JP4898274B2 - Locust hydrolyzate, process for producing the same, and locust hydrolyzate compounding agent - Google Patents

Description

  The present invention relates to a technique for hydrolyzing locust (Huang Cong), and relates to a locust hydrolyzate mainly composed of a locust-specific peptide produced by hydrolysis, a method for producing the same, and a locust hydrolyzate compounding agent.

  Conventionally, as a technique for hydrolyzing proteins contained in animals and plants, for example, those described in Patent Documents 1 and 2 are known. Patent Document 1 describes a hydrolysis technique for obtaining a protein hydrolyzate from whey protein or the like, and Patent Document 2 describes a hydrolysis technique for obtaining a hydrolyzate from algae. .

Japanese Patent Publication No. 7-32718 JP 2005-263707 A

  However, there has not been a hydrolysis technique that uses locusts as its target for animals and plants to be hydrolyzed.

  Therefore, in view of the above problems, the present invention has a locust as a hydrolysis target, a locust hydrolyzate mainly composed of locust-specific peptides, a method for producing the same, and a locust hydrolyzate compounding agent. The issue is to provide

In order to solve the above-mentioned problem, the locust hydrolyzate according to the invention of claim 1 is produced by hydrolyzing locust powder by adding a compounding enzyme having a predetermined compounding weight ratio. The compounding enzyme is papain and , Neutral prodinase and polypeptidase, and the blending weight ratio is papain: neutral prodinase: polypeptidase = 5: 3: 2, and the hydrolysis has a hydrogen ion concentration index of 6.5. To 7.0, hydrolysis temperature 50 to 55 ° C., and hydrolysis time 3 to 4 hours . Here, locusts belong to the locust family locust family, and are, for example, Kobaneiago and Hananagainago.

The method for producing a locust hydrolyzate according to the invention of claim 2 comprises that locust powder contains papain, neutral prodinase and polypeptidase, and the blending weight ratio is papain: neutral prodinase: poly Adding peptidase = 5: 3: 2 mixed enzyme and hydrolyzing under conditions of hydrogen ion concentration index 6.5-7.0, hydrolysis temperature 50-55 ° C., hydrolysis time 3-4 hours It is characterized by.

The locust hydrolyzate compounding agent according to the invention of claim 3 is blended with the locust hydrolyzate of claim 1 and is configured to have a remarkable fatigue recovery action.

The locust hydrolyzate compounding agent according to the invention of claim 4 is obtained by blending the locust hydrolyzate of claim 1 , bee jar frozen dried powder, and royal jelly frozen dried powder in a predetermined blending weight ratio. Locust hydrolyzate compounding agent, wherein the blending weight ratio is as follows: locust hydrolyzate: bee jar freeze dried powder: royal jelly freeze dried powder = 3: 5: 2.

Locust hydrolyzate formulations according to the invention of claim 5, the dose was 0.4G～45g / person / day, and wherein the.

According to invention of Claims 1-2 , while improving the sexual function about the mouse | mouth which administered this locust hydrolyzate, it becomes possible to raise an anti-oxygen deficiency capability.

According to invention of Claims 3-5 , the remarkable fatigue recovery effect can be exhibited.

  Hereinafter, one embodiment of the locust hydrolyzate according to the present invention will be described. The locust hydrolyzate is mainly composed of a peptide produced by hydrolyzing a protein contained in locusts by the action of a compound enzyme. Hereinafter, the present locust hydrolyzate is referred to as locust peptide (Huang Cong Peptide) and is referred to as HCP.

  The average water content of the raw locusts used in the present invention is 100 g × 0.667 = 66.7 g. Moreover, the average dry weight of the raw locust is 100 g × (1−0.667) = 33.3 g. And the protein content in the dried locust powder is 70.0% when measured by the Kjeldahl method.

Moreover, the compounding enzyme used by this invention is mix-adjusted as follows.
First, 80,000 u / g of papain, 200,000 u / g of neutral prodinase, 200,000 u / g of basic prodinase, and 10,000 u / g of polypeptidase were prepared as the enzymes to be blended. All of these enzymes were provided by Guangxi South Ningfang and Expo Biotechnology Co., Ltd.
The blending ratio of the blended enzyme was papain: neutral prodinase: polypeptidase = 5: 3: 2. This blending ratio indicates the blending weight ratio.
In addition, for the activation of the compounded enzyme, 100 mg of the compounded enzyme prepared at the above compounding ratio was taken, 10 ml of 1% NaCl aqueous solution was added thereto, and the activation temperature of 37 ° C. was maintained and the temperature was kept at the activation time of 1 hour Was done.

  FIG. 1 shows an embodiment of the method for producing HCP according to the present invention, and is an explanatory diagram of the production process of HCP including a hydrolysis step for a locust powder using an experimental compound enzyme.

As shown in FIG. 1, HCP is manufactured by the following procedure.
(1) 4 g locust powder HC (substrate) is placed in a 150 ml beaker and kept warm at 40 ° C. for 1 hour (pretreatment step S1-1).
(2) After the incubation, 121 mg of the activated compounded enzyme described above is added to the beaker, and the temperature is raised to 50 ° C. At this time, the total volume of the suspension in the beaker is 150 ml, and the ratio of the compounded enzyme to the substrate in the suspension is 3%.
(3) The suspension was adjusted so that the hydrogen ion concentration index (hereinafter referred to as PH) = 7, and stirred for 4 hours while maintaining the hydrolysis temperature at 50 ° C., and the components such as proteins contained in HC Is hydrolyzed (hydrolysis step S1-2).
(4) After hydrolysis, the suspension is heated at 90 ° C. for 10 minutes to kill the compounded enzymes and the like.
(5) After heating, the suspension is centrifuged and the filtrate is recovered. Meanwhile, the residue is washed twice with 40 ml of hot water at 50 ° C. The previous filtrate is mixed with the two washings.
(6) The mixed solution composed of the cleaning solution and the filtrate is sterilized at 90 ° C. for 10 minutes, concentrated under reduced pressure by a rotary evaporation measure, and water is evaporated at a water bath temperature of 70 ° C. until drying (post-processing step S1-3).
(7) As a result, 1.68 g of light red-yellow HCP crystals are obtained. At this time, the yield of HCP is 1.68 g / (4 × 0.7 g) = 60%. Moreover, in this HCP, as a result of measuring content of a peptide by SDS-polyacrylamide gel electrophoresis, content is 72% and the relative molecular weight of the peptide is 2000-6000.

  FIG. 2 shows another embodiment of the method for producing HCP according to the present invention, and is an explanatory diagram of the production process of HCP including a hydrolysis step by a mass-production compound enzyme for locust powder.

As shown in FIG. 2, the HCP is manufactured by the following procedure.
(1) 43 kg locust powder (substrate) is put into a 1000 liter covered stainless steel can, 600 liters of water is added and stirred, and this suspension is kept warm at 40 ° C. for 1 hour (pretreatment step S2 -1).
(2) After keeping the temperature, 0.903 kg of the activated compounded enzyme described above is added to the stainless steel can, and the temperature is raised to 50 ° C. At this time, the suspension is supplemented with water, the total volume of the suspension is 980 liters, and the ratio of the compounded enzyme to the substrate in the suspension is 3%.
(3) The suspension is adjusted to PH = 7 and stirred for 4 hours while maintaining the hydrolysis temperature at 50 ° C. to hydrolyze components such as proteins contained in HC (hydrolysis step) S2-2).
(4) After hydrolysis, the suspension is heated at 90 ° C. for 10 minutes to kill the compounded enzymes and the like.
(5) After heating, the suspension is centrifuged and the filtrate is recovered. Meanwhile, the residue is washed twice with 400 liters of 50 ° C. water. The previous filtrate is mixed with the two washings.
(6) Sterilize the mixed solution composed of the washing solution and the filtrate at 90 ° C. for 10 minutes. At this time, the specific gravity of the mixed solution is 1.00 to 1.05. This mixed solution is dried using a centrifugal spray dryer having an inlet temperature of 140 ° C. and an outlet temperature of 70 ° C. (post-processing step S2-3).
(7) As a result, 15.12 kg of light brown and fluffy HCP solid is obtained. At this time, the yield of HCP is 15.12 / 30.1 = 50%. Here, “30.1” was derived from 70% (protein content) of 43 kg of locust powder. Moreover, in this HCP, as a result of measuring content of a peptide by SDS-polyacrylamide gel electrophoresis, content is 72% and the relative molecular weight of the peptide is 2000-6000. The water content is 3%. And the result of the bacterial test is negative.

Next, various active functions of the HCP compounding agent formed by blending HCP and a predetermined amount of HCP will be verified.
The first HCP compounding agent (hereinafter referred to as HCP1) is HCP420 mg (60%) to be 700 mg / tablet, Tohoku ginseng extract 210 mg (30%), and Western ginseng extract 70 mg (10%).
The second HCP compounding agent (hereinafter referred to as HCP2) is HCP420 mg (60%) so as to be 700 mg / tablet, and as a blend, Tohoku ginseng extract 175 mg (25%), Western ginseng extract 70 mg ( 10%), and 35 mg (5%) of white extract.
HCP is a pure locust peptide and contains 72% peptide.

Various active functions by HCP, HCP1, and HCP2 were verified by the following animal experiments (1) to (8).
First, as an experimental group, a control group in which nothing is administered, a positive control group (HC group) in which locust powder (a protein contained in a dried powdered locust, hereinafter, locust protein) is administered, and an HCP1 group in which HCP1 is administered. , HCP2 group to administer HCP2 and HCP group to administer HCP. Twelve mice are assigned for each group. Here, each mouse is selected from among 300 ICR mice, each having a male and female half body weight of 18 to 22 g and an average body weight of about 20 g.
The dose of each group is 870 mg / kg for locust protein or HCP, 1242.9 mg / kg for HC, and 17.4 mg / 0.3 ml / animal for HCP. The dose of each group corresponds to the following clinical recommended amount. It is (17.4 mg × 50) / (20 g × 50) × 55 Kg (male and female average body weight) / 1400 mg = 34 times. Therefore, the recommended clinical use amount is 700 mg / tablet × 2 tablets = 1400 mg.

First, in order to verify the effect of HCP1, HCP2, and HCP on physical fatigue of mice, the following experiments (1) to (6) were performed.
(1) Swimming experiment First, a swimming box having a water surface area of at least 30 cm and a predetermined depth on one side and a predetermined amount of hot water having a water temperature of 25 ± 1 ° C. is prepared. Thirty minutes after the final test article is administered to the mice, the mouse's hips are loaded with a weight of 5% of the body weight, and swimming is performed in this swimming box. The time from the start of swimming until the time when all of the head is underwater and cannot float on the surface of the water is recorded as the swimming time of the mouse.

(2) Stick climbing experiment An organic glass rod treated so that the mouse can climb a stick is placed in the vertical direction. Thirty minutes after the final test article is administered to the mouse, the mouse is placed on an organic glass rod so that the muscle of the mouse is in tension. Record the time the mouse falls from the organic glass rod due to muscle fatigue from the time the mouse is placed. The experiment ends when the mouse falls three times. The cumulative total of three times is taken as the mouse stick lift time.

(3) Blood Urea Nitrogen Measurement Experiment 30 minutes after the final test article was administered to a mouse, the mouse was allowed to swim for 90 minutes in the aforementioned swimming box with a water temperature of 25 ± 1 ° C. After resting for 60 minutes, blood is collected from the eyeball, serum is taken, and blood urea nitrogen is measured with a reagent kit.

(4) Liver glycogen measurement experiment 30 minutes after the final test article was administered to a mouse, the mouse was allowed to swim in a swimming box with a water temperature of 30 ± 1 ° C for 60 minutes. The mouse is killed and the liver is removed. Exactly 200 mg is taken, 4 ml of trichloroacetic acid (hereinafter referred to as TCA) is added, homogenized for 1 minute per tube, centrifuged at 3000 rpm for 15 minutes, and the supernatant is removed. Place in another test tube. Add 4 ml of TCA to the precipitate, homogenize for 1 minute and centrifuge for 15 minutes, take the supernatant and mix with the supernatant and homogenize well. Take 1 ml of supernatant and add 4 ml 95% alcohol per test tube and homogenize well until there is no interface between the two liquids. Place at room temperature until the next day, and after sufficient precipitation, centrifuge at 3000 r / min for 15 minutes. The supernatant is emptied, and the test tube is placed for 10 minutes. After shaking and dissolving with 1 ml distilled water, liver glycogen is measured.

(5) Measurement experiment of muscle glycogen 30 minutes after administration of the final test article to the mouse, the mouse is allowed to swim for 60 minutes in the aforementioned swimming box having a water temperature of 30 ± 1 ° C. The mouse is killed and the muscle is removed, washed with 0.9% NaCl solution, dried with filter paper, exactly 1 g muscle is taken into a 3 ml 30% KOH test tube and placed in boiling water for 20 minutes. Let it bathe. After taking out and cooling, transfer into a 50 ml constant volume bottle, wash the test tube several times with water, transfer all into the constant volume bottle, add water to the scale and homogenize. Place in boiling water, water bath for 10 minutes, remove and cool. Thereafter, the amount of light absorbed is measured at a wavelength of 620 nm using ultraviolet spectrophotometry, and the blank test tube is adjusted to the zero point.

From the experimental results (1) to (5) above, the effects of HCP, HCP1, and HCP2 on the swimming time, stick-up time, blood urea nitrogen, liver glycogen, and myocardial content of mice will be discussed.
As shown in Table 1, the reference experimental group should have a swimming time of 92% (p <0.01) for the HCP1 group and 72% (p <0.05) for the HCP1 group. Can do. Compared to the control group, the experimental group was 132% longer than the control group, 203% higher than the HCP1 bar lifting time (p <0.001), and 325% higher than the HCP2 bar lifting time (p <0.001). , HCP set stick up time can be increased by 291% (p <0.01). The experimental group can reduce the blood urea nitrogen content of the HCP group by 16% (p <0.01) and the HCP1 group by 13% (p <0.05) than the control group. The amount of hepatic glycogen eye bath in HCP2 group is equivalent to 2.4 times (p <0.01) that in the control group, and the amount of liver glycogen eye bath in HCP group is equivalent to 3.6 times (p <0.001) in the control group. To do.

(6) Measurement experiment of blood lactic acid 30 minutes after the final test sample was administered to the mouse, the weight of 4% body weight was placed on the buttocks of the mouse, and the aforementioned swimming box with a water temperature of 30 ± 1 ° C. Let swim for 10 minutes. Blood is taken from the mouse venous vein before swimming and every 0, 15, and 60 minutes after swimming, respectively. Add 0.48 ml of 1% NaF solution to a 5 ml centrifuge tube, accurately take 20 μl of blood with a micropipette, put it in the bottom of the test tube, wash the micropipette several times with the test tube supernatant, and add a protein precipitant. Homogenize by shaking, centrifuge at 3000 r / min for 10 minutes, remove supernatant and measure lactic acid in blood.

From the measurement result of (6) above, the effect of HCP, HCP1, and HCP2 on the blood lactic acid content in mice will be discussed.
As shown in Table 2, the HCP group at 0 minutes and 15 minutes after swimming can reduce the blood lactic acid content by 24% (p <0.01) and 24% (p <0.05), respectively, compared with the control group. . It can also be seen that it approaches the blood lactic acid content before swimming.

Next, in order to verify the effect of HCP, HCP1 and HCP2 on the mating of normal male mice, the following experiment (7) was performed.
(7) Experiment for verifying influence on mating Experimental animals are ICR mice, 48 males, 144 females, and an average body weight of about 30 g. As for the dose, physiological saline is administered to the control group, and HCP, HCP1 and HCP2 are all 17.4 mg / 0.3 ml / animal. The sex ratio is 3: 1.
The experimental results are shown in Tables 3 and 4.

Next, in order to verify the effect of HC, HCP1, HCP2, and HCP on the anti-oxygen deficiency of ICR mice, the following experiment (8) was performed.
(8) Experiment for verifying influence on deficiency of anti-oxygen The experimental animals are 60 groups of 85 days ICR mice belonging to the middle age, and 12 groups are divided into 5 groups. At this time, the weight of each half of the male and female is 28 to 32 g, and the average weight is about 30 g. The experimental condition is that the degree of vacuum in the bottle is 0.07 mPa. This value corresponds to a degree of vacuum corresponding to an altitude of 26300 m. This altitude corresponds to about three times the top height of Chomoramma.
The experimental results are shown in Table 5.

  As a conclusion of the experimental results, according to this experiment, HCP, HCP1, and HCP2 are significantly different from mouse swimming time, stick-up time, blood lactate, blood urea nitrogen, liver glycogen, and myoglycogen content. It was confirmed that there was an effect. This means that the sexual function of the mouse can be improved and the hypoxic capacity of the mouse is enhanced.

Next, various active functions of HCP and other HCP compounding agents obtained by blending a predetermined amount of HCP will be verified.
This HCP compounding agent (New Fufan Hang Polypeptide, hereinafter abbreviated as NFHP) is composed of HCP, bee jar frozen dried powder and royal jelly frozen dried powder, with a compounding weight ratio of 30% HCP and bee jar frozen. It is composed of 50% dry powder and 20% royal jelly freeze-dried powder.

  Each compounding material constituting the present NFHP is provided by Beijing Junyang Air Technology Co., Ltd. The recommended amount of human use of NFHP is 0.125 g / kg × 60 kg ÷ 5 = 1.5 g / day.

  As experimental animals, Kunming mice provided by the Faculty of Experimental Animals at Peking University are randomly divided into four groups each consisting of 64 animals. The 64 of the 4 groups were subjected to weight swimming experiments, 64 of the 2 groups were tested for blood urea nitrogen, and 64 of the 3 groups were tested for liver glycogen. A measurement experiment is conducted, and blood lactate measurement experiment is conducted on 64 animals in four sets.

  In addition, each group of four groups is administered with 16 mice, a negative control group in which nothing is administered, and NFHP of 5 times, 10 times, 30 times the human recommended use amount, that is, NFHP 0.125 / kg. low dose group to administer bw, NFHP 0.250 / kg. medium dose set for administering bw, NFHP 0.750 / kg. The high dose group to administer bw is divided into a total of 16 groups.

  Administration to mice is performed by placing distilled water in the negative control group and each dose of NFHP orally in the other group. The dose was 0.2 ml / 10 g. bw. After continuous administration for 30 days, each fatigue recovery action index is measured.

First, the following experiments (9) to (12) were performed in order to measure each fatigue recovery action index of mice by NFHP.
(9) Swimming experiment 30 minutes after the final experiment was administered to a set of mice, 5% body weight lead was placed on the tail of the mouse, and swimming was performed in the aforementioned swimming box with a water temperature of 25 ± 1 ° C. Let The time from the start of swimming until the time when all of the head is underwater and cannot float on the surface of the water is recorded as the swimming time of the mouse.

(10) Blood Urea Nitrogen Measurement Experiment 30 minutes after the final experimental product was administered to two sets of mice, the specimen was allowed to swim for 90 minutes in the aforementioned swimming box with a water temperature of 30 ± 1 ° C. After resting for 60 minutes after swimming, the eyeball is taken out, 0.5 ml blood is collected, serum is separated, and blood urea nitrogen is measured.

(11) Liver glycogen measurement experiment 30 minutes after the final experimental product was administered to three sets of experimental mice, it was allowed to swim for 90 minutes in the aforementioned swimming box with a water temperature of 30 ± 1 ° C. The patient is killed by cervical dislocation, the liver is removed, washed with physiological saline, and dried with filter paper. Weigh approximately 200 mg of liver (accurately record actual weight), homogenize with 4 ml of 5% TCA, put homogenized solution into centrifuge tube, centrifuge at 3000 rpm for 15 minutes, and put supernatant into other test tube. . Add 4 ml 5% TCA to the precipitate, homogenize for 1 minute, take the supernatant, mix with the supernatant and thoroughly homogenize. Measure liver glycogen by the Antrone method.

(12) Blood Lactate Measurement Experiment 30 minutes after the final experimental product was administered to four sets of experimental mice, 50 μl of blood was collected and placed in an anticoagulant vessel. Thereafter, 4% body weight of lead is carried on the tail of the mouse, and the mouse is allowed to swim for 10 minutes in the aforementioned swimming box having a water temperature of 30 ± 1 ° C. 50 μl of blood is collected every 0 minutes and 60 minutes after swimming, placed in an anticoagulant blood vessel, and lactic acid in the whole blood is measured with a lactic acid meter.

  The experimental data is processed by a power difference analysis software. In this experiment, the number of animals in each group was different for each experiment because it died in a swimming experiment.

The experimental results of the above (9) to (12) are shown below.
First, Tables 6, 7, and 8 show the influence on the body weight of the mice in one set of experiments, two sets of experiments, three sets of experiments, and four sets of experiments.

  From Table 6, it can be seen that there is no significant difference in the initial body weight of each group (P> 0.05), and the body weights between the experimental groups are consistent. Each dose group has a significant difference (P <0.05) in the medium-term body weight (Table 7) of the high-dose group of one experimental group compared to the negative control group, otherwise the medium-term body weight of each group There is no significant difference between the body weight and terminal weight (Table 8) (P> 0.05). That is, it means that administration of NFHP has no significant effect on the body weight of mice.

  Next, Table 9 shows the influence of NFHP administration on weight swimming time.

  From Table 9, it can be seen that the weight swimming times for the high, medium and low dose groups are all significantly different (P <0.05) compared to the negative control group. That is, this means that the administered NFHP exerts an extending action on the weight swimming time of the mouse.

  Next, Table 10 shows the effect of NFHP on blood urea nitrogen.

  From Table 10, it can be seen that there is a very significant difference (P <0.01) in the low dose set blood urea nitrogen compared to the negative control set. That is, this means that the administered NFHP exerts a lowering action on the blood urea nitrogen of the mouse.

  Next, Table 11 shows the influence of NFHP administration on liver glycogen.

  From Table 11 it can be seen that the medium dose set of liver glycogen has a very significant difference (P <0.01) compared to the negative control set. That is, this means that the administered NFHP increases the liver glycogen in mice or exerts an inhibitory action on the consumption of liver glycogen.

Next, Tables 12 and 13 show the effects of NFHP on blood lactic acid.
In Table 12, blood is collected immediately after exercise for 10 minutes, and the difference between the lactic acid value and the lactic acid value before exercise is shown. In Table 13, blood is collected immediately after exercise for 10 minutes, blood is collected again 60 minutes after exercise, and the difference value of the change in lactic acid level is shown.

  From Table 12, it can be seen that the blood lactate elevation in the low, medium and high dose groups is significantly different (P <0.01) compared to the negative control group. That is, this means that the administered NFHP exerts a lowering effect on the blood lactate increase rate in mice.

  From Table 13, it can be seen that the blood lactate removal rates for the three dose groups are significantly different (P> 0.005) compared to the negative control group. That is, this means that the administered NFHP has no effect on the blood lactate removal rate of the mouse.

Next, the experimental results will be examined.
(1) From the above experiment, it was confirmed that NFHP had no significant effect on the body weight of all mice.
(2) The above experiments confirmed that the high, medium and low dose groups of NFHP all showed very significant differences compared to the negative control group (P <0.05 and P <0.01). .
(3) According to the above experiment, NFHP showed significant and very significant differences in the blood urea nitrogen, liver glycogen, and blood lactic acid rising rates after and during exercise compared to the negative control group. Was confirmed (P <0.05 and P <0.01). However, it was confirmed that NFHP had no effect on the removal rate of blood lactic acid after exercise of mice. From these examinations, it was found that this NFHP has development value.

  In order to clarify the influence on the human body when NFHP was administered to the human body, the following experiments (13) to (15) were performed.

Experiment (13)
Six members of a university weightlifting team took 0.7 g × 2 NFHP tablets daily and took one tablet 1 h before exercise, and everyone felt a sense of hotness 1 to 2 hours later. One month later, the weightlifting performance of these six people increased to some extent.
Experiment (14)
Ten male marathoners from one company took 0.7g x 2 NFHP tablets daily. Two months later, the average score increased from 2 hours 22 minutes before taking to 2 hours 18 minutes 50 seconds.
Experiment (15)
Five high school men's athletics teams of 100 meters took 0.7g x 2 NFHP tablets daily and trained for 2 hours daily. The average result of 100m before taking is 12 seconds 60. Two months later, the average performance of 100 meters improved to 12 seconds 07. Also, a boy's performance improved from 12 seconds 80 to 11 seconds 91 before taking NFHP.

  From this experiment, it was found that the present NFHP can exert a remarkable fatigue recovery action.

In addition, this invention is not limited to the said embodiment, As it enumerates below, it is also possible to implement by changing suitably the shape and structure of each part in the range which does not deviate from the meaning of this invention.
(1) The value of the hydrogen ion concentration index is particularly preferably 7, but is applicable in the range of 6.5-7.
(2) The hydrolysis temperature is particularly preferably 50 ° C, but can be applied in the range of 50 to 55 ° C.
(3) The hydrolysis time is preferably 4 hours, but can be applied in the range of 3 to 4 hours.
(4) The locust hydrolyzate compounding agent is not limited to the composition of locust hydrolyzate blended at 60% by weight, and can be applied at 5 to 95% by weight.
(5) The locust hydrolyzate compounding agent only needs to be obtained by blending at least a locust hydrolyzate, and can be constituted alone, as well as other than bee jar frozen dried powder or royal jelly frozen dried powder. You may mix and comprise the extract, chemical | medical agent, foodstuff, etc. which used other animals and plants.

It is manufacturing-process explanatory drawing which shows one Embodiment of the locust hydrolyzate which concerns on this invention. It is manufacturing process explanatory drawing which shows other embodiment of the locust hydrolyzate which concerns on this invention.

Explanation of symbols

S1-1, S2-1 ... Pretreatment step, S1-2, S2-2 ... Hydrolysis step, S1-3, S2-3 ... Post treatment step, HC ... locust powder, HCP ... locust water Decomposition product.

Claims (5)

It is produced by hydrolyzing locust powder by adding a compounding enzyme consisting of a predetermined compounding weight ratio,
The compounding enzyme comprises papain, neutral prodinase, and polypeptidase, and the compounding weight ratio is papain: neutral prodinase: polypeptidase = 5: 3: 2.
Because
The hydrolysis is performed under the conditions of a hydrogen ion concentration index of 6.5 to 7.0, a hydrolysis temperature of 50 to 55 ° C., and a hydrolysis time of 3 to 4 hours.
Locust hydrolyzate characterized by that. To the locust powder, a papain, a neutral prodinase, and a polypeptidase are added, and a blended enzyme having a blending weight ratio of papain: neutral prodinase: polypeptidase = 5: 3: 2
Hydrolyze under conditions of hydrogen ion concentration index 6.5 to 7.0, hydrolysis temperature 50 to 55 ° C., hydrolysis time 3 to 4 hours,
A method for producing a locust hydrolyzate. It comprises the locust hydrolyzate according to claim 1 and has a remarkable fatigue recovery action.
A locust hydrolyzate formulation. A locust hydrolyzate compounding agent obtained by blending the locust hydrolyzate according to claim 1 , bee cocoon frozen dried powder, and royal jelly frozen dried powder at a predetermined blending weight ratio,
The blended weight ratio is locust hydrolyzate: bee persimmon frozen dried powder: royal jelly frozen dried powder = 3: 5: 2.
A locust hydrolyzate formulation. The dosage was 0.4 g to 45 g / person / day ,
The locust hydrolyzate compounding agent according to claim 3 or 4 .

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