to double modification treatment, that is, free anserine and carnosine mixed powder was added directly in the same mass ratio, and the rest were the same.
[0047] Comparative Example 4: Compared with Example 3, the difference is that the compartmentalized microfiltration cold sterilization and online aseptic filling process were not used. Instead, the core dipeptide complex and all adaptogens and excipients were directly added to the tea milk base, mixed evenly, and then subjected to ultra-high temperature instantaneous sterilization at 135°C for 4 seconds and cooled for filling. All other aspects were the same.
[0048] Comparative Example 5: Compared with Example 3, the difference is that the ratio of the core dipeptide complex was changed, that is, the mass ratio of chemorepeptide to carnosine in the dual-modified powder was adjusted from 3.5:1 to the conventional 1:1, while the total amount of dual-modified powder added remained unchanged, and all other aspects were the same.
[0049] Test Example 1: Feasibility and Stability Evaluation of the Invention This test case evaluates the sensory flavor and tests the thermal stability of active ingredients in the products of Examples 1 to 4 and Comparative Examples 1 to 4.
[0050] The experimental steps are as follows: Fifteen sensory evaluators were selected to conduct blind tests on the samples at 25°C. Evaluators rinsed their mouths with purified water before each sample evaluation, with a 5-minute interval between each evaluation. Scoring was based on a 100-point scale. Evaluation dimensions and weights included: residual fishy odor (30%), with higher scores indicating lower fishy odor; residual metallic astringency (30%), with higher scores indicating lower odor residue; body consistency (20%), with higher scores indicating more uniform texture; and color (20%), with higher scores indicating color more consistent with the labeled flavor and no abnormal browning. The overall sensory score was the sum of the products of each individual score and its corresponding weight.
[0051] Stability analysis was performed using accelerated aging tests. Each group of samples was placed in a constant temperature and humidity chamber at 37℃ and 75% relative humidity for 90 days. After aging, 10 mL of each sample was added to an equal volume of 10% trichloroacetic acid solution to precipitate and demulsify. The mixture was centrifuged at 8000 rpm for 15 minutes, and the supernatant was filtered through a 0.45 μm filter. High-performance liquid chromatography (HPLC) with a UV detector was used for detection. The chromatographic column was a C18 reversed-phase column (250 mm × 4.6 mm, 5 μm); the mobile phase was a mixture of 0.05 mol / L potassium dihydrogen phosphate solution and acetonitrile (90:10, v / v); the flow rate was 1.0 mL / min; the detection wavelength was 210 nm; and the column temperature was 30℃. An external standard method was used to establish a standard curve to calculate the retention rates of chemoresin and carnosin.
[0052]
[0053] Table 1. Sensory evaluation and core component retention rate test results of milk tea samples Data Results and Mechanism Analysis: Based on the data in Table 1, the example group achieved high scores and retention rates in sensory evaluation and component stability. Comparative Example 1, without β-cyclodextrin encapsulation, had a fishy odor residue score of 42.6. Comparative Example 2, without tea polyphenol complexation, had a metallic astringent odor score of 47.1 and a low color quality score. Data comparison shows that a single treatment cannot mask the dipeptide odor. This scheme utilizes a host-guest physical cavity structure and a hydrogen bond complexation mechanism. The outer layer of the β-cyclodextrin molecule is hydrophilic, while the inner cavity is hydrophobic. The hydrophobic side chain groups of anserine and carnosine molecules enter the cyclodextrin cavity to form an inclusion complex, physically isolating the odor molecules from contact with the receptor. Tea polyphenol molecules contain polyphenolic hydroxyl groups, which, at low temperatures, undergo a complexation reaction with the terminal amino groups of the peptide chains exposed outside the inclusion complex via hydrogen bonds and van der Waals forces. Secondary bond binding alters the charge distribution of the peptide segments, neutralizing the metallic odor produced by the complexation of metal ions by histidine residues. The tea liquor base color of cold-extracted tea polyphenols has an optical masking effect in the system, reducing the dullness of polypeptide substances in the emulsion system. The color scores of the example group were all above 90.
[0054] Regarding chemical stability, after 90 days of accelerated testing, the retention rates of anserine and carnosine in the example group were both above 94%. Comparative Example 4, which underwent ultra-high temperature instantaneous sterilization at 135℃, showed a decrease in anserine retention rate to 62.5% and carnosine retention rate to 58.3%, with a color score of 68.4. Carnosine and anserine contain amino groups, which undergo Maillard reactions with reducing sugars and milk proteins during high-temperature heat sterilization, leading to peptide bond breakage and browning of the system. The examples employed a compartmentalized microfiltration sterilization process, where the active peptide solution was individually cold-sterilized through a 0.2-micron filter membrane, and then mixed online with the sterilized tea-milk base under aseptic conditions. This treatment method avoids high-temperature shearing of the dipeptide system, blocking thermal denaturation and non-enzymatic saccharification reaction pathways, thus maintaining the concentration of functional substances and sensory quality in the product.
[0055] Test Example 2: In Vitro Efficacy Evaluation This test case determined the xanthine oxidase inhibition rate and the inhibition rate of advanced glycation end products formation in the products of Examples 1 to 4, Comparative Example 5, and the blank control group.
[0056] A mixed reaction system containing 0.1 mol / L phosphate buffer (pH 7.5), 0.5 mmol / L xanthine solution, and the test sample was prepared. 0.05 units / mL xanthine oxidase solution was added to initiate the reaction. The system was incubated at 25°C in a water bath for 30 minutes, and the reaction was terminated by adding 0.1 mol / L hydrochloric acid solution. The absorbance of the system at 295 nm was measured using a UV spectrophotometer. Parallel blank groups (without sample) and background groups (without enzyme solution) were set up to calculate the xanthine oxidase inhibition rate. An equal volume of 10 mg / mL bovine serum albumin solution and 0.5 mol / L fructose solution was mixed, and the test sample was added. The mixture was incubated at 37°C in the dark for 7 days. The fluorescence intensity of the reaction solution was measured using a fluorescence spectrophotometer. The excitation wavelength was set to 370 nm and the emission wavelength to 440 nm, and the inhibition rate of advanced glycation end products (AGEs) formation was calculated.
[0057]
[0058] Table 2. In vitro biochemical index inhibition rate test data of the examples and comparative examples Test results showed that the xanthine oxidase inhibition rates of Examples 1 to 4 ranged from 64.37% to 71.15%. In Comparative Example 5, the mass ratio of anserine to carnosine was adjusted to 1:1, and the xanthine oxidase inhibition rate decreased to 42.19% while maintaining the total amount of the dual-modified powder. Anserine molecules possess a 1-methylhistidine group, which can bind to the active site of xanthine oxidase, blocking the catalytic pathway of xanthine substrate oxidation to uric acid through steric hindrance. The examples used a mass ratio of 3:1 to 4:1 to increase the concentration of anserine, saturating the enzyme's active site. In Comparative Example 5, the proportion of anserine was low, failing to reach enzyme binding saturation, resulting in a decrease in the inhibitory effect of xanthine oxidase.
[0059] Anti-glycation test results showed that the inhibition rate of AGEs formation in the Example group remained between 65.41% and 69.82%, while that in Comparative Example 5 was 70.35%. Carnosine molecules contain free amino groups, which can preferentially replace protein amino groups and undergo nucleophilic addition reactions with reducing sugar carbonyl groups, consuming glycosylation intermediates and blocking non-enzymatic glycation processes. The encapsulation and complexation treatments during the preparation stage shielded the binding loss of free amino groups to milk proteins in the dairy beverage system. After the sample entered the simulated reaction environment, the free amino groups were released and participated in the anti-glycation reaction. A 3:1 to 4:1 ratio enhanced the inhibitory capacity of xanthine oxidase while maintaining a sufficient concentration of carnosine to sustain the anti-glycation reaction, achieving dual biochemical regulation of uric acid reduction and anti-glycation.
[0060] Test Example 3: Population Physiological and Biochemical Indicators and Sleep Intervention Test This test case employs a single-blind randomized controlled trial to determine the efficacy of the product in Example 3, the product in Comparative Example 5, and commercially available sugary caffeinated milk tea in terms of intervention on physiological indicators of the subjects.
[0061] Sixty participants who worked at least three night shifts per week and had not recently taken any metabolic intervention medications were randomly divided into three groups of 20 each. The intervention protocol involved a single consumption of 300 ml of the corresponding test sample during each night shift (10 PM to 2 AM the following day) for 28 consecutive days. Measurement indicators included: fasting venous blood samples were collected from the morning following the night shift, and serum uric acid concentration was measured using the uricase-peroxidase coupled colorimetric method; venous blood samples were collected immediately after the night shift, and serum lactate concentration was measured using the lactate dehydrogenase method; the Pittsburgh Sleep Quality Index (PSQI) was tested on the day before and the day after the intervention period, and the total score was calculated. All data were summarized, and invalid samples were removed before calculating the arithmetic mean.
[0062]
[0063] Table 3. Physiological and biochemical indicators and sleep scores of subjects after 28 days of continuous testing. In Example 3, after 28 days of testing, the fasting serum uric acid concentration in the morning decreased from 441.6 μmol / L to 375.2 μmol / L, the serum lactate concentration immediately after the night shift was 1.58 mmol / L, and the PSQI score decreased from 13.4 to 8.1. In the commercially available control group, all metabolic indicators showed a cumulative increase, with the PSQI score rising to 15.7.
[0064] Free dipeptides are degraded by peptidases in the gastrointestinal environment. The preparation process utilizes β-cyclodextrin encapsulation to create steric hindrance, reducing the probability of contact between pepsin and the peptide bonds of the dipeptide molecule, maintaining the structural integrity of the core component in the digestive tract and allowing it to enter the bloodstream. After entering the bloodstream, anserine carnosine targets and inhibits the activity of hepatic xanthine oxidase, reducing uric acid synthesis; carnosine accepts hydrogen ions through its imidazole ring structure, neutralizing lactic acid produced by anaerobic glycolysis and reducing blood acid load. In Comparative Example 5, with anserine carnosine to carnosine mass ratio adjusted to 1:1, the blood uric acid concentration was 419.7 μmol / L after testing, failing to achieve effective intervention. Comparative analysis confirms that a ratio of 3:1 to 4:1 is technically necessary for controlling blood uric acid levels.
[0065] The commercially available control group relied on caffeine as a central nervous system stimulant. Caffeine competitively binds to adenosine receptors, blocking fatigue signal transmission and causing compensatory sluggish excitation of the central nervous system after get off work, disrupting sleep structure and leading to an increase in PSQI scores. This formula is caffeine-free and contains L-theanine and Rhodiola rosea extract. L-theanine crosses the blood-brain barrier to promote the release of inhibitory neurotransmitters in the central nervous system and regulate brain wave states; carnosine provides protection against oxidative stress damage to neurons. Subjects experienced no receptor binding aftereffects after completing their work tasks, were able to restore their sleep cycles, and saw a reduction in PSQI scores.
[0066] Test Example 4: Evaluation of Cognitive Response and Neurophysiological State During Simulated Night Shift Work This test case uses a simulated night shift mental work experiment paradigm to quantitatively evaluate the neuromodulation effects and anti-cognitive fatigue capabilities of the product in the example, the product in Comparative Example 4, and the commercially available caffeine-containing control product.
[0067] The experimental steps are as follows: Thirty healthy participants without sleep disorders were selected and instructed to abstain from alcohol and caffeine for 48 hours prior to the test. Participants were randomly assigned to different test groups. The experiment was conducted in a standard behavioral science laboratory. Participants ingested 300 ml of the corresponding test sample at 10 PM and then performed a simulated night shift task involving continuous visual search and logical reasoning in front of a computer terminal.
[0068] At 2:00 AM the following day, the simulation was interrupted, and the subjects' transient cognitive reaction ability was tested using a psychomotor alertness task (PVT) procedure. The test lasted for 10 minutes, and the system automatically recorded the subjects' average reaction time to random visual stimuli and counted the number of errors with a reaction time exceeding 500 milliseconds.
[0069] During the PVT test, a portable multichannel EEG device was used to simultaneously acquire prefrontal cortex EEG signals from the subjects. The power spectral density of alpha waves (8-13 Hz) and beta waves (13-30 Hz) was extracted and calculated, and the alpha / beta ratio was output. A heart rate monitor was connected to acquire heart rate variability (HRV) data from the subjects, and the power of the low-frequency and high-frequency bands was extracted to calculate the LF / HF ratio.
[0070]
[0071] Table 4. Cognitive responses and neurophysiological and biochemical indicators after simulated night shift work. Analyzing the data in Table 4, the average reaction time of subjects in Examples 1 to 4 at 2 AM in the PVT ranged from 284.2 ms to 296.7 ms, with the number of missed errors remaining at a low level. The average reaction time of the commercially available control group was 268.3 ms, but its Alpha / Beta ratio decreased to 0.74, and its LF / HF ratio increased to 2.91. The reaction time of the control group in Example 4 prolonged to 345.6 ms, and the number of missed errors increased to 8.7.
[0072] The commercially available control group relied on caffeine to block adenosine receptors in the central nervous system to maintain wakefulness. This pathway triggered hyperexcitability of the sympathetic nervous system, leading to a significantly abnormally high LF / HF ratio in heart rate variability. The extremely low alpha / beta ratio in the electroencephalogram (EEG) reflected that the subjects were in a state of anxiety and excessive stress, increasing the burden on the cardiovascular system.
[0073] The formulation system of this example utilizes natural adaptogens such as L-theanine and γ-aminobutyric acid (GABA) to replace caffeine. L-theanine promotes the production of inhibitory neurotransmitters in the brain, increasing the proportion of alpha wave power in electroencephalogram (EEG) signals. Test results showed that the alpha / beta ratio in the example group remained stable between 1.35 and 1.48, and the LF / HF ratio was controlled near the normal baseline. Subjects exhibited alert and calm physiological characteristics. Free carnosine and anserine in the system penetrated the blood-brain barrier, exerting antioxidant effects, clearing reactive oxygen species accumulated in neurons during long-term work, reducing oxidative stress damage to brain tissue, and maintaining the efficiency of nerve signal transmission. This enabled the example group to maintain excellent reaction time performance even without intervention from central nervous system stimulants.
[0074] Comparative Example 4 involved treating the entire feed solution with a high-temperature instantaneous sterilization process, which led to thermal degradation of the active amino groups and reducing sugars in the core dipeptide complex, as well as Maillard reactions, resulting in the loss of neuroprotective activity of the peptides. Subjects lacking the antioxidant support of peptides exhibited significant cognitive fatigue and attention deficit, manifested as a substantial increase in reaction time and a surge in false negatives. This comparative data confirms the technical necessity of aseptic cold sterilization and cold filling processes for maintaining the formulation's neurocognitive intervention function.
[0075] Test Example 5: Testing of Skin Glycation Index and Physicochemical Indicators in Populations This test case determined the effects of Example 3, Comparative Example 4, and the purified water blank control group on the accumulation of advanced glycation end products (AGEs) and physical and biochemical indicators in the skin of night shift workers.
[0076] Forty-five female subjects who regularly work night shifts were randomly divided into three groups of 15 each. The testing period was 28 days. Subjects maintained their original skincare routines before and during the test, and were prohibited from using any new functional cosmetics. Each subject consumed 300 ml of the corresponding test sample during a single night shift. On the first day of the test and on the morning of the 29th day, subjects rested for 30 minutes in a constant temperature and humidity chamber at 20°C and 50% relative humidity before measurements were taken. The accumulation of advanced glycation end products (AGEs) in the skin of the inner forearm was measured using a non-invasive skin autofluorescence spectrometer, and the autofluorescence index was recorded. The percentage of stratum corneum moisture content in the cheekbone area of the face was measured using a stratum corneum moisture meter. The L* value of the skin in the same area was measured using a portable spectrophotometer. All measurements were repeated three times, and the arithmetic mean was taken.
[0077]
[0078] Table 5. Data on skin glycation and physical parameters of subjects after 28 days of continuous testing. The test results showed that in Example 3 group, after 28 days of testing, the skin AGEs autofluorescence index decreased from 2.41 to 2.15, the stratum corneum moisture content increased from 38.4% to 46.7%, and the skin brightness L* value increased from 61.2 to 64.8. In the blank control group, the AGEs index increased to 2.51, and both stratum corneum moisture and brightness values decreased. The changes in various test indicators were minimal in Comparative Example 4 group.
[0079] Oxidative stress caused by night shift work accelerates the non-enzymatic cross-linking reaction between collagen and reducing sugars in the dermis, generating advanced glycation end products (AGEs). These AGEs deposit under the skin, leading to browning and reduced hydration capacity of the stratum corneum. In Example 3, carnosine, once in the bloodstream, preferentially binds to the carbonyl group of glucose, competitively blocking the nucleophilic addition reaction between reducing sugars and collagen, consuming the dicarbonyl intermediate of the glycation reaction, and inhibiting the synthesis and deposition of AGEs. Carnosine also scavenges reactive oxygen species generated during night shift metabolism, reducing tissue oxidative stress levels. Together, these two components reduce the damage of glycation cross-links to the intercellular matrix, improving skin hydration and radiance.
[0080] Comparative Example 4 used a 135℃ ultra-high temperature instantaneous sterilization process to treat the entire feed solution. During the thermal processing stage, the free amino groups in the dipeptide complex underwent Maillard reactions with reducing sugars and milk proteins in the milk matrix, resulting in thermal degradation of the active ingredients and the consumption of free amino binding sites. After the subjects ingested the product, the blood could not maintain the concentration of free carnosine molecules, the non-enzymatic glycation process in the dermis was not inhibited, and AGEs continued to accumulate. The test data indicate that cold sterilization and cold filling processes are technically necessary to protect the anti-glycation activity of the dipeptide.
[0081] Although embodiments of the invention have been shown and described, it will be understood by those skilled in the art that various changes, modifications, substitutions and alterations can be made to these embodiments without departing from the principles and spirit of the invention, the scope of which is defined by the appended claims and their equivalents.
Claims
1. A milk tea based on the synergistic buffering of chemoresin and carnosine, characterized in that, By weight percentage, it contains the following components: Core dipeptide complex: 0.15%-0.45%; Plant-based or A2 milk powder matrix: 5.0%-10.0%; Natural adaptogens and neuromodulators: 0.02%-0.08%; Anti-glycation and metabolic cofactors: 0.05%-0.15%; Sweeteners: 1.0%-5.0%; Flavor modifiers: 0.5%-2.0%; pH buffer system: 0.05%-0.15%; the remainder is water or cold-brewed tea liquid; The core dipeptide complex contains anserine and carnosine, with the mass ratio of anserine to carnosine being 3:1 to 4:1, and the sum of the weight percentages of each component being 100%.
2. The milk tea based on the synergistic buffering of chemoresin and carnosine according to claim 1, characterized in that, The core dipeptide complex is a powder that has undergone dual modification treatment, including β-cyclodextrin encapsulation and low-temperature cold extraction of tea polyphenols.
3. The milk tea based on the synergistic buffering of chemoresin and carnosine according to claim 1, characterized in that, The plant-based or A2 milk powder matrix is selected from one or more of oat protein powder, pea protein powder and skimmed A2 β-casein milk powder; The natural adaptogen and neuromodulator are selected from one or more combinations of L-theanine, γ-aminobutyric acid and Rhodiola rosea extract. The anti-glycation and metabolic cofactors are selected from one or more of vitamin B6, vitamin B12, chromium yeast and mulberry leaf extract.
4. The milk tea based on the synergistic buffering of chemoresin and carnosine according to claim 1, characterized in that, The pH buffer system is composed of sodium citrate and dipotassium hydrogen phosphate, and the pH buffer system maintains the pH value of the milk tea system at 6.6-6.
8.
5. A milk tea based on the synergistic buffering of chemoresin and carnosine according to claim 1, characterized in that, The core dipeptide complex contains anserine to carnosine in a mass ratio of 3.5:1; the sweetener is composed of erythritol and mogroside in a mass ratio of 100:1-200:
1.
6. A method for preparing milk tea based on the synergistic buffering of chemoresin and carnosine according to any one of claims 1-5, characterized in that, Includes the following steps: S1. Preparation of tea milk base: The plant-based or A2 milk powder matrix, flavor modifier and part of water or cold-extracted tea liquid are mixed and emulsified and homogenized under high pressure to obtain tea milk base; S2. Preparation of sterile active solution: Dissolve the core double peptide complex, natural adaptogen and neuromodulator, anti-glycation and metabolic cofactor and pH buffer system in the remaining water or cold-extracted tea liquid, and filter through a cross-flow membrane for cold sterilization to obtain a sterile active solution. S3. Cold Mixing and Cold Filling: The tea milk base obtained in step S1 is sterilized at ultra-high temperature and then cooled. It is then pumped into a sterile environment and mixed evenly with the sterile active solution obtained in step S2. The mixture is then aseptically cold filled to obtain the final product.
7. The method for preparing milk tea based on the synergistic buffering of chemoresin and carnosine according to claim 6, characterized in that, The core dipeptide complex was prepared in advance using the following specific preparation method: Prepare an aqueous solution of β-cyclodextrin with a mass concentration of 6%-10% and an aqueous solution of free dipeptide with a mass concentration of 5%-8%, wherein the aqueous solution of free dipeptide contains anserine and carnosine in a mass ratio of 3:1-4:
1. The free dipeptide aqueous solution was added dropwise to the β-cyclodextrin aqueous solution, and the mass ratio of the total amount of dipeptide to β-cyclodextrin was controlled at 1:5-1:
7. The mixture was stirred at 35-45℃ for 1.5-2.5 hours to form a primary inclusion complex micelle solution. Cool the primary inclusion complex micelle solution to 20-25℃, add low-temperature cold-extracted tea polyphenol solution dropwise at a ratio of total peptide mass to dry matter mass of tea extract of 10:1-15:1, stir and react for 30-60 minutes, and then freeze-dry under vacuum to obtain the core double peptide complex powder.
8. The method for preparing milk tea based on the synergistic buffering of chemoresin and carnosine according to claim 6, characterized in that, In step S1, the high-pressure homogenization process adopts a two-stage homogenization process, wherein the first-stage homogenization pressure is controlled at 15-20 MPa and the second-stage homogenization pressure is controlled at 3-5 MPa.
9. The method for preparing milk tea based on the synergistic buffering of chemoresin and carnosine according to claim 6, characterized in that, The specific implementation method of step S2 is as follows: the cross-flow membrane cold sterilization filtration uses a filter membrane with a pore size of 0.20-0.22 micrometers, and performs filtration at an operating pressure of 0.1-0.3 MPa and a feed liquid temperature of 20-25℃.
10. A method for preparing milk tea based on the synergistic buffering of chemoresin and carnosine according to claim 6, characterized in that, In step S3, the tea milk base is subjected to ultra-high temperature instantaneous sterilization technology at 135-137℃ for 4-5 seconds, followed by rapid cooling to below 30℃; the mixing process in the aseptic environment controls the stirring speed to 50-100 rpm, and the temperature of aseptic cold filling is controlled at 15-25℃.
Citation Information
Patent Citations
Process of electrodepositing metals of the platinum group
CA305840A
Woven wire fencing apparatus
CA56122A
Iron nitrides of improved high frequency electromagnetic properties
CA584850A