Multi-enzyme compound noodle stretching agent and application thereof

Abstract

The invention discloses a multi-enzyme compound noodle stretching agent and application thereof, and belongs to the technical field of food additives. The multi-enzyme compound noodle stretching agent is prepared from the following components in parts by mass: 1 to 10 parts of papain, 1 to 10 parts of trypsin, 1 to 10 parts of glucose oxidase, 1 to 10 parts of lipase and 10 to 30 parts of tea polyphenol. Through the synergistic effect of multienzyme compounding and tea polyphenol, the dough structure and the noodle processing performance are improved, the protein depolymerization and crosslinking degree and the protein oxidation degree of the dough can be regulated and controlled at the same time, the dough strength and ductility are considered, the cooking loss is reduced, meanwhile, the green and natural characteristics are kept, no chemical modifier is added, and the production cost is reduced. And the limitation of the existing single enzyme or chemical modifier is overcome, so that the method has a relatively good application prospect in the technical field of food additives.

Description

Technical Field

[0001] This invention belongs to the field of food additive technology, specifically relating to a multi-enzyme compound ramen agent and its application. Background Technology

[0002] Current dough improvement technologies primarily rely on single-enzyme preparations or chemical modifiers (such as sodium metabisulfite and alkali) to regulate dough structure, thereby improving dough extensibility and elasticity. However, these technologies still have certain limitations in practical applications. Single-enzyme preparations typically target only a specific type of protein or local structure in the dough, resulting in a relatively singular regulatory dimension. This makes it difficult to simultaneously address both the strength and extensibility of the gluten network within the same system, limiting the overall improvement in noodle quality. Furthermore, due to the narrow applicability of single regulatory mechanisms, it is difficult to achieve synergistic and stable regulation of dough structure under different flour raw materials and processing conditions. While chemical modifiers can improve dough extensibility by disrupting disulfide bonds in gluten proteins or adjusting the system's pH, this type of regulation lacks selectivity, easily leading to excessive softening of the dough structure or increased cooking losses. Moreover, some chemical additives pose potential health risks, which is inconsistent with the development direction of natural and green foods. The reason for this is that the dough protein system has a complex structure, primarily composed of glutenin and prolamins participating in gluten network construction, with different protein components playing different roles in network formation and stability. Single enzyme preparations or chemical modification methods are insufficient to achieve synergistic regulation of multiple structural units, making it difficult to consistently obtain noodle products with both good elasticity and extensibility while ensuring processing stability. Summary of the Invention

[0003] This invention provides a multi-enzyme compound ramen agent, which is composed of the following components in parts by mass: 1-10 parts papain, 1-10 parts trypsin, 1-10 parts glucose oxidase, 1-10 parts lipase, and 10-30 parts tea polyphenols.

[0004] In one specific embodiment, the multi-enzyme compound ramen agent is composed of the following components in parts by weight: 3 parts papain, 3 parts trypsin, 2 parts glucose oxidase, 2.5 parts lipase, and 15 parts tea polyphenols.

[0005] This invention provides the application of the above-mentioned multi-enzyme compound ramen agent in improving the performance of ramen; the ramen performance includes extensibility, cooking characteristics, texture and rheological properties.

[0006] This invention provides a high-performance ramen noodle, which is prepared by the following method: Dissolve salt and multi-enzyme compound ramen agent in water, then add it to flour in three parts. Add 75% first and stir the flour into a uniform dough flake state. Add 20% second and continue kneading until the dough flakes gradually gather and form a uniform dough flake state without obvious dry powder. Add 5% third and knead the dough flakes into a smooth dough. Let it rest at 25~30 ℃ for 30~40 minutes. After kneading, stretching, dividing into dough portions, and stretching, high-performance ramen is obtained.

[0007] In the above-mentioned method for preparing high-performance ramen, the raw materials are selected from the following parts by weight: 100-300 parts flour, 4-6 parts salt, and 0.1-2 parts multi-enzyme compound ramen agent; the amount of water should be appropriate for kneading the dough.

[0008] The beneficial effects of this invention are as follows: This invention improves dough structure and noodle processing performance through the synergistic effect of multi-enzyme complex and tea polyphenols. It can simultaneously regulate the depolymerization and cross-linking of dough proteins, lipid distribution, and antioxidant protection, achieving a balance between dough strength and extensibility, reducing cooking losses, and maintaining green and natural characteristics. It does not require the addition of chemical modifiers such as sodium metabisulfite, overcoming the limitations of existing single enzymes or chemical modifiers, and thus has good application prospects in the field of food additive technology. Attached Figure Description

[0009] Figure 1 This is a picture of the actual ramen.

[0010] Figure 2 The rheological storage modulus diagrams for each group of dough are shown.

[0011] Figure 3 The rheological loss modulus diagrams for each group of dough are shown.

[0012] Figure 4 The diagram shows the rheological loss coefficients of each group of dough.

[0013] Figure 5 This is a SEM image of the papain proteome in ramen.

[0014] Figure 6 This is a SEM image of the trypsinome ramen.

[0015] Figure 7 This is a SEM image of the papain + trypsin group of ramen noodles.

[0016] Figure 8 SEM image of dough containing GOX, lipase, and EGCG.

[0017] Figure 9 This is a SEM image of the compound ramen.

[0018] Figure 10 This is a SEM image of the Penghui group ramen.

[0019] Figure 11 This is a SEM image of the blank control group dough. Detailed Implementation

[0020] In this invention, papain is used for protein depolymerization, improving gluten extensibility, and non-specifically cleaving the main chain at random and multi-site sites; trypsin can synergistically depolymerize proteins, mainly cleaving side chains, and improving dough flexibility; glucose oxidase (GOX) promotes disulfide bond formation through oxidation, enhances gluten network strength, strengthens the gluten network, compensates for the gluten strength loss caused by protease and alkali reduction, and improves hardness, elasticity, and cooking resistance after cooking; lipase can improve the lipid distribution in dough, improve dough lubricity and extensibility uniformity; tea polyphenols (EGCG) stabilize the gluten structure and provide antioxidant protection by forming non-covalent complexes with proteins.

[0021] Papain (100,000 U / g), trypsin (200,000 U / g), glucose oxidase (2,700 U / g), and lipase (2,600 U / g) were all purchased from Sunson Enzyme Co., Ltd., and tea polyphenols (98%) were purchased from Xi'an Mixianer Biotechnology Co., Ltd.

[0022] Other materials used in this invention, unless otherwise stated, are commercially available. Other terms used in this invention, unless otherwise specified, generally have the meanings commonly understood by those skilled in the art. The invention is further described in detail below with reference to specific embodiments and data. The following embodiments are merely illustrative and not intended to limit the scope of the invention in any way.

[0023] Example 1 Prepare the ramen noodles as follows: 1. Ramen recipe 250 g flour, 5 g salt, noodle seasoning; Ramen seasonings are categorized as follows: (1) Papain 0.06 g; (2) Trypsin 0.06 g; (3) Papain 0.03 g + Trypsin 0.03 g; (4) Glucose oxidase (GOX) 0.02 g + Lipase 0.025 g + Tea polyphenol (EGCG) 0.15 g; (5) Papain 0.03 g + Trypsin 0.03 g + Glucose oxidase (GOX) 0.02 g + Lipase 0.025 g + Tea polyphenol (EGCG) 0.15 g; (6) Peng ash (alkaline traditional Peng ash) 1.5 g; (7) Blank control.

[0024] 2. Ramen processing Dissolve salt and noodle seasoning in water (pH 7.0), then add it to the flour in three batches. First, add 75% and stir the flour into a uniform dough (with some dry powder remaining). Second, add 20% and continue kneading until the dough gradually gathers together, forming a dough with a uniform surface and no obvious dry powder. Third, add 5% and knead the dough into a smooth dough. Let it rest at 30℃ for 40 minutes. After kneading, rolling, dividing into portions, and stretching (the production method is the same as for regular handmade noodles), handmade noodles are obtained.

[0025] The ramen prepared according to the recipe in group (5) above is shown in the following picture. Figure 1 As shown.

[0026] I. Ramen / Dough Performance Test 1. Extensibility The hand-kneaded dough was subjected to a tensile test using a Brabender stretch meter according to standard procedure ICC114 / 1. 150 g of dough was kneaded into a standard cylindrical shape on the forming unit. The shaped dough was then proofed in a 30°C proofing room for 40 minutes, and its tensile properties were then tested.

[0027] The test results are shown in Table 1: Table 1. Dough Extensibility As shown in Table 1: Group (7) dough (blank control) had the lowest extensibility and the highest tensile resistance. Gluten protein maintains intact disulfide bonds and non-covalent interactions, with a dense and continuous network, but its plasticity is limited; its processing and quality are characterized by strong tensile strength and good boiling resistance, but insufficient stretchability, which is not conducive to multiple stretching of noodles, and is a typical state of wheat dough that is "strong but not soft".

[0028] In the first group of dough (papain), the papain has a broad-spectrum cleavage effect, breaking down high molecular weight gluten and "softening" the gluten skeleton, but it has not yet completely depolymerized. This makes the dough much easier to stretch, but reduces its tensile strength. The final result is that the noodles are soft and easy to stretch, but have reduced chewiness and increased cooking losses.

[0029] The dough in group (2) (trypsin) showed that, compared to papain, trypsin had a more specific cleavage site (Lys / Arg) and a less severe network disruption. This resulted in limited improvement in dough extensibility, with resistance remaining at a moderate level. It was more "glutenous" than papain, but slightly less elastic.

[0030] The dough in group (3) (papain + trypsin) had the highest extensibility and the lowest stretching resistance. This group exhibited a broad-spectrum + specific cutting synergy, with significant depolymerization of the polymer gluten and severe weakening of the network continuity; thus, the dough was very easy to stretch, but had almost no "skeleton support", and was very easy to break and become mushy. This was an extreme state of "maximum stretchability, but poor overall quality".

[0031] Group (4) dough (GOX + lipase + EGCG) belongs to a structure-enhancing system. GOX promotes protein-protein oxidative cross-linking (-SS-), EGCG promotes polyphenol-protein covalent / non-covalent cross-linking, and lipase improves the lipoprotein interface and enhances network density. The gluten network is tighter and more elastic, but the high degree of cross-linking of the gluten protein network limits the dough's extensibility and deformation to some extent, thus limiting its processing performance improvement.

[0032] The dough in group (5) (compound) showed significantly higher extensibility than the blank control and the GOX+lipase+EGCG group, and significantly lower resistance than the pure enzymatic hydrolysis system. This allows the dough to be "stretchable without breaking easily," which is an ideal structural window for functional ramen additives. From a structural perspective, protease can provide dough with elasticity, while GOX + EGCG can limit excessive degradation and rebuild the network.

[0033] The dough in group (6) (Peng Hui) has similar extensibility to the compound group, but the mechanism is different. The alkalinity causes the protein to swell and the conformation to relax. It is not a real network enhancement, but a "chemical stretching", which poses a quality risk: the shear resistance and cooking resistance are unstable, the cooking loss and soup turbidity are high. It is a characteristic of traditional alkaline noodles that are "easy to stretch but not resistant to cooking". In addition, as a chemical alkaline modifier, Peng Hui is prone to producing an irritating odor during the processing, which is not conducive to the stable control of product quality.

[0034] 2. Cooking characteristics Place 25 noodles in 450 mL of boiling distilled water for the optimal cooking time (2 minutes, measured using two transparent plastic plates), then rinse with distilled water for 1 minute, and finally blot the surface moisture with filter paper. The water absorption rate is calculated as follows: ; In the formula, m1 and m2 represent the weight of the noodles before and after steaming or cooking, respectively.

[0035] The broth from the steamed noodles was collected and cooled to room temperature. The cooking loss was expressed as absorbance measured by UV-Vis spectrophotometry at 675 nm.

[0036] The breakage rate during stretching is counted during the stretching process.

[0037] The test results are shown in Table 2: Table 2 Results of noodle cooking characteristics As shown in Table 2: Regarding the water absorption rate of noodles: Alkali (54.4%) had the highest absorption rate, a typical example of alkaline fortification that promotes gluten expansion and hydration, significantly increasing water absorption. Papain (45.1%) was similar to that of papain + trypsin (45.6%), indicating that the synergistic effect of enzymes in the compound did not significantly disrupt the water-absorbing structure. Trypsin (43.3%) was slightly lower; its strong protease activity damaged the gluten backbone, leading to a decrease in water absorption. The multi-enzyme compound had the lowest absorption rate (41.8%), indicating that the dense cross-linked network restricted water entry, resulting in a lower water absorption rate.

[0038] Regarding cooking loss (absorbance): trypsin showed the highest absorbance (0.285), consistent with its strong ability to disrupt gluten structure, leading to greater protein and starch dissolution. Papain (0.265) and the multi-enzyme combination (0.263) showed similar absorbance, indicating that the combined effect of partial enzymatic hydrolysis and cross-linking controlled dissolution. Potash showed the lowest absorbance (0.253). Despite its high water absorption, its network expands and is not easily broken, resulting in lower cooking loss, possibly due to the alkaline environment enhancing protein binding. The combination of papain and trypsin (0.275) reflects moderate dissolution resulting from synergistic enzymatic hydrolysis.

[0039] Regarding the breakage rate during stretching: Papain had the lowest breakage rate (0.5%), indicating good gluten network toughness and an extremely low breakage rate, making it suitable for ramen production. The multi-enzyme combination (1.4%) and the papain + trypsin combination (2.3%) also showed low breakage rates, indicating that enzyme activity enhanced flexibility and reduced breakage, making them suitable for ramen production. The single-enzyme group (papain 4.2%, trypsin 5.4%) had a higher breakage rate, especially trypsin, which may have caused brittleness due to uneven network disruption.

[0040] Furthermore, when using the GOX+lipase+EGCG combination system, the dough structure is too dense or the processing adaptability is insufficient, making it impossible to prepare ramen. Therefore, it is difficult to complete the steaming and cooking characteristic test, which further illustrates that a single cross-linking enhancement system is not conducive to actual ramen processing operations in the absence of appropriate structural regulation.

[0041] In summary, papain and trypsin, when used alone, significantly damage the gluten structure, resulting in substantial changes in water absorption and breakage rate. Enzyme combinations can, to some extent, balance the gluten structure, maintain a good water absorption rate, reduce breakage rate, and limit cooking losses. The cross-linking effect of multiple enzymes + EGCG enhances the density of the gluten network; although water absorption decreases, the breakage rate is minimized, which is beneficial for noodle processing.

[0042] 3. Texture To evaluate the impact of different ramen additives on the quality of ramen, textural properties of ramen samples prepared using different additive systems were tested, and parameters such as hardness, viscosity, elasticity, and chewiness were measured.

[0043] Twenty-five fresh noodles were placed in 450 mL of boiling distilled water for the optimal cooking time (2 min), and then rinsed with distilled water for 1 min. To prevent moisture evaporation, the noodles were covered with plastic wrap after absorbing excess water with filter paper. Total texture (TPA) parameters were measured using a P / 36R probe at a speed of 0.8 mm / s, with a compression ratio of 75% and an interval of 2 s.

[0044] The test results are shown in Table 3: Table 3. Texture analysis results of noodles As shown in Table 3, different additive systems have a significant impact on the structure and eating quality of ramen.

[0045] When papain was used as a ramen agent, the hardness of the ramen was 4235, the elasticity was 0.82, and the chewiness was 2257.26. The overall structural support and chewiness were low, indicating that the gluten network structure was easily weakened under the action of papain alone, making it difficult to obtain the ideal chewy texture of ramen.

[0046] When trypsin was used as a ramen agent, the hardness of the ramen increased to 4614 and the chewiness increased to 2510.02, but the elasticity decreased to 0.80. This indicates that trypsin alone has a certain effect on improving the quality of ramen, but it is still insufficient in terms of elasticity and structural coordination.

[0047] When papain and trypsin are used in combination, the hardness of the ramen noodles is further reduced to 3846, and the chewiness is reduced to 1961.46. This indicates that the combination of two enzymes, in the absence of other regulatory means, is prone to excessive hydrolysis of the gluten structure, which reduces the support and chewiness of the ramen noodles.

[0048] When using the compound enzyme ramen agent described in this invention, the resulting ramen has a hardness of 5014, an elasticity of 0.85, and a chewiness of 3196.43, exhibiting good coordination among various textural indicators. Specifically, the hardness is maintained within a suitable range, ensuring the structural stability of the ramen; the significantly improved elasticity gives the ramen good resilience; and the markedly enhanced chewiness indicates that the ramen has a good chewy texture and lasting flavor during consumption.

[0049] When traditional ash is used as a ramen agent, the hardness of the ramen is 5116, the chewiness is 2864.96, but the elasticity is only 0.80. This indicates that ash mainly improves the texture of ramen by increasing hardness, but it is not as good as the compound enzyme ramen agent of this invention in terms of elasticity and overall coordination.

[0050] Furthermore, when using the GOX+lipase+EGCG combination system, the dough structure is too dense or the processing adaptability is insufficient, making it impossible to prepare ramen. Therefore, it is difficult to complete the standard texture test, which further illustrates that a single cross-linking enhancement system is not conducive to actual ramen processing operations in the absence of appropriate structural regulation.

[0051] In summary, the compound enzyme ramen agent of this invention can significantly improve elasticity and chewiness while ensuring the structural stability of ramen, making the overall textural properties of ramen superior to those of single enzyme systems and traditional ash-addition methods, demonstrating significant technical effects.

[0052] 4. Rheological properties The viscoelasticity of the dough samples was determined using a rheometer. Each group of samples was allowed to stand at 25°C for 20 min. Then, a suitable amount of dough was placed on the rheometer stage, and a PP50 probe was used for measurement. The gap between the probe and the stage was 1 mm, and the temperature of the circular stage was 25°C. After loading the samples, excess material was gently scraped off from the edges, and a layer of liquid paraffin was applied to prevent moisture loss. The samples were allowed to relax for 5 min before testing. A frequency scanning mode was selected, with a frequency range of 0.1–100 Hz and a constant strain amplitude of 0.5%. Parameters such as storage modulus (G'), loss modulus (G''), and tanδ (G'' / G') were recorded.

[0053] Test results are as follows Figure 2 , Figure 3 and Figure 4 As shown: With the blank control group as the baseline, the dough system mainly relies on the disulfide bonds, hydrogen bonds and hydrophobic interactions formed by the gluten proteins themselves to construct a continuous three-dimensional network structure, which is characterized by weak gel features dominated by elasticity (G′>G″, tan δ<1).

[0054] Different enzyme preparations and their compounding methods significantly alter the rheological properties and structural stability of dough by regulating the degradation and recombination behavior of gluten proteins.

[0055] Single protease treatments all weakened the gluten network to varying degrees. Papain, as a non-specific protease, extensively hydrolyzed the glutenin and wheat glutenin backbones, causing high molecular weight polymers to break down into shorter polypeptide segments. This resulted in a significant decrease in G′ and G″ and an increase in tan δ, indicating that the dough network structure tended to be looser and its elastic contribution was weakened. In contrast, trypsin, due to its site specificity, only hydrolyzed some accessible peptide bond regions, resulting in a relatively limited degree of damage to the overall gluten network. Its rheological parameter changes were smaller than those of the papain group, indicating that it improved the molecular chain slippage ability to a certain extent while still preserving some network structure.

[0056] When papain and trypsin are used in combination, the G′ and G″ of the dough system decrease significantly, while tan δ increases markedly, exhibiting a stronger viscosity-dominant characteristic. This indicates a synergistic degradation effect between the two proteases, leading to deep depolymerization of gluten proteins, severe weakening or even local destruction of the continuous network structure, causing the system to gradually shift towards fluidization, which is detrimental to the requirements of structural stability and elasticity maintenance during the ramen processing.

[0057] In contrast, the combination of GOX, lipase, and EGCG significantly improved the elastic properties of dough, as evidenced by a significant increase in G′ and a decrease in tan δ. GOX enhances the covalent bonds between gluten proteins by promoting the formation of disulfide bonds or disulfide crosslinks, while EGCG further strengthens the non-covalently crosslinked network through hydrogen bonds and hydrophobic interactions. Lipase indirectly affects the viscoelastic behavior of dough by regulating lipid states and interfacial lubrication properties. In this system, the gluten network not only has a more stable structure but also maintains a strong energy storage capacity under high-frequency conditions, exhibiting significant anti-relaxation characteristics.

[0058] Building upon this foundation, the compound formulation achieves a dynamic balance between moderate proteolysis and cross-linking enhancement, effectively reshaping the gluten network structure. Limited proteolysis helps alleviate an overly dense network structure, improving dough extensibility; while the cross-linking induced by GOX and EGCG inhibits excessive depolymerization, maintaining network continuity and stability. Although proteolysis may reduce some thiol sites that can participate in cross-linking, and EGCG has a certain inhibitory effect on proteolysis activity, the synergistic regulation of multiple effects achieves a more reasonable balance between elasticity and viscosity. The combined characteristics of the changes in G′, G″, and tan δ demonstrate that the compounding strategy can ensure structural stability while imparting good processing adaptability to the dough, thereby achieving optimal overall quality of the ramen dough.

[0059] 5. Scanning electron microscope Figures 5-11 Scanning electron microscope (SEM) images of each ramen sample are shown.

[0060] Papainome: The ramen noodles exhibited a distinctly loose and fragmented gluten network structure. The continuity of the gluten skeleton was reduced, with numerous pores and broken areas appearing in the protein network, some even showing a dotted or fragmented structure. The exposure of starch granules increased, with clear granule boundaries and a significantly weakened encapsulation effect. This microstructure is highly consistent with its macroscopic textural characteristics, which showed a significant decrease in hardness and chewiness and an increase in elasticity, indicating that protein hydrolysis weakened the network's supporting capacity.

[0061] Trypsinome: The gluten network of the ramen noodles still maintains some continuity, but is more porous than the control group. SEM reveals gluten protein fibrillation and a directional arrangement of the gluten protein network, with a more regular but increased number of pores. Starch granules are partially embedded, but the interfacial bonding is weakened. This microstructure corresponds to its macroscopic performance of decreased hardness while maintaining a certain structural strength.

[0062] Papain + trypsin group: The ramen exhibits the loosest and most damaged microstructure. The gluten network is clearly fragmented, the continuous skeleton is difficult to identify, and the pores are large and irregularly distributed. A large number of starch granules are exposed, with localized accumulation or detachment, indicating a severe weakening of the gluten-starch complex structure. This structural characteristic closely matches its lowest hardness, lowest chewiness, and highest extensibility, suggesting a high risk of substance loss during cooking.

[0063] The GOX+lipase+EGCG combination was unsuitable for ramen preparation; therefore, the SEM image shows dough with this combination added. This image reveals a dense and uniform gluten network structure. The protein network walls are thick and tightly connected, with small and evenly distributed pores. Starch granules are highly embedded, with blurred outlines. The non-covalent interaction between EGCG and protein, along with GOX-induced oxidative cross-linking, enhances network stability. Simultaneously, lipase promotes the formation of starch-lipid complexes, further filling the network pores. This dense structure is perfectly consistent with its highest hardness, chewiness, and high elasticity, typical microscopic characteristics of high-quality ramen.

[0064] Compound Group: The compound system samples exhibit a relatively dense yet flexible gluten network. Compared to the pure GOX system, its network is slightly looser with slightly larger pores, but overall continuity is good. Slight network breaks or voids can be observed in local areas, but the overall gluten-starch composite structure remains relatively stable. This "strength-flexibility balance" microstructure well explains its moderate hardness, high elasticity, and good overall eating quality. The microstructure of the compound system samples is intermediate between that of the protease and GOX systems. SEM reveals a relatively continuous but not extremely dense gluten network with a relatively uniform pore structure. The starch granules are well embedded, but their outlines are still discernible. This structure exhibits a "flexibility-strength balance," consistent with its high elasticity, moderate hardness, and good chewiness.

[0065] The "Peng Hui" group: In SEM images, ramen noodles exhibit a contracted, dense, but uneven gluten structure. Under alkaline conditions, the gluten protein molecular chains rearrange, with localized areas displaying a lamellar or oriented structure. This network structure is often accompanied by uneven pore size distribution, local collapses, or cracks, indicating that while its structure is dense, it lacks flexibility.

[0066] Blank control group: Since this group lacked ramen-making agents and could not produce ramen, SEM images of its dough were taken. The SEM images showed that this group's dough exhibited a relatively continuous but not dense gluten network structure. Gluten proteins formed a basically continuous three-dimensional framework, with most starch granules partially embedded in the protein network. However, some starch granules still showed clear boundaries and were exposed on the network surface. The overall pore distribution was uneven, with some large pores, indicating that the gluten network structure had limited stability.

[0067] The above description is merely a preferred embodiment of the present invention and is not intended to limit the invention in any other way. Any person skilled in the art may make changes or modifications to the above-disclosed technical content to create equivalent embodiments. However, any simple modifications, equivalent changes, and modifications made to the above embodiments based on the technical essence of the present invention without departing from the scope of the present invention shall still fall within the protection scope of the present invention.

Claims

1. A multi-enzyme complexed ramen agent, characterized by, The papain 1-10 parts, the trypsin 1-10 parts, the glucose oxidase 1-10 parts, the lipase 1-10 parts, and the tea polyphenol 10-30 parts by mass parts.

2. The multi-enzyme complexed noodle agent according to claim 1, characterized by, The multi-enzyme compound la mian agent is composed of the following components by mass parts: papain 3 parts, trypsin 3 parts, glucose oxidase 2 parts, lipase 2.5 parts, and tea polyphenol 15 parts.

3. The use of the multi-enzyme compound la mian agent of claim 1 or 2 in improving the performance of la mian.

4. Use according to claim 3, characterized in that, The performance of la mian includes ductility, cooking characteristics, texture, and rheological properties.

5. A high performance ramen characterized by, The la mian is prepared by the following method: The salt and the multi-enzyme compound la mian agent are dissolved in water, and then added to the flour in three times; the first time is 75%, and the flour is stirred into a uniform dough state; the second time is 20%, and the dough is continuously kneaded, so that the dough gradually aggregates to form a dough state with a uniform surface and no obvious dry powder; The third time is 5%, and the dough is kneaded into a smooth dough; the dough is rested at a temperature of 25-30 ℃ for 30-40 min; after kneading, rolling, dividing, and stretching, high-performance la mian is prepared.

6. The high performance pulled noodle according to claim 5, wherein, Each raw material is selected from the following mass parts: flour 100-300 parts, salt 4-6 parts, and multi-enzyme compound la mian agent 0.1-2 parts.

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