GROUND MEAT ANALOGUE PRODUCT

Abstract

The present invention relates in general to meat analogue products suitable for the vegan consumer. In particular, it relates to a ground meat analogue product and method of making thereof.

Claims

1. A method of making a ground meat analogue product, said method comprising a. Preparing a plant protein extrudate by wet extrusion; b. Preparing a 10 to 20% (w/w) plant protein dispersion; c. Preparing a fat mimetic by emulsifying a protein dispersion and a lipid phase; d. Comminution of the plant protein extrudate; e. Comminution of the fat mimetic; and f.

2. A method according to claim 1, wherein the plant protein extrudate has a water content of not less than 45% (w/w).

3. A method according to claim 1, wherein the plant protein dispersion is prepared by a. Preparing a mix of protein isolate in water; b. heating until gel formation; and c. cooling.

4. A method according to claim 3, wherein 14-16 wt % soy protein isolate is mixed with water.

5. A method according to claim 3, wherein salt is added to the mix at a final concentration of 0.2-0.4M.

6. A method according to claim 1, wherein the fat mimetic is prepared by emulsifying a mixture of about 30% (w/w) of a protein dispersion, and about 70% (w/w) of a lipid phase.

7. A method according to claim 6, wherein about 0.2-0.6M sodium chloride is added.

8. A method according to claim 7, wherein about 0.4M sodium chloride is added.

9. A method according to claim 7, wherein the protein is prepared using a soy, potato, pea, pumpkin, wheat or canola protein isolate.

10. A method according to claim 6, wherein the protein dispersion comprises 10 to 16 wt % soy protein isolate.

11. A ground meat analogue product comprising: a. Plant protein extrudate; b. 10-20% (w/w) plant protein dispersion; and c. Fat mimetic comprising a protein dispersion emulsified in an lipid phase.

12. The ground meat analogue product according to claim 11, wherein the plant protein extrudate is a textured fibrous plant protein extrudate.

13. The ground meat analogue product according to claim 11, wherein the fat mimetic comprises about 30% (w/w) of a protein isolate dispersion comprising a protein isolate and about 70% (w/w) of a lipid phase.

14. The ground meat analogue product according to claim 11, wherein the protein isolate dispersion comprises 10 to 16 wt % soy protein isolate.

15. (canceled)

Description

Example 6

[0161] Development of a Plant-Based Binder (Protein Dispersion)

[0162] For the development of vegan burger patties, the fat mimetics and protein extrudates need to adhere to each other. This internal cohesion was to be achieved by means of a plant-based binder. The binder was to have mostly viscous properties prior to heating so as to allow patties to be formed, but should transition to a gel upon heating to cause the burger patty to become solid. By mixing a suitable binder with the other two components (extrudates and fat particles), a deformable mass was to be created. A highly concentrated SPI dispersion was used since that was also used in the manufacture of the fat system, and thus represented already present compounds. FIG. 2 shows the impact of different heating times on the gel strength of gelled SPI dispersion containing varying concentrations of SPI. The strength was again measured with a material property measurement device, i.e. an Instron, Model 3365. Data shown represents the mean value of ten measurements and the respective standard deviation.

[0163] SPI dispersions containing 10% and 12% SPI showed little change in gel strength as a function of heating times indicating that very weak gels were formed or no gelation occurred. The gel strength stayed constantly around 0.1 N for 10% SPI and 0.5 N for 12% SPI. For protein dispersions containing 14% SPI the gel strength increased from 1.5 N when not heated to 2.7 N when heated for 45 min. The 16% SPI dispersion had an initial gel strength of around 3 N that increased to a little over 6 N, when the dispersion was heated for 45 min. As such and not surprisingly, higher SPI concentrations cause gels to assume higher strengths after sufficient heating times. It should be noted that samples containing 14% and 16% exhibited already gel like properties without any heating, whereas 10% and 12% SPI had more liquid-like properties.

[0164] Without wishing to be bound by theory, higher gel strengths with increasing heating times may have been caused by a higher degree of unfolding since proteins had more time to undergo conformational changes. When SPI is heated, the globular proteins denature and start to unfold. Unfolded proteins have mostly hydrophobic groups exposed on the surface, whereas hydrophobic patches are buried inside the globular protein structure. An unfolding thus enables hydrophobic areas on different proteins to interact with each other leading to network formation and therefore to gelation of the dispersions. At higher protein concentrations, the proteins bind more water and are more densely packed, so that interactions between molecules is favored. Therefore, the gel strength is strongly dependent on the protein concentration. For SPI concentrations of 10% and 12%, even long heating times did not cause formation of a strong gel. In those samples the number of protein-protein interactions was simply too low to cause a strong gel formation that entraps solvent. Therefore, no form stable gel was formed.

[0165] It was concluded from this that these SPI concentrations are insufficient for the use as a binder in vegan burger patties, since a formation of a gel network that is able to keep the comminuted ingredients together is required for the application. In contrast, the gel strength increased with increasing heating times for protein dispersions with 14% and 16% SPI. Due to higher gel strengths of the samples with 14% and 16% SPI those two samples and additionally protein dispersion containing 18% and 20% SPI were used to further investigate the impact of NaCl addition on the gel strength of the protein dispersions. For that purpose, 0.2, 0.3 and 0.4 M of NaCl were added to the protein dispersion before heating. The results of the gel strengths measured with the Instron at 75% deformation are shown in FIG. 3.

[0166] FIG. 3 shows a slight increase for the gel strength of the SPI dispersion containing 14% SPI. The gel strength increased from 2.82±0.25 N to 3.56±0.17 N when 0.2 M NaCl were added. At higher NaCl concentrations the increase in gel strength was less distinct. The maximum force at 0.3 and 0.4 M NaCl was 3.45±0.48 N and 3.74±0.12 N, respectively. SPI concentrations of 16% caused higher gel strengths at the same NaCl concentrations compared to 14%. It can be seen that without NaCl the gel strength was already twice as high as for the 14% system with a maximum gel strength of 6.13±0.35 N. This gel strength was further increased to 6.95±0.45 N upon addition of 0.2 M NaCl. A slight decline was noticed at 0.3 M where the maximum gel strength was lowered to <6 N. For 0.4 M NaCl the gel strength seemed to be very similar to the gel strength of samples containing 0.2 M NaCl. The protein dispersions containing 18% SPI had a gel strength of 12.41±0.96 N for the dispersions without NaCl and 11.5±1.14 N, 10.52±0.63 N, 11.12±0.63 N for the samples with 0.2 M, 0.3 M and 0.4 M NaCl, respectively. This constitutes a slight decrease in gel strength after NaCl was added. For the gel strength of the protein dispersion with 20% SPI, the strength increased from 16.13±2.27 N (0 M NaCl) to 20.14±2.04 N (0.4 M NaCl). This increase in gel strength with increasing NaCl concentration can be explained by the fact that at higher NaCl concentrations the electrostatic repulsion between the proteins is screened which facilitates intermolecular network formation. Higher numbers of intermolecular interactions due to hydrophobic or electrostatic interactions may increase gel strength.

[0167] The results showed that protein dispersions with 10% and 12% SPI, respectively, formed only weak gels when heated at 85° C. In contrast, the gel strength increased with increasing heating time for protein dispersions with 14% and 16% SPI. 18% and 20% SPI dispersion show gel behavior before heating is applied. To investigate the influence of the binder on the overall textural properties of the burger patties two SPI concentrations were further investigated. According to the presented results 12% SPI was chosen as a weaker binder, since the formed gels were weak, even after long heating times and 20% SPI which represents a strong gel.

[0168] Rheological measurements were conducted with a SPI concentration (12% SPI) that showed no strong gels when analyzed on gel strength and a concentration that showed high gel strengths (20% SPI) to further characterize them.

[0169] 20% SPI dispersion show similar courses for heated (D) and unheated (C) dispersions. Independent of the frequency the storage modulus is always higher than the loss modulus. The ratio between the storage and loss modulus is increasing from approx. 4 for the unheated to >6 for the heated dispersions. Therefore, it is concluded, that those protein gels do only show solid gel behavior. In contrast to that, the 12% SPI gels show a transition from more elastic to more viscous fluid properties at high frequencies indicating weaker intermolecular interactions. Therefore, the inner molecular order is affected at high speed deformation. This concludes higher gel strength for 20% SPI gels compared to 12% SPI gels.

[0170] The impact of large deformation treatments on SPI gels is performed by means of a shear rate ramp varying from 0.01-100 1/s for the unheated SPI dispersions. The shear stress at higher protein concentrations (20%) exceeded the shear stress of 12% SPI. Both curves showed strong increases in shear stress at shear rates between 0.01 1/s and 0.03 1/s. This is due to the fact, that especially at low shear rates, the resolution of the measurement device reaches its limits and other slipping and friction effects have big impacts on the measurement signal. For the samples with 12% SPI the shear stress is increasing linear above shear rates >0.3 1/s. This indicates a behavior comparable to a Newtonian fluid. The protein dispersion containing 20% SPI start with shear stresses of 190 Pas and shows a plateau from 0.03 1/s to 0.1 1/s. At higher shear rates the shear stress increases to a maximum at 10 1/s. Above this shear rate the shear stress is decreasing again due to the destruction of the gel.

Example 7

[0171] Development of Vegan Burger Patties

[0172] Extrudates produced with the 13 mm hole plate were used for further studies. Trials of the production of patties using respective extrudate showed a very homogenous mass. The burger mass showed a very uniform composition. Neither fat, nor extrudate pieces appear to be visible. Therefore, it is more comparable to an emulsified sausage type of product.

[0173] Compression experiments of patties produced manually and by use of the kitchenAid were performed. The maximum force for the manually mixed burger patties equals 525.87±45.24 N and 553.52±38.33 N for the patties produced with the kitchenAid. The fracture forces are also very similar with a value of 30.15±5.14 N for the manually produced and 26.73±4.45 N for the kitchenAid mixed patties. In both types of burger patties the components are distributed homogenously, so that both measurements reach the same values. Therefore, it can be assumed that the mixing by hand and with the kitchenAid are comparable to each other and for simplification, only the kitchenAid was used for further production of patties.

[0174] To improve the textural properties of the patties different binders were used. Besides the already presented SPI dispersions, gluten powder and gluten-SPI mixtures were tested. Moreover, unwanted hardening of cooked patties that originated from extrudates exhibiting a glass transition upon cooling had been observed. Thus, a broth was prepared containing 18 g/L vegetable stock powder in water and the extrudate were cooked for 10 or 15 min, and after that comminuted in a bowl chopper for 1.15 min. The comminuted extrudate pieces were then covered in gluten powder or in a gluten and SPI powder mixture before mixing. To some of the sample additional water was added to allow soaking of the proteins. The burgers were analyzed optically and haptically.

[0175] After frying, the burger patties produced with gluten powder had an appealing appearance and exhibited adhesion. The patties produced with extrudate that was covered in gluten and SPI powder showed great strength before and after frying. The strength was higher compared to other burger patties produced with SPI dispersions alone. No protein aggregates were observed within this mixture. To increase the swelling of the proteins and therefore improve the interactions some additional water (5%) was added to the recipe for the patties.

Example 8

[0176] Influence of Binder Strength and Concentration on Texture of Patties

[0177] Different textural measurements were performed with the patties, a non-destructive measurement (20% deformation) with and without a relaxation period was conducted. Deformation of 60% was applied for the destructive measurement.

[0178] The universal texture analyzer was used to perform a 20% deformation of the burger patties and different textural properties were investigated. The amount of binder of those burgers was varied between 10% and 40% to investigate the impact of this component on the properties.

[0179] For the same binder concentration, the patties containing 20% SPI generally exhibited higher gel strength than burger patties containing 12% SPI in the binder. Hence, the maximum force of burger patties containing 20% SPI started with a strength of 25.13±10.71 N for 10% binder in the burger mass, which was more than halved to a maximum force of 12.63±1.99 N for 40% binder in the burger mass. Burger masses containing 12% SPI had a maximum strength of 21.94±2.10 N at 10% binder concentration which was tremendously decreased to 4.06±2.34 N at 40% binder concentration. The difference in strength increased at higher binder concentrations, as for those samples the impact of the binder on the textural properties got higher due to the higher amount of binder in the recipe. As the 20% SPI gels were higher in gel strength than the 12% SPI gels.

[0180] The burger patties containing 20% SPI showed different breaking behavior for the two binder concentrations. For 20% SPI in binder the samples containing 10% binder showed break points indicated by the black arrows. This break points indicated the breaking of the structure and yielding of the burger patty. At higher binder concentrations, the strength of the overall patty got stronger influenced by the binder properties. The break point is reached after longer time and therefore stronger compression. Patties containing 12% SPI on the other hand showed the break point at lower strength and the break was less distinct compared to the samples containing 20% SPI in binder. At high binder concentrations (40%) the break point was almost not detectable anymore. This is caused by the big impact of the binder on the texture of the patty. The patty was smearing apart rather than breaking. The patties produced with 20% SPI in binder led to stronger interaction within the patty causing break behavior of the patty. At lower SPI concentrations this interactions were lowered and the patties were very soft. Their behavior under compression can by explained as flowing apart instead of breakage of the inner structure.

[0181] All burger patties showed decreasing values for rising binder concentrations in the burger mass. At 10% binder the maximum force was nearly the same for both SPI concentrations (166.14±73.92 N and 170.99±6.89 N). Above these concentrations the difference between the binders grew. An exception was observed at 25% binder, where the maximum strength of 20% SPI patties was lower compared to the ones produced with 12% SPI. For all the other samples the patties produced with 20% SPI showed higher maximum strengths compared to the ones produced with 12% SPI. Higher strength for the gels produced with 20% SPI are caused by the denser gel network enabled due to higher concentration of proteins within the binder. Because of that, more intermolecular interactions could contribute to the strength of the binder and also to the overall strength of the patty.