JPS587261B2 - Greta - Google Patents

Description

DETAILED DESCRIPTION OF THE INVENTION The present invention relates to a method for producing a fibrous high-protein food, and more particularly to a method for producing a fibrous high-protein food that has excellent heat softening resistance and elasticity.

In recent years, research on artificial fibrous proteins such as so-called artificial meat has progressed, and some attempts have been made to put them into practical use.

The present inventors also previously treated non-fibrous protein with a proteolytic enzyme under certain conditions, stretched it and modified it into fibrous protein, and produced a fibrous protein food with a meat-like texture. (Japanese Patent Publication No. 46-29870).

In this method, non-fibrous proteins such as casein are converted into Cal.
The fibrous composition obtained by this method is made by forming micelles with l-, etc., gelling it by treating it with a proteolytic enzyme, stretching this gel to form an oriented fibrillar composition, and fixing it with acid. Because the material has poor heat resistance, there is a risk that it will soften and lose its fibrous form when heated during cooking.

It has been found that such softening due to heat can be prevented by using acetic anhydride for its fixation (see Japanese Patent, supra).

However, this acetic anhydride has safety problems as a food additive, and has a strong pungent odor, which causes problems in handling and product purification, so it cannot be used in practice.

Under these circumstances, the present inventors have devised a method for producing an excellent fibrous high-protein food that has excellent anti-thermal softening properties and does not cause heat softening even when mixed with other fish and livestock meats. As a result of repeated research to find out, we found that a fixed bath with two phosphoric acid groups in one molecule
By using an aqueous solution containing at least one kind of condensation or esterification compound of phosphoric acid or a mixed aqueous solution containing at least one kind of the above-mentioned phosphoric acid compound and sulfuric acid, it is possible to obtain better heat softening properties than the above method. We have invented a method for producing extremely superior fibrous proteins.

These phosphoric acid compounds are widely present in natural foods and are also widely used as additives.They have the advantage of being almost tasteless and odorless, and are easy to handle during manufacturing operations. It is excellent in all aspects, including the fact that even if some amount remains in the product, there is no need to purify and remove it.

In order to further improve this method, the present inventors added an emulsifier to the fixed bath and investigated its effect.The results showed that this effect was unexpectedly large, improving the anti-thermal softening property and widening the optimum pH range. , the time required for fixation is shortened and operability is greatly improved, and the flexibility of the gel is increased, its stretchability is improved, and the elasticity of the resulting fibrous protein is increased, resulting in recovery properties and improved texture. It turned out that an excellent product could be obtained.

For example, a 20% casein solution (% indicates weight %).

The same applies hereinafter) is added to an aqueous solution of calcium chloride, which is then treated with protease, and the resulting gel is spread to form an oriented fibrillar composition, which then contains a fixed solution of a phosphoric acid compound alone, a phosphoric acid compound, and an emulsifier. When treated with a fixed solution and examined for its anti-thermal softening properties, the results shown in Table 1 below were obtained.

In addition, the heat softening resistance in the table shows the treated fibrous material at 20°C at 80°C.
The results are shown when heated for minutes, +++: No change in fibrous properties, ++: Most of the fibers remain, +: Some fibrous remains, ±: Almost no fibrous materials, 1: No fibrous materials at all. , (hereinafter used in the same way).

As is clear from Table 1, when a phosphoric acid compound such as phytic acid or sodium hexametaphosphate is used in combination with an emulsifier such as lecithin, the anti-heat softening property is improved, and the anti-heat softening property is particularly high when using a phosphoric acid compound such as sodium hexametaphosphate alone. The improvement effect is large in areas with high content.

Next, in order to investigate the effect of adding an emulsifier on the optimum pH, we used phytic acid as a phosphoric acid compound, lecithin and recommended sugar fatty acid ester as emulsifiers, and adjusted the pH with hydrochloric acid and caustic soda. The anti-thermal softening properties were examined by treating with a fixative solution.

The results are shown in Table 2. As shown in Table 2, the lower limit of pH at which anti-thermal softening properties are imparted by adding an emulsifier is 0.
It drops from 5 to 0, the range widens from 0 to 5, and then 8.
The pH range that provides the best anti-heat softening properties with no change in fiber properties even when heated at 0°C for 20 minutes has a lower limit of 1.5 to 1.0 and an upper limit of 2.5 to 3.0. rise, 1
．． It becomes wider from 5-2.5 to 1.0-3.0.

Since the optimum pH range is widened in this way, pH control becomes easier, which is an extremely significant operational advantage.

Next, Table 3 shows some of the results of investigating the effects of the addition of an emulsifier on the fixing time, flexibility of the gel, and elasticity of the resulting fibrous protein.

In addition, the elasticity in the table was qualitatively examined by chewing the obtained fibrous protein. +++: Extremely high resilience (
Gastrointestinal wall membrane-like shape of livestock), ++: High resilience (mollusk flesh-like shape), +: High resilience (livestock muscle-like shape), ±: Poor resilience (chicken sashimi, fish flesh-like shape) means.

As shown in Table 3, as the amount of emulsifier added increases, the fixation time is shortened, and when 10% lecithin is added, the fixation time is 1/10 of that without addition of lecithin, and the same or better anti-heat softening properties can be obtained. It will be done.

In this way, the addition of an emulsifier greatly shortens the fixing time and greatly improves operability.

Furthermore, as shown in the table, it was found that the flexibility of the gel increased as the amount of emulsifier added increased, and the stretchability became very good, making the fiberizing operation easier.

As shown in the table, the elasticity of the obtained fibrous protein increased as the amount of emulsifier added increased, and it was revealed that an extremely excellent chewy texture could be obtained.

The mechanism by which the addition of an emulsifier produces these extremely effective effects is not clear, but one reason is that the addition of an emulsifier greatly accelerates the penetration of the fixative into the interior of fibrous proteins. considered to be a thing.

Examples of emulsifiers that exhibit the above effects include lecithin, recommended sugar fatty acid esters (monostearin, monopalmitin, monoolein, distearin, dipalmitin esters), mono- and diglycerides of fatty acids such as stearic acid, oleic acid, and palmitic acid; and fatty acid esters of polyhydric alcohols such as sorbitan monostearate, and these are usually added to the fixed bath in an amount of 0.1 to 10%, preferably 02 to 2.0%.

In addition to being added to the fixation bath, the emulsifier can also be added before the fixation treatment, ie, when preparing the protein solution, or during the micelle formation step, to achieve the above effects.

Phosphoric acid compounds used in the fixing bath include phosphoric acid condensates having two or more phosphoric acid groups such as sodium pyrophosphate, sodium tripolyphosphate, sodium hexametaphosphate, and sodium ultraphosphate, glyceric acid diphosphate, and fructose. Examples include esterified compounds having two or more phosphoric acid groups in one molecule, such as diphosphoric acid ester, succinic acid, and phosphorylated starch.

These compounds are used in 0.1-30% aqueous solutions.

The fixation time can be shortened by increasing the concentration, and the fixation time can be adjusted depending on the concentration.

Particularly desirable are sodium hegysametaphosphate, sodium ultraphosphate, phytic acid, etc., each having six or more phosphate groups in one molecule.

Furthermore, when these compounds are used in combination with sulfuric acid or a sulfate such as sodium sulfate or magnesium sulfate, they are even more effective in terms of anti-thermal softening properties.

The raw milk protein used in the method of the present invention is usually used as a solution dissolved in an aqueous solution of an alkali metal salt such as sodium hydroxide or potassium carbonate, an alkaline phosphate such as sodium phosphate, or ammonia. The pH value is preferably 6 to 9 and the concentration is preferably about 5 to 30%.

This milk protein may be used in the form of a mixture with other non-fibrous animal and vegetable proteins such as soybean protein and gluten.

Examples of multivalent metal ions used for micellization of milk proteins include calcium ions (Ca-H-) and magnesium ions (Mg''), and specific examples include calcium chloride, calcium bromide, calcium nitrate, Water-soluble calcium salts such as calcium acetate, water-soluble magnesium salts such as magnesium chloride, magnesium bromide, magnesium nitrate, and magnesium sulfate are used.

A method of destroying the formed micelles and forming a gel is to add a proteolytic enzyme such as bacterial protease, fungal protease, trypsin, chymotopsin, papain, etc. at room temperature or under heating (usually 40 to 60°C).
A method of treatment with a reducing agent is preferable, but instead of this enzyme treatment, a method of treatment with a reducing agent may also be adopted.

As a method using a reducing agent, a reducing agent such as a sulfite such as sodium bisulfite, β-mercaptoethanol, sodium monothiocunate, or sodium borohydride is added to an alkaline solution of the protein, usually as a 1 to 10% aqueous solution. , at room temperature or under heating (usually 40-60℃)
It is gelled by stirring.

The obtained gel is subjected to stress such as stretching according to a conventional method to form an oriented fibrillar composition.

As for the method of applying these stresses, common methods such as stretching between mechanical stress rollers, roller rolling, screw extrusion, stirring, and high-speed extrusion (jet injection, etc.) are used.

The fixing treatment is not only carried out after applying stress to the gel to orient it, but also by applying stress to the gel while orienting it. It is also possible to obtain excellent fibrous protein.

By further adding appropriate pigments, seasonings, flavors, etc. to the fibrous protein obtained by the method of the present invention, a fibrous high-protein food with excellent appearance, texture, and taste can be obtained.

Next, the method of the present invention will be explained in more detail with reference to Examples.

Example 1 100 g of casein and 10 g of soybean protein are added and dissolved in 500 ml of a 2.0% potassium carbonate aqueous solution at 50°C.

Add 33 ml of a 30% calcium chloride aqueous solution to this to form micelles.

When 200 mg of protease is added to the micelles, the micelles aggregate to form a gel.

This gel was spread, oriented and fibrillated, and divided into three equal parts: 1% phytic acid and 0% lecithin, 1% phytic acid and 0.5% lecithin, and 1% phytic acid and 1% lecithin. The protein was treated in three kinds of fixation baths containing 100% water, washed with water, and neutralized to obtain a fibrous protein with a water content of 75%.

There was no change in the fibrous properties of any of these even when heated at 80°C for 20 minutes, but in the gel spreading process during production, the higher the lecithin content, the better the flexibility and stretchability. and fiprillization was easy.

The elasticity of the obtained fibrous protein increases as the amount of lecithin increases; when the lecithin content is 0%, it looks like sashimi or fish meat and has poor restorability; when it is 0.5%, it looks like meat and has poor restorability; 1. 0
%, it was like mollusk flesh and had high resiliency.

The time required for fixation treatment was shortened as the lecithin increased, and was reduced to 5 minutes when lecithin was O%, 2 minutes when lecithin was 0.5%, and 1.
When it was 0%, it was 0.5 minutes.

Example 2 Add and dissolve 90 g of casein in 400 ml of 1.5% KOH solution, and prepare 30% calcium chloride aqueous solution 3 at 50°C.
0 ml is added to form micelles, and when 200 mg of grotease is added to the micelles, the micelles aggregate to form a gel.

This gel is spread, oriented and fibrillated, treated in a fixing solution containing 1% sodium hexametaphosphate and 0.5% saccharide monopalmitine ester, fixed, washed with water and neutralized to a moisture content of 70%. About 270g of fibrous protein was obtained.

After heating this fibrous protein at 80° C. for 20 minutes, there was no change in its fibrous properties, and its elasticity was similar to that of animal meat and had resilience.

Example 3 Add 100 g of casein to 400 ml of 50°C warm water, suspend it, and add 28% ammonia water6. Add Oml and dissolve.

Add calcium chloride aqueous solution (calcium chloride to 101
) to form micelles.

After micelle formation, 200 mg of protease is added to obtain a gel.

This gel is separated from the syneresis liquid, extruded through a slit under pressure, and further stretched three times between rollers to form an oriented fibril composition.

This was treated in a fixing bath containing 0.5% phytic acid and 0.5% lecithin, washed with water, and neutralized to obtain about 300 g of fibrous protein with a water content of 70%.

There was no change in the fibrous properties of this fibrous protein even after heating at 80° C. for 20 minutes, and its elasticity was similar to that of mollusc meat and had high resilience.

Example 4 100g of casein was added to 50°C warm water4. Suspend in O O ml and add 28% ammonia water 6 to this.

Add 0ml and dissolve.

Add 33 ml of 30% calcium chloride solution to this to form micelles.

After forming micelles, 200 mg of protease is added to aggregate the micelles to obtain a gel.

This is separated from the syneresis liquid, extruded through a slit, stretched twice between rollers, and then fixed while being stretched 1.5 times in an aqueous solution containing 0.5% phytic acid and 0.5% lecithin. The sparrows are then fixed in a fixation bath containing 1% phytic acid and 0.5% lecithin.

This is washed with water and neutralized to form a fibrous protein with a water content of 72%.
20g was obtained.

Even when this fibrous protein was heated at 80° C. for 20 minutes, there was no change in its fibrous properties, and its elasticity was similar to that of mollusc meat and had high resilience.

Claims (1)

[Claims] 1 A protease is added to milk protein or a mixture of it and other non-fibrous animal and vegetable proteins, or a micelle obtained by the action of multivalent metal ions to form a gel, and this gel is After applying stress to form an oriented fibrous composition, or while applying stress, at least one condensation or esterification compound of phosphoric acid having two or more phosphoric acid groups in one molecule and at least an emulsifier. A method for producing a fibrous high-protein food having excellent heat-resistant softening properties and elasticity, which comprises fixing the food at pH 5 to 5 with a mixed aqueous solution containing one of the above.