High internal phase emulsion as well as preparation method and application thereof in 3D (three-dimensional) food printing

Abstract

The invention discloses a high internal phase emulsion as well as a preparation method and application thereof in 3D (three-dimensional) food printing. The high internal phase emulsion is prepared by homogenizing a mixed solution of a deamidated modified pea protein solution and vegetable oil, the concentration of the deamidated modified pea protein in the high internal phase emulsion is 0.25 wt%-2.5 wt%. The deamidated modified pea protein is used as a protein stabilizer to prepare the high internal phase emulsion, and the high internal phase emulsion has excellent centrifugal stability, temperature stability and pH stability, can be kept stable under the conditions of high salt, acid-base change and high temperature, avoids the phenomena of emulsion layering and oil drop aggregation, and has good stability. The high-performance emulsion prepared by the preparation method disclosed by the invention has the advantages of high viscosity, small oil drop size and high viscosity, shows excellent rheological property, is suitable for being used as an ink material for 3D printing food, can be used for printing a food structure with high precision, self-supporting capacity and ideal texture, and meets the requirement of the modern food industry on high-performance emulsion stability.

Description

Technical Field

[0001] The present invention belongs to the field of food science and technology. More specifically, the present invention relates to an ultra-stable high internal phase emulsion stabilized by deamidated modified pea protein and a preparation method thereof, as well as an application of the ultra-stable high internal phase emulsion in 3D food printing. Background Art

[0002] As an innovative technology, 3D food printing is changing the traditional way of food manufacturing. Through computer-controlled nozzles, 3D printing can layer ingredients and create complex food structures, which not only meets consumers' demand for personalization and customization, but also optimizes the nutritional content and sensory properties of food. High Internal Phase Emulsions (HIPEs) refer to emulsions with an internal phase volume fraction of more than 0.74. Because of their adjustable texture and high loading capacity, they show great potential as 3D food printing ink materials.

[0003] However, the natural emulsifiers currently used for food-grade HIPEs have deficiencies in stability. Especially under extreme conditions such as high salt, acid-base changes and high-temperature treatment, the emulsion is prone to stratification and oil droplet aggregation, affecting its application effect and product quality in 3D food printing.

[0004] Natural biopolymers such as proteins (e.g. whey protein, soy protein and gelatin) have become potential choices for stabilizing HIPEs due to their excellent biocompatibility, biosafety and degradability. Proteins, as natural edible emulsifiers, show great potential for stabilizing HIPEs due to their unique hydrophilic / hydrophobic properties. However, the use of these proteins alone or in combination with polysaccharides is still difficult to effectively prevent oil separation and emulsion instability under harsh environments.

[0005] In order to overcome the lack of stability of existing natural emulsifiers under extreme conditions, researchers have tried to improve the stability of HIPEs by modifying proteins or compounding a variety of natural biopolymers. Although these methods have improved the stability of the emulsion to a certain extent, it is still difficult to fully meet the high requirements of 3D food printing for emulsion stability and rheological properties in practical applications. Summary of the invention

[0006] Based on this, the object of the present invention is to improve the stability and rheological properties of high internal phase emulsions.

[0007] The specific technical solutions for achieving the above-mentioned invention objectives include the following.

[0008] The first aspect of the present invention provides the use of deamidated modified pea protein in the preparation of a high internal phase emulsion.

[0009] The second aspect of the present invention provides a high internal phase emulsion, which is obtained by homogenizing a mixture of a deamidated pea protein solution and vegetable oil; the concentration of the deamidated pea protein in the high internal phase emulsion is 0.25wt% to 2.5wt%.

[0010] The third aspect of the present invention provides a method for preparing the above-mentioned high internal phase emulsion, comprising the following steps: mixing the deamidated modified pea protein solution with vegetable oil at a shear rate of 2000rpm / min to 9000rpm / min, and then homogenizing the mixed solution at a shear rate of 10000rpm / min to 20000rpm / min.

[0011] A fourth aspect of the present invention provides the use of a high internal phase emulsion in 3D food printing.

[0012] A fifth aspect of the present invention provides a method for 3D food printing, comprising the following steps: using the above-mentioned high internal phase emulsion as edible ink to print food structures.

[0013] The present invention prepares a high internal phase emulsion by using deamidated pea protein isolate (DPPI) as a protein stabilizer. The high solubility and excellent interfacial activity of DPPI are utilized to improve the stability of the high internal phase emulsion in various oil phases. The emulsion has excellent centrifugal stability, temperature stability and pH stability, and can remain stable under high salt, high temperature conditions and acid-base changes, avoiding emulsion stratification and oil droplet aggregation, thereby meeting the specific needs of 3D food printing for high-performance emulsion stabilizers.

[0014] The high internal phase emulsion of the present invention has a small oil droplet size and high viscosity, exhibits excellent rheological properties, and is suitable as an ink material for 3D printing of food. It can print food structures with high precision, self-supporting ability and ideal texture, and meet the needs of the modern food industry for high-performance emulsion stability.

[0015] The high internal phase emulsion of the present invention adopts plant-based protein as a stabilizer, which meets the requirements of green environmental protection and sustainable development, meets the growing market demand for plant-based diets, and can be prepared using a variety of vegetable oils, has a wide range of application adaptability, and can meet the requirements of different food formulations.

[0016] The preparation method of the high internal phase emulsion of the present invention has a simple process, does not require complicated protein modification steps, is easy to operate, is easy to industrialize, and significantly reduces production costs. BRIEF DESCRIPTION OF THE DRAWINGS

[0017] Figure 1This is the appearance of HIPE formed by DPPI with different protein concentrations in Experimental Example 1 of the present invention.

[0018] Figure 2 The appearance (A) and water loss rate (B) of HIPE formed by DPPI with different protein concentrations after centrifugation in Experimental Example 1 of the present invention.

[0019] Figure 3 The oil droplet diameters of HIPE stabilized by NPPI at different protein concentrations and HIPE stabilized by DPPI at different protein concentrations in Experimental Example 2 of the present invention.

[0020] Figure 4 The viscosity of HIPE stabilized by NPPI at different protein concentrations and HIPE stabilized by DPPI at different protein concentrations in Test Example 2 of the present invention.

[0021] Figure 5 The moduli of the frequency scans of HIPE stabilized by NPPI at different protein concentrations and HIPE stabilized by DPPI at different protein concentrations in Experimental Example 2 of the present invention, wherein G' is the elastic modulus, G" is the viscous modulus, the solid line in the figure is the elastic modulus, and the dotted line is the viscous modulus.

[0022] Figure 6 The microstructure of HIPE stabilized by NPPI and DPPI at different ion concentrations and pH values ​​in Experimental Example 3 of the present invention.

[0023] Figure 7 The microstructure of NPPI- and DPPI-stabilized HIPE after treatment at different temperatures in Experimental Example 3 of the present invention.

[0024] Figure 8 The changes of primary and secondary oxidation products of NPPI-stabilized HIPE and DPPI-stabilized HIPE during accelerated storage in Experimental Example 3 of the present invention.

[0025] Fig. 9 This is a comparison of the printing effects of NPPI-stabilized HIPE and DPPI-stabilized HIPE in 3D printing in Experimental Example 4 of the present invention.

[0026] Fig.10 This is the texture of the NPPI-stabilized HIPE and DPPI-stabilized HIPE printing models in Experimental Example 4 of the present invention.

[0027] In the above figure, D represents DPPI, N represents NPPI, and the number after D / N represents protein concentration (%). DETAILED DESCRIPTION

[0028] In order to facilitate the understanding of the present invention, the present invention will be described more fully below. The present invention can be implemented in many different forms and is not limited to the embodiments described herein. On the contrary, the purpose of providing these embodiments is to make the understanding of the disclosure of the present invention more thorough and comprehensive.

[0029] Unless otherwise defined, all technical and scientific terms used in the present invention have the same meaning as those commonly understood by those skilled in the art to which the present invention belongs. The terms used in the specification of the present invention are only for the purpose of describing specific embodiments and are not intended to limit the present invention. The term "and / or" used in the present invention includes any and all combinations of one or more of the related listed items.

[0030] Unless otherwise specified, the embodiments are carried out according to conventional experimental conditions or the conditions recommended in the manufacturer's instructions. The instruments, raw materials and reagents used in the present invention without indicating the manufacturer are all conventional products that can be purchased commercially.

[0031] In some embodiments of the present invention, the use of deamidated modified pea protein in preparing a high internal phase emulsion is disclosed.

[0032] In some embodiments, the deamidated modified pea protein is prepared by adding glutaminase to a pea protein solution to carry out a deamidation reaction.

[0033] In some embodiments, the reaction temperature of the deamidation reaction is 40°C to 50°C, preferably 44°C to 46°C; the reaction time of the deamidation reaction is 60min to 70min, preferably 65min to 67min.

[0034] In other embodiments of the present invention, a high internal phase emulsion is disclosed, which is obtained by homogenizing a mixture of a deamidated pea protein solution and vegetable oil; the concentration of the deamidated pea protein in the high internal phase emulsion is 0.25 wt % to 2.5 wt %.

[0035] In some embodiments, the concentration of the deamidated modified pea protein in the high internal phase emulsion is 1.0 wt% to 2.5 wt%, preferably 1.5 wt% to 2.5 wt%, and more preferably 1.9 wt% to 2.1 wt%.

[0036] In some embodiments, the volume percentage of vegetable oil in the mixed liquid is 65% to 80%, preferably 70% to 77.5%, and more preferably 74% to 76%.

[0037] In some embodiments, the vegetable oil is sunflower oil, soybean oil, corn oil, rice bran oil, linseed oil, camellia oil, peanut oil, and / or perilla oil.

[0038] In other embodiments of the present invention, a method for preparing the above-mentioned high internal phase emulsion is disclosed, comprising the following steps: mixing the deamidated modified pea protein solution with vegetable oil at a shear rate of 2000rpm / min to 9000rpm / min, and then homogenizing the mixed solution at a shear rate of 10000rpm / min to 20000rpm / min.

[0039] In some embodiments, the shear rate during mixing is 5500 rpm / min to 6500 rpm / min, more preferably 5900 rpm / min to 6100 rpm / min.

[0040] In some embodiments, the shear rate during the homogenization process is 10500 rpm / min to 15500 rpm / min, and more preferably 10900 rpm / min to 11100 rpm / min.

[0041] In some embodiments, the homogenization time is 2 min to 4 min, more preferably 2.5 min to 3.5 min.

[0042] In some of the embodiments, the preparation method of the deamidated pea protein solution is as follows: dissolve the pea protein in a phosphate buffer solution with a pH of 6.8 to 7.2, stir at room temperature for 1.5 to 2.5 hours, adjust the pH to 6.8 to 7.2; then stir and preheat in a water bath at 40°C to 50°C, add glutaminase to react, and then heat to inactivate the enzyme to obtain the solution.

[0043] In some embodiments, the active concentration of the glutaminase is 0.010U / mg protein to 0.020U / mg protein, preferably 0.012U / mg protein to 0.018U / mg protein, more preferably 0.015U / mg protein to 0.017U / mg protein, and most preferably 0.016U / mg protein.

[0044] In some embodiments, the reaction temperature is 40°C to 50°C, preferably 44°C to 46°C.

[0045] In some embodiments, the reaction time is 60 min to 70 min, preferably 65 min to 67 min.

[0046] In other embodiments of the present invention, the application of the above-mentioned high internal phase emulsion in 3D food printing is disclosed.

[0047] In other embodiments of the present invention, a method for 3D food printing is disclosed, comprising the following steps: using the above-mentioned high internal phase emulsion as edible ink to print a food structure. The high internal phase emulsion is loaded into an extrusion 3D printer, and a computer-controlled nozzle is used for printing to print a food structure with high precision, self-supporting ability and ideal texture, meeting the modern food industry's demand for high-performance emulsion stability.

[0048] The present invention is described in detail below with reference to the accompanying drawings and specific embodiments.

[0049] Example 1 Preparation of a high internal phase emulsion stabilized by deamidated pea protein

[0050] This example prepares a high internal phase emulsion (HIPE) with a deamidated pea protein (DPPI) concentration of 1.5 wt% and an oil phase fraction of 75%. The method comprises the following steps:

[0051] 1. Preparation of pea protein (NPPI)

[0052] The pea powder was mixed with deionized water at a mass ratio of 1:10, and the pH of the solution was adjusted to 8.0 with 6 mol / L NaOH, and magnetic stirring was performed at room temperature for 2 hours to fully dissolve it. Centrifugation (8000g, 30min), the supernatant was collected, the pH was adjusted to 4.5 with 6 mol / L HCl, the precipitate was collected after centrifugation (5000g, 20min), and it was washed twice with deionized water. The precipitate was collected and added to deionized water, and the solution was adjusted to 7.0 with 6 mol / L NaOH, stirred to fully redissolve the protein, and the supernatant was collected after centrifugation again (5000g, 20min), and freeze-dried and stored for later use.

[0053] 2. Preparation of deamidated pea protein (DPPI) solution

[0054] Weigh 10 grams of pea protein obtained in step 1 and dissolve it in 95 mL of phosphate buffer solution (10 mmol / L, pH 7.0), stir at room temperature for 2 hours, and adjust the pH to 7.0. Then place it in a magnetic stirring water bath at 45 ° C and stir and preheat for 2 minutes, then add 5 ml of glutaminase (32U / mL) to reach a final enzyme activity concentration of 0.016U / mg protein. React for 66 minutes under the action of the enzyme, then heat the mixture to 80 ° C and keep it in a shaking water bath for 20 minutes to inactivate the enzyme to obtain a deamidated pea protein (DPPI) solution.

[0055] 3. Preparation of high internal phase emulsion (HIPE)

[0056] The deamidated modified pea protein (DPPI) solution obtained in step 2 was diluted to a protein concentration of 6 wt% with 10 mmol / L PBS buffer (pH 7.0). The protein solution was gradually mixed with corn oil at a volume ratio of 1:3 at 6000 rpm using a high-speed digital homogenizer (such as IKA's T-25 Ultra-Turrax). After the oil phase was added, homogenization was performed at 11000 rpm for 3 minutes to form a high internal phase emulsion (HIPE) with a protein concentration of 1.5 wt% and an oil phase volume fraction of 75%.

[0057] Example 2 Preparation of a high internal phase emulsion stabilized by deamidated pea protein

[0058] In this example, a high internal phase emulsion (HIPE) with a deamidated pea protein (DPPI) concentration of 2.0 wt% and an oil phase fraction of 75% was prepared. Except for diluting the protein to a concentration of 8% in step 3, the other steps were the same as in Example 1.

[0059] Example 3 Preparation of a high internal phase emulsion stabilized by deamidated pea protein

[0060] In this example, a high internal phase emulsion (HIPE) with a deamidated pea protein (DPPI) concentration of 2.5 wt % and an oil phase fraction of 75% was prepared. Except for diluting the protein to a concentration of 10% in step 3, the other steps were the same as in Example 1.

[0061] Comparative Example 1

[0062] In this comparative example, a high internal phase emulsion (HIPE) with a deamidated pea protein (DPPI) concentration of 0.1 wt% and an oil phase fraction of 75% was prepared. Except for diluting the protein to a concentration of 0.4% in step 3, the other steps were the same as those in Example 1.

[0063] Comparative Example 2

[0064] In this comparative example, a high internal phase emulsion (HIPE) with a deamidated pea protein (DPPI) concentration of 0.25 wt % and an oil phase fraction of 75% was prepared. Except for diluting the protein to a concentration of 1% in step 3, the other steps were the same as those in Example 1.

[0065] Comparative Example 3

[0066] In this comparative example, a high internal phase emulsion (HIPE) with a deamidated pea protein (DPPI) concentration of 0.5 wt % and an oil phase fraction of 75% was prepared. Except for diluting the protein to a concentration of 2% in step 3, the other steps were the same as those in Example 1.

[0067] Comparative Example 4

[0068] In this comparative example, a high internal phase emulsion (HIPE) with a deamidated pea protein (DPPI) concentration of 1.0 wt% and an oil phase fraction of 75% was prepared. Except for diluting the protein to a concentration of 4% in step 3, the other steps were the same as those in Example 1.

[0069] Comparative Example 5

[0070] In this comparative example, a high internal phase emulsion stabilized by pea protein (NPPI) was prepared. Compared with Example 1, the preparation method did not include step 2, and the protein used in step 3 was pea protein, thereby preparing a high internal phase emulsion with a protein concentration of 1.5wt% and an oil phase fraction of 75%.

[0071] Comparative Example 6

[0072] In this comparative example, a high internal phase emulsion stabilized by pea protein (NPPI) was prepared. Compared with Example 2, the preparation method did not include step 2, and the protein used in step 3 was pea protein, thereby preparing a high internal phase emulsion with a protein concentration of 2.0 wt% and an oil phase fraction of 75%.

[0073] Comparative Example 7

[0074] In this comparative example, a high internal phase emulsion stabilized by pea protein (NPPI) was prepared. Compared with Example 3, the preparation method did not include step 2. Meanwhile, the protein used in step 3 was pea protein, and a high internal phase emulsion with a protein concentration of 2.5 wt % and an oil phase fraction of 75% was prepared.

[0075] Test Example 1: Observation of the appearance of high internal phase emulsion and characterization of water loss rate

[0076] The high internal phase emulsions prepared in Examples 1 to 3 and Comparative Examples 1 to 4 were observed for appearance and characterized for water loss rate. The results were as follows: Figure 1 and Figure 2 shown.

[0077] from Figure 1 It can be seen that when the concentration of deamidated modified pea protein (DPPI) is 0.1wt%, HIPE cannot be formed, but when the concentration of DPPI is 0.25wt% to 2.5wt%, HIPE can be formed.

[0078] From the appearance after centrifugation ( Figure 2 A) and water loss rate results ( Figure 2 It can be seen from B) that when the DPPI concentration is 0.25wt% to 1.0wt%, the water holding capacity of the formed HIPE is poor, while when the DPPI concentration is 1.5wt% to 2.5wt%, the water holding capacity of the formed HIPE is good, the water loss rate is less than 1%, and the stability is good. Test Example 2 Particle Size and Rheological Properties Characterization of High Internal Phase Emulsion

[0079] The high internal phase emulsions prepared in Examples 1 to 3 and Comparative Examples 5 to 7 were characterized by the following properties:

[0080] 1. Particle size measurement: Use Mastersizer 3000 to measure the size and distribution of emulsion oil droplets. The results are as follows: Figure 3 shown.

[0081] from Figure 3 It can be seen that with the increase of protein concentration, the oil droplet size of the high internal phase emulsion (HIPE) stabilized by pea protein (NPPI) and deamidated pea protein (DPPI) both showed a decreasing trend. At the same protein concentration, the oil droplet size of the high internal phase emulsion (HIPE) stabilized by deamidated pea protein (DPPI) was significantly smaller than that of the high internal phase emulsion (HIPE) stabilized by pea protein (NPPI). This result shows that compared with pea protein (NPPI), deamidated pea protein (DPPI) has higher interfacial activity, can more effectively reduce the oil-water interfacial tension, promote more uniform oil droplet formation, and reduce the aggregation and merging of oil droplets.

[0082] 2. Rheological properties test: Use a rheometer to evaluate the shear viscosity and storage modulus of the emulsion.

[0083] Shear viscosity results are as follows Figure 4 As shown, from Figure 4 It can be seen that all high internal phase emulsions HIPEs exhibit typical shear thinning behavior, and the viscosity of HIPEs increases significantly with the increase of protein concentration. At the same protein concentration, the viscosity of HIPEs stabilized by DPPI is higher than that of HIPEs stabilized by NPPI. This result shows that DPPI can form a more solid and dense protein network, enhance the rheological properties of the emulsion, and have higher self-supporting properties.

[0084] also, Figure 5 It is shown that the storage modulus of DPPI-stabilized HIPEs is significantly higher than the loss modulus, and its storage modulus is significantly higher than that of NPPI-stabilized HIPEs, reflecting its stronger elastic behavior and higher gel strength, which can further support its superior performance in 3D printing.

[0085] Test Example 3 Stability Test of High Internal Phase Emulsion

[0086] In this test example, the stability of HIPEs under different treatment conditions was tested by observing the microstructural changes of HIPEs under an optical microscope, measuring the oil droplet size and viscosity changes of HIPEs, and measuring the content of oxidation products (to evaluate the oxidation stability of the emulsion).

[0087] 1. Ion concentration treatment

[0088] Different concentrations of Na were added to the protein solution (step 3 of Example 1 and Comparative Example 5). + (0~1200mmol / L) and Ca 2+ (0-25 mmol / L) ions were added to evaluate their effects on the stability of HIPEs (subsequent operations were the same as in Example 1).

[0089] 2. pH adjustment

[0090] The protein solution (step 3 of Example 1 and Comparative Example 5) was adjusted at different pH values ​​(3, 5, 7, 9) to observe its stability and oil droplet distribution (subsequent operations were the same as in Example 1).

[0091] 3. Heat treatment

[0092] HIPEs (Examples 1 to 3 and Comparative Examples 5 to 7) were heated at 90°C and 120°C for 20 minutes, respectively, and the aggregation of oil droplets and changes in emulsion stability were observed.

[0093] 4. Oxidation condition treatment

[0094] The HIPEs (Examples 1 to 3 and Comparative Examples 5 to 7) were stored at 50° C. for 21 days, and the contents of primary and secondary oxidation products were measured regularly to evaluate their antioxidant stability.

[0095] The results show that DPPI-stabilized HIPEs exhibit significantly better stability than NPPI-stabilized HIPEs under different environmental conditions. + In the range of ion concentration (0-1200mmol / L), the oil droplet size of DPPI-stabilized HIPEs changed little, indicating that it has a high ability to resist ion interference, while NPPI-stabilized HIPEs changed little in the presence of high Na + The oil droplet size increases significantly at the concentration, and the emulsion stability decreases ( Figure 6 A in the Ca 2+ DPPI-stabilized HIPEs remained stable at all concentrations, and the oil droplet size decreased only at high Ca 2+ The concentration of Ca2+ increased slightly (20-25 mmol / L), while NPPI stabilized HIPEs at 10 mmol / L Ca2+. 2+ At concentrations above 1000 ℃, the oil droplets aggregate to form large-size oil droplets, and the emulsion stability decreases significantly ( Figure 6 In addition, at different pH values ​​(3, 5, 7, 9), DPPI-stabilized HIPEs maintained high stability, with moderate changes in oil droplet size and no protein aggregation, while NPPI-stabilized HIPEs showed severe protein aggregation at pH 5, resulting in a significant increase in oil droplet size and decreased emulsion stability ( Figure 6C in the figure). Under heat treatment conditions, DPPI-stabilized HIPEs maintained good oil droplet microstructure and emulsion stability at both 90°C and 120°C, with only slight deformation at low concentrations, while NPPI-stabilized HIPEs had severe oil droplet structure deformation, protein aggregation, and significantly decreased emulsion stability at high temperatures ( Figure 7 ). Therefore, DPPI can effectively maintain the stability of HIPEs under a variety of harsh environmental conditions, reflecting its superiority as a high-performance emulsifier and further proving its wide application potential and advantages in 3D food printing and other food formulations.

[0096] Oxidative stability results such as Figure 8 As shown in the results, after HIPEs were stored at 50°C for 21 days, the primary and secondary oxidation products of DPPI-stabilized HIPEs at a concentration of 2.5% were 33.34±0.79mmol / kg oil and 60.19±6.05μmol / kg oil, respectively, which were significantly lower than 54.95±1.08mmol / kg oil and 104.69±0.66μmol / kg oil of NPPI-stabilized HIPEs. The results showed that DPPI-stabilized HIPEs had stronger antioxidant capacity, mainly because its compact interfacial protein layer effectively blocked the penetration of oxidants, while the higher viscosity slowed down the diffusion rate of oxidants.

[0097] Test Example 4 Application of HIPE in 3D printing

[0098] The HIPEs prepared in Examples 1 to 3 and Comparative Examples 5 to 7 were used as edible inks and loaded into the syringe of an extrusion 3D printer, and printed after removing bubbles. The printed models included tower and cylinder shapes, and the shape retention, texture quality, and texture of the printed structures were evaluated.

[0099] The results are as follows Fig. 9 and Fig.10 shown.

[0100] NPPI-stabilized HIPEs exhibited poor printing performance under all conditions. For example, at pH 7, the 1.5% NPPI tower still collapsed immediately, and only HIPEs with a 2.5% NPPI concentration were able to maintain structural integrity, but the self-supporting ability was still poor, with a slight tilt. In contrast, DPPI-stabilized HIPEs exhibited superior printing performance, with a clear and layered printed tower structure, good self-supporting ability, and achieved higher resolution and better surface quality. It is worth noting that the printing accuracy of the HIPE formed at a DPPI concentration of 2.5wt% deteriorated slightly, and burrs appeared on the surface of the printed tower, which may be due to the high viscosity, resulting in unstable air pressure during extrusion printing and burrs.

[0101] In addition, the texture results showed that the DPPI-stabilized 3D printed HIPEs had higher hardness and adhesion, indicating better stability, which was mainly attributed to the formation of a stronger protein network by DPPI, which enhanced the mechanical strength and structural integrity.

[0102] Therefore, DPPI-stabilized HIPEs significantly improve the printing performance and textural properties, and are suitable for high-performance 3D food printing applications.

[0103] The technical features of the above-described embodiments may be arbitrarily combined. To make the description concise, not all possible combinations of the technical features in the above-described embodiments are described. However, as long as there is no contradiction in the combination of these technical features, they should be considered to be within the scope of this specification.

[0104] The above-mentioned embodiments only express several implementation methods of the present invention, and the descriptions thereof are relatively specific and detailed, but they cannot be understood as limiting the scope of the invention patent. It should be pointed out that, for ordinary technicians in this field, several variations and improvements can be made without departing from the concept of the present invention, and these all belong to the protection scope of the present invention. Therefore, the protection scope of the patent of the present invention shall be subject to the attached claims.

Claims

1. Application of deamidated pea protein in the preparation of high internal phase emulsion.

2. The use according to claim 1, characterized in that: The deamidated modified pea protein is prepared by adding glutaminase to a pea protein solution to carry out a deamidation reaction.

3. The use according to claim 2, characterized in that: The concentration of the pea protein solution is 6wt% to 10wt%; and / or, the activity concentration of the glutaminase is 0.010U / mg protein to 0.020U / mg protein, preferably 0.012U / mg protein to 0.018U / mg protein, more preferably 0.015U / mg protein to 0.017U / mg protein, and most preferably 0.016U / mg protein; and / or, the reaction temperature of the deamidation reaction is 40°C to 50°C, preferably 44°C to 46°C; And / or, the reaction time of the deamidation reaction is 60 min to 70 min, preferably 65 min to 67 min.

4. A high internal phase emulsion, characterized in that: The high internal phase emulsion is obtained by homogenizing a mixed solution of a deamidated pea protein solution and vegetable oil; the concentration of the deamidated pea protein in the high internal phase emulsion is 0.25wt% to 2.5wt%.

5. The high internal phase emulsion according to claim 4, characterized in that The concentration of the deamidated modified pea protein in the high internal phase emulsion is 1.0 wt% to 2.5 wt%, preferably 1.5 wt% to 2.5 wt%, and more preferably 1.9 wt% to 2.1 wt%; And / or, the volume percentage of vegetable oil in the mixed liquid is 65% to 80%, preferably 70% to 77.5%, more preferably 74% to 76%; And / or, the vegetable oil is sunflower seed oil, soybean oil, corn oil, rice bran oil, linseed oil, camellia oil, peanut oil, and / or perilla oil.

6. A method for preparing the high internal phase emulsion according to claim 4 or 5, characterized in that: The method comprises the following steps: mixing a deamidated modified pea protein solution with vegetable oil at a shear rate of 2000 rpm / min to 9000 rpm / min, and then homogenizing the mixed solution at a shear rate of 10000 rpm / min to 20000 rpm / min.

7. The method for preparing a high internal phase emulsion according to claim 6, characterized in that: The shear rate during the mixing is 5500 rpm / min to 6500 rpm / min, more preferably 5900 rpm / min to 6100 rpm / min; And / or, the shear rate during the homogenization process is 10500 rpm / min to 11500 rpm / min, more preferably 10900 rpm / min to 11100 rpm / min; And / or, the homogenization time is 2 min to 4 min, more preferably 2.5 min to 3.5 min.

8. The method for preparing a high internal phase emulsion according to claim 6, characterized in that: The preparation method of the deamidated pea protein solution is as follows: dissolving the pea protein in a phosphate buffer solution with a pH of 6.8 to 7.2, stirring at room temperature for 1.5 to 2.5 hours, adjusting the pH to 6.8 to 7.2; then stirring and preheating in a water bath at 40° C. to 50° C., adding glutaminase to react, and then heating to inactivate the enzyme to obtain the deamidated pea protein solution; and / or, the activity concentration of the glutaminase is 0.010U / mg protein to 0.020U / mg protein, preferably 0.012U / mg protein to 0.018U / mg protein, more preferably 0.015U / mg protein to 0.017U / mg protein, and most preferably 0.016U / mg protein; And / or, the concentration of the pea protein in the phosphate buffer solution is 6wt% to 10wt%; And / or, the reaction temperature is 40°C to 50°C, preferably 44°C to 46°C; And / or, the reaction time is 60 min to 70 min, preferably 65 min to 67 min.

9. Use of the high internal phase emulsion according to claim 4 or 5 in 3D food printing.

10. A method for 3D food printing, characterized in that: The method comprises the following steps: using the high internal phase emulsion described in claim 4 or 5 as edible ink to print food structures.

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