A preparation method of a hypoglycemic whey-pea zoobiotic double protein gastrointestinal enzymatic hydrolysate based on amino acid complementation

Abstract

The application discloses a preparation method of a blood glucose reducing whey-pea animal-plant double protein gastrointestinal enzymatic product based on amino acid complementation, and belongs to the technical fields of food processing and biological medicine. In the method, whey protein concentrate and pea protein isolate are used as raw materials, the two are compounded and subjected to hydration pretreatment, and then a double protein digestion product is prepared by using pepsin and trypsin to simulate human gastrointestinal enzymolysis in steps. The product is balanced in amino acid ratio and meets the nutritional requirements of human bodies, and has good blood glucose reducing activity. Since the preparation raw materials are all natural food components, the product has good biological safety.

Description

Technical Field

[0001] This invention belongs to the fields of food processing and biomedicine, specifically relating to a method for preparing a gastrointestinal enzymatic hydrolysate of whey protein concentrate-pea protein isolate based on complementary amino acid ratios, wherein the gastrointestinal enzymatic hydrolysate has hypoglycemic activity. Background Technology

[0002] The global prevalence of diabetes continues to expand, and postprandial hyperglycemia is a core contributing factor to insulin resistance and cardiovascular complications. Some commonly used hypoglycemic drugs have side effects such as hypoglycemia, diarrhea, and allergies, and can only relieve symptoms without providing long-term regulation of intestinal glucose metabolism; naturally derived hypoglycemic bioactive peptides have become a research hotspot due to their high safety and gentle blood sugar control.

[0003] Existing complex protein systems still have several key shortcomings: First, the amino acid composition of individual plant and animal proteins has inherent defects, and the combination ratio lacks precise optimization based on the theory of amino acid complementarity. For example, whey protein concentrate (WPC) is rich in sulfur-containing amino acids and branched-chain amino acids. Pea protein isolate (PPI) has a relatively low content of sulfur-containing amino acids, resulting in an imbalanced amino acid ratio and limited nutritional value. Second, intact, unhydrolyzed protein molecules are difficult to exert their hypoglycemic effects. Due to their large molecular weight and complex spatial conformation, the potential active sequences of unhydrolyzed protein molecules may be structurally shielded, hindering effective interaction with target enzymes such as α-glucosidase and α-amylase.

[0004] Current research on WPC-PPI compound systems mainly focuses on physicochemical processing properties such as gelation and emulsification, with less research on systematically screening for the optimal amino acid matching ratio based on amino acid complementarity theory, and even less research on the targeted enrichment of hypoglycemic active peptides using stepwise enzymatic hydrolysis technology that simulates the human gastrointestinal tract. Therefore, a preparation process for WPC-PPI gastrointestinal enzymatic hydrolysates that can simultaneously achieve optimal amino acid nutritional quality and hypoglycemic efficacy remains to be developed. Summary of the Invention

[0005] The purpose of this invention is to provide a method for preparing a hypoglycemic whey-pea plant-animal dual-protein gastrointestinal enzymatic hydrolysate based on complementary amino acid ratios, in order to solve the problems of unbalanced amino acid composition, difficulty in fully releasing hypoglycemic active peptides from undigested protein molecules, and lack of precise ratio optimization based on amino acid nutritional evaluation in existing composite protein systems.

[0006] To achieve the above objectives, the present invention adopts the following technical solution:

[0007] A method for preparing a hypoglycemic whey-pea plant-animal dual-protein gastrointestinal enzymatic hydrolysate based on amino acid complementarity includes raw material compounding, hydration pretreatment, and stepwise simulated gastrointestinal enzymatic hydrolysis. Specific operations are as follows:

[0008] Step 1: Preparation of WPC aqueous solution

[0009] WPC powder was dissolved in distilled water to prepare a 5% w / v WPC stock solution. The specific steps included: first, adding distilled water to the dry powder and stirring with a magnetic stirrer until the powder was completely dissolved, and then stirring magnetically at room temperature for 4 h, and then placing it in a refrigerator at 4-8 ℃ for hydration for 8-12 h.

[0010] Step 2: Preparation of PPI aqueous solution

[0011] PPI powder is dissolved in distilled water to prepare a 5% w / v PPI stock solution. The specific steps include: first, adding distilled water to the dry powder and stirring with a magnetic stirrer until the powder is completely dissolved, and then stirring magnetically at room temperature for 4 h, and then placing it in a refrigerator at 4-8 ℃ for hydration for 8-12 h.

[0012] Step 3: Preparation of WPC-PPI composite protein aqueous solution

[0013] The WPC solution and PPI solution were mixed to obtain a final mixture with a total protein concentration of 5% w / v and WPC to PPI mass ratios of 0:10, 1:9, 3:7, 5:5, 7:3, 9:1, and 10:0. The mixture was stirred on a vortex mixer for at least 5 min to prepare the WPC-PPI composite protein aqueous solution.

[0014] Step 4: Enzymatic digestion in the stomach

[0015] Take 10 mL of the hydrated protein stock solution, add 8 mL of gastric electrolyte solution, and adjust the pH of the system to 3 with hydrochloric acid. Add 5 μL of 0.3 M CaCl2 solution, then add pepsin to bring the final enzyme activity concentration to 2000 U / mL. Make up the volume with gastric electrolyte solution to 20 mL, and incubate at 37 ℃ and 100 rpm for 2 h to complete gastric hydrolysis.

[0016] Step 5: Intestinal stage enzymatic digestion

[0017] Add 8 mL of intestinal electrolyte solution to the entire gastric phase hydrolysis system, and adjust the pH to 7 with NaOH. Then, add 3 mL of 200 mg / mL bile salt solution and 40 μL of 0.3 M CaCl2 solution sequentially, and add trypsin to achieve an activity of 2000 U / mL. Make up the volume to 40 mL with intestinal electrolyte solution, and incubate at 37 ℃ and 100 rpm for 2 h with continuous stirring to complete the deep hydrolysis of the intestinal phase. Stop the enzymatic reaction in an ice-water bath. The resulting product is the WPC-PPI gastrointestinal enzymatic hydrolysate.

[0018] Another objective of this invention is to provide a WPC-PPI dual protein gastrointestinal enzymatic hydrolysate with a balanced amino acid profile. This meets the human body's complete essential amino acid requirements and enhances the nutritional value of protein.

[0019] Another object of the present invention is to provide an α-glucosidase and α-amylase inhibitor. Its active ingredient includes the aforementioned WPC-PPI plant-animal dual-protein gastrointestinal enzymatic hydrolysate. This WPC-PPI plant-animal dual-protein gastrointestinal enzymatic hydrolysate possesses potent inhibitory capabilities against α-glucosidase and α-amylase targets, making it suitable as a natural source inhibitor raw material for the preparation of pharmaceutical or biochemical reagents.

[0020] The beneficial effects of this invention are reflected in:

[0021] 1. The raw materials used in this invention are all food-grade commercial whey protein concentrate and pea protein isolate, and the source of the raw materials is natural and controllable.

[0022] 2. This solution scientifically combines WPC and PPI to fully preserve the unique nutritional advantages of each protein, achieve a complementary and synergistic effect of amino acids, and improve the defect of imbalance in the essential amino acid ratio of single proteins.

[0023] 3. This invention does not rely on experience to select the blending ratio of whey protein concentrate and pea protein isolate. Instead, it systematically evaluates different ratios using indicators such as the whole egg protein model, the FAO / WHO adult essential amino acid reference model, AAS, RC, and SRC. The results show that a 7:3 blend of whey protein concentrate and pea protein isolate exhibits superior nutritional matching in amino acid composition.

[0024] 4. The present invention combines whey protein concentrate and pea protein isolate in a 7:3 ratio, and then performs stepwise enzymatic hydrolysis in a simulated gastrointestinal tract to obtain the gastrointestinal enzymatic hydrolysate. While maintaining a relatively optimal composition of essential amino acids, the hydrolysate exhibits high inhibitory activity against both α-glucosidase and α-amylase, with the α-amylase inhibitory activity reaching a relatively optimal level among the tested compounding ratios.

[0025] 5. The present invention uses pepsin and pancreatin sequentially for stepwise enzymatic hydrolysis, which is beneficial to releasing the potential bioactive peptides in the complex protein, so that the obtained product has the potential to be used as a food ingredient, functional food ingredient, special dietary food ingredient or natural enzyme inhibitor ingredient. Attached Figure Description

[0026] Figure 1 The digestibility of WPC-PPI samples with different proportions is given, where A is the digestibility of WPC-PPI samples with different proportions after gastric enzymatic hydrolysis and B is the digestibility of WPC-PPI samples with different proportions after gastrointestinal enzymatic hydrolysis.

[0027] Figure 2 The images show SDS-PAGE images of WPC-PPI samples with different proportions. In the images, A is the SDS-PAGE image of WPC-PPI samples with different proportions before enzymatic digestion, B is the SDS-PAGE image of WPC-PPI samples with different proportions after 1 h of gastric digestion, C is the SDS-PAGE image of WPC-PPI samples with different proportions after 2 h of gastric digestion, 2D is the SDS-PAGE image of WPC-PPI samples with different proportions after 1 h of intestinal digestion, and E is the SDS-PAGE image of WPC-PPI samples with different proportions after 2 h of intestinal digestion.

[0028] Figure 3 The inhibition rate of α-glucosidase by gastrointestinal enzymatic hydrolysates of WPC-PPI samples with different proportions;

[0029] Figure 4 The inhibition rate of α-amylase by gastrointestinal enzymatic hydrolysates of WPC-PPI samples with different proportions. Detailed Implementation

[0030] The present invention will be further illustrated below with reference to specific embodiments. It should be understood that the embodiments are for illustrative purposes only and are not intended to limit the scope of the invention. Therefore, any modifications, equivalent substitutions, improvements, etc., made without departing from the spirit and scope of the invention should be included within the protection scope of the invention. Furthermore, the appended claims are intended to cover all variations and modifications falling within the scope and boundaries of the appended claims, or equivalent forms of such scope and boundaries.

[0031] Example 1: Determination of amino acid content with different WPC-PPI ratios

[0032] Weigh the sample into a hydrolysis tube and add 10.0 mL of 6N hydrochloric acid solution. Continue adding 50 mg of phenol to the hydrolysis tube. Place the hydrolysis tube in a refrigerant (ice-saline solution) and freeze for 3-5 minutes. Connect it to the vacuum pump's suction tube, evacuate, and then purge with nitrogen. Repeat this process three times, tightening the cap under nitrogen purging. Place the sealed hydrolysis tube in a 110°C electric heating oven for 22 hours of hydrolysis. Remove and cool to room temperature. Open the hydrolysis tube and filter the hydrolysate into a 50 mL volumetric flask, bringing the volume to 50 mL. Take 1.0 mL of the filtrate and dry it using a nitrogen blower at 60°C. Dissolve the residue in 1 mL of water and then dry it again. Dissolve the residue in 10 mL of pH sodium citrate buffer in the dried test tube, shake to mix, and then pass the solution through a 0.22 μm filter membrane to a 1.5 mL sample vial. Proline and hydroxyproline are detected at 440 nm, and other amino acids are detected at 570 nm.

[0033] Example 2: Amino acid composition analysis of proteins with different WPC-PPI ratios

[0034] 1. Fuzzy recognition method for determining protein proximity

[0035] The proximity between the target protein μ and the standard protein a was identified using the Lannister distance method, with whole egg protein and FAO / WHO models as references. The specific formula is as follows:

[0036]

[0037] In the above formula: For the target protein, For the kth type of the i-th evaluation object ( EAA content (mg / gPro), For the kth type of the i-th evaluation object ( EAA content (mg / g Pro).

[0038] The whole egg protein pattern and the FAO / WHO standard pattern are shown in Table 1:

[0039] Table 1. Content of 7 essential amino acids in whole egg protein and FAO / WHO standard protein models.

[0040]

[0041] Table 2. Relative similarity of proteins to standard proteins at different ratios

[0042]

[0043] Table 2 shows that when using the whole egg amino acid profile as the evaluation standard, the similarity between WPC and PPI is 0.9414 and 0.9172, respectively. Notably, the two proteins exhibit a synergistic effect when combined. The 7:3 combination group achieved the highest similarity, followed closely by the 5:5 group. Similarly, when using the FAO / WHO reference model, the PPI score was relatively low at 0.8535; while the 7:3 and 9:1 combination groups achieved the best results, with similarity scores of 0.9167 and 0.9175, respectively. Overall, the 7:3 combination ratio performs best. These results indicate that selecting an appropriate combination ratio (especially within the 5:5–9:1 range) can optimize the amino acid composition, making the amino acid profile of this dual-protein system closer to the ideal nutritional pattern compared to a single plant protein.

[0044] 2. Amino acid score

[0045] Using the FAO / WHO essential amino acid standard model as a reference, the amino acid ratio (AAS), amino acid ratio coefficient (RC), and amino acid ratio coefficient score (SRC) were calculated according to relevant formulas, as follows:

[0046]

[0047]

[0048]

[0049] Table 3 Comparison of AAS, RC, and SRC of WPC-PPI with different ratios

[0050]

[0051] From the perspective of SRC value, the closer the value is to 100, the closer the amino acid composition of the two proteins in this ratio is to this ideal amino acid pattern, the richer its nutritional value, and the easier it is for the human body to absorb and utilize. According to Table 3, the protein ratio of 7:3 has the highest SRC under the FAO / WHO model, indicating that the amino acid composition of this ratio of two proteins is optimal, which is more conducive to the digestion and absorption of amino acids by the human body. When the blending ratio is in the range of 5:5 to 9:1, the SRC score is improved compared to the single protein, indicating richer nutritional value.

[0052] Example 3: Preparation of Optimal Ratio of Gastrointestinal Enzymatic Hydrolysates from Two Proteins

[0053] (1) Preparation of WPC aqueous solution

[0054] To prepare a 5% w / v WPC stock solution, WPC powder is dissolved in distilled water. The specific steps include: first, adding distilled water to the dry powder and stirring with a magnetic stirrer until the powder is completely dissolved, and then stirring magnetically at room temperature for 4 hours, and then placing it in a refrigerator at 4-8°C for hydration for 8-12 hours.

[0055] (2) Preparation of PPI aqueous solution

[0056] PPI powder is dissolved in distilled water to prepare a 5% w / v PPI stock solution. The specific steps include: first, adding distilled water to the dry powder and stirring with a magnetic stirrer until the powder is completely dissolved, and then stirring magnetically at room temperature for 4 hours, and then placing it in a refrigerator at 4-8°C for hydration for 8-12 hours.

[0057] Step 3: Preparation of WPC-PPI composite protein aqueous solution

[0058] The WPC solution and PPI solution were mixed to obtain a final mixture with a total protein concentration of 5% w / v and a WPC to PPI mass ratio of 7:3. The mixture was then stirred on a vortex mixer for at least 5 minutes to prepare the WPC-PPI composite protein aqueous solution.

[0059] Step 4: Gastric enzymatic digestion (pepsin hydrolysis)

[0060] Take 10 mL of the hydrated protein stock solution, add 8 mL of gastric electrolyte solution, and adjust the pH of the system to 3 with hydrochloric acid. Add 5 μL of 0.3 M CaCl2 solution, then add pepsin to bring the final enzyme activity concentration to 2000 U / mL. Make up the volume with gastric electrolyte solution to 20 mL, and incubate at 37 ℃ and 100 rpm for 2 h to complete gastric hydrolysis.

[0061] Step 5: Intestinal stage enzymatic digestion

[0062] Add 8 mL of intestinal electrolyte solution to the entire gastric phase hydrolysis system, and adjust the pH to 7 with NaOH. Then, add 3 mL of 200 mg / mL bile salt solution and 40 μL of 0.3 M CaCl2 solution sequentially, and add trypsin to achieve an activity of 2000 U / mL. Make up the volume to 40 mL with intestinal electrolyte solution, and incubate at 37 ℃ and 100 rpm for 2 h with continuous stirring to complete the deep hydrolysis of the intestinal phase. Stop the enzymatic reaction in an ice-water bath. The resulting product is the WPC-PPI gastrointestinal enzymatic hydrolysate.

[0063] Example 4: Preparation of control WPC-PPI dual-protein gastrointestinal enzymatic hydrolysate

[0064] This embodiment provides a control sample of WPC-PPI dual-protein gastrointestinal enzymatic hydrolysate. The preparation steps are basically the same as in Example 3, except for the ratio of WPC to PPI in step 3: the WPC solution and PPI solution are mixed so that the total protein concentration in the final mixture is 5% w / v, and the mass ratio of WPC to PPI is 0:10, 1:9, 3:7, 5:5, 9:1, and 10:0, respectively. The mixture is then stirred on a vortex mixer for at least 5 minutes to prepare an aqueous solution of the WPC-PPI complex protein.

[0065] Example 5: Physicochemical characterization of gastrointestinal enzymatic hydrolysates of WPC-PPI with different ratios

[0066] 1. Digestibility characterization

[0067] Figure 1 A and Figure 1 B represents the digestibility of WPC-PPI after gastric and intestinal enzymatic digestion at different ratios. Figure 2 A represents the digestibility after continuous gastrointestinal enzymatic hydrolysis with WPC-PPI. The characterization method was as follows: the degree of enzymatic hydrolysis of the sample was assessed by changes in protein content during the gastric and intestinal hydrolysis stages. The sample was mixed with ethanol at a ratio of 1:3, vortexed, and allowed to stand for 24 h to precipitate soluble proteins that had not been degraded into amino acids and small peptides. The sample was centrifuged at 4 ℃ and 1000 r / min for 10 min, and the protein content before and after enzymatic hydrolysis was detected using a BCA protein assay kit. The in vitro digestibility of the sample was calculated as follows:

[0068]

[0069] in, and The figures indicate the protein content in the sample precipitate at the beginning and end of the enzymatic hydrolysis process. As shown in the figure, WPC exhibits the highest gastric digestibility. When WPC is combined with PPI, the gastric digestibility is significantly higher than that of pure PPI, but different combination ratios have limited effect on improving gastric digestibility. After continuous enzymatic hydrolysis in the gastrointestinal tract, all samples showed high digestibility, generally exceeding 80%. Even the pure PPI samples achieved a similar overall digestibility to WPC. These results indicate that the hydrolytic activity of intestinal trypsin can compensate for the insufficient hydrolytic capacity of pepsin in the stomach, thereby enriching more hypoglycemic peptides.

[0070] 2. SDS-polyacrylamide gel electrophoresis (SDS-PAGE)

[0071] Figure 2 AE represent SDS-PAGE images of WPC before, after 1 h of gastric digestion, after 2 h of gastric digestion, after 1 h of intestinal digestion, and after 2 h of intestinal digestion, at different ratios. The characterization method was as follows: the sample was mixed with 5× loading buffer containing β-mercaptoethanol and heated at 100°C for 8 minutes. Subsequently, SDS-PAGE electrophoresis was performed using a 12.5% ​​separating gel and a stacking gel at 100 V, with a loading volume of 5 μL per well. The gels were stained with Coomassie Brilliant Blue rapid staining solution for 2 hours, followed by destaining with deionized water. Finally, the gel images were analyzed using Image Lab™ software (version 4.0). The figures show that most proteins were fully hydrolyzed during the gastric digestion stage. Except for β-lactoglobulin in WPC, which is more difficult for pepsin to degrade, the other protein components showed a relatively fast hydrolysis rate. After 2 hours of gastric enzymatic digestion, protein bands of varying degrees were still observed in samples with different ratios within the 10–15 kDa range, and the band intensity varied with the mixing ratio, indicating that some protein components in WPC and PPI exhibited different degradation behaviors under gastric conditions. Combined with the digestibility results, it was found that the degradation degree of PPI-related protein components was relatively low under gastric conditions. Upon entering the intestinal enzymatic digestion stage, almost all protein bands on the gel disappeared, indicating that all protein groups achieved relatively thorough degradation.

[0072] Example 6: Hypoglycemic function of gastrointestinal enzymatic hydrolysates of WPC-PPI with different ratios

[0073] 1. α-glucosidase inhibition rate

[0074] The characterization method was as follows: 50 μL of sample solution and 50 μL of α-glucosidase solution were thoroughly mixed and reacted at 37℃ for 10 min. Then, 50 μL of 1 mM PNPG solution was added, and the reaction was continued at 37℃ for another 10 min. Finally, 2.5 mM sodium carbonate solution was added to terminate the reaction, and the absorbance was measured at 405 nm. Blank group A was set to add only α-glucosidase, blank control group B was set to add neither sample nor α-glucosidase, sample group C was set to add both sample and α-glucosidase, and sample control group D was set to add only sample. The α-glucosidase inhibition rate was calculated using the following formula:

[0075]

[0076] 2. α-Amylase inhibition rate

[0077] The characterization method was as follows: 500 μL of sample solution was thoroughly mixed with α-amylase solution and reacted in a 37℃ water bath for 10 min. Then, 500 μL of 1% (m / v) potato starch solution was added, and the mixture was reacted in a 37℃ water bath for another 10 min. Finally, 1 mL of DNS was added and reacted in a boiling water bath for 5 min. After cooling, 6 mL of water was added for dilution, and the absorbance was measured at 540 nm. Blank group A was set to add only α-amylase, blank control group B was set to add neither sample nor α-amylase, sample group C was set to add both sample and α-amylase, and sample control group D was set to add only sample. The α-amylase inhibition rate was calculated using the following formula:

[0078]

[0079] from Figure 3 The figure shows the α-glucosidase inhibition rate of gastrointestinal enzymatic hydrolysates of WPC-PPI at different ratios. As can be seen from the figure, the inhibition rate of all tested samples was higher than 88% for α-glucosidase inhibition activity. The single PPI group showed the lowest α-glucosidase inhibition ability. In the complex protein system, the inhibitory activity gradually increased with the increase of WPC content. When the complex ratio was in the range of 3:7 to 5:5, there was no significant difference in α-glucosidase inhibition ability (P > 0.05).

[0080] from Figure 4The figure shows the α-amylase inhibition rate of gastrointestinal enzymatic hydrolysates of WPC-PPI at different ratios. As can be seen from the figure, the PPI group had the lowest α-amylase inhibition rate, and the inhibitory activity significantly increased after the addition of WPC. When the WPC:PPI ratio was 7:3, the α-amylase inhibitory activity of the compound sample reached its peak; further excessive addition of WPC slightly decreased the inhibitory effect. Nevertheless, the α-amylase inhibitory activity of all compound groups was still significantly higher than that of the PPI group.

Claims

1. A method for preparing a hypoglycemic whey-pea plant-animal dual-protein gastrointestinal enzymatic hydrolysate based on amino acid complementarity, characterized in that, Includes the following steps: (1) Preparation of whey protein concentrate (WPC) aqueous solution Dissolve WPC powder in distilled water to prepare a 5% w / v WPC stock solution. The specific steps include: first, add distilled water to the dry powder and stir with a magnetic stirrer until the powder is completely dissolved, and then stir magnetically at room temperature for 4 hours, and then place it in a refrigerator at 4-8°C for hydration for 8-12 hours. (2) Preparation of pea protein isolate (PPI) aqueous solution PPI powder is dissolved in distilled water to prepare a 5% w / v PPI stock solution. The specific steps include: first, adding distilled water to the dry powder and stirring with a magnetic stirrer until the powder is completely dissolved, and then stirring magnetically at room temperature for 4 hours, and then placing it in a refrigerator at 4-8°C for hydration for 8-12 hours. (3) Preparation of WPC-PPI composite protein aqueous solution The WPC solution and PPI solution were mixed so that the total protein concentration in the final mixture was 5% w / v and the mass ratio of WPC to PPI was in the range of 5:5 to 9:1; the mixture was then placed on a vortex mixer and stirred for at least 5 minutes to prepare the WPC-PPI composite protein aqueous solution. (4) Enzymatic digestion in the stomach Take 10 mL of hydrated protein stock solution, add 8 mL of gastrointestinal electrolyte solution, and adjust the pH of the system to 3 with hydrochloric acid; add 5 μL of 0.3M CaCl2 solution, and then add pepsin to make the final enzyme activity concentration of the system 2000 U / mL; add electrolyte solution to make up the volume to 20 mL, and shake at 37 ℃ and 100 rpm for 2 h to complete the gastric phase hydrolysis; (5) Enzymatic digestion in the intestinal stage Add 8 mL of intestinal electrolyte solution to the entire gastric phase hydrolysis system, and adjust the pH to 7 with NaOH; add 3 mL of 200 mg / mL bile salt solution and 40 μL of 0.3 M CaCl2 sequentially, and add a mixed enzyme solution of trypsin and lipase, with the terminal activity of both enzymes being 2000 U / mL; add intestinal electrolyte solution to make up the volume to 40 mL, and incubate at 37℃ and 100 rpm for 2 h with continuous stirring to complete the deep hydrolysis of the intestinal phase. Stop the enzymatic reaction in an ice-water bath, and the obtained product is the WPC-PPI digest product.

2. The method for preparing a hypoglycemic whey-pea plant-animal dual-protein gastrointestinal enzymatic hydrolysate based on amino acid complementarity according to claim 1, characterized in that, In step 3, the mass ratio of whey protein concentrate to pea protein isolate is 7:3.

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