JP4384249B2 - Manufacturing method of bee processed food and drink, and bee processed food and drink - Google Patents

Description

  The present invention relates to a method for producing a processed food for a bee kid, and particularly relates to a method for producing a processed food for a honey bee having a low allergenicity while enhancing the nutritional value and health promotion effect of the bee.

Conventionally, bees have been used as foods with high nutritional value, and bees such as bees, wasps, cross bees, wasps, wasps and the like have been edible. These are used for simmering, fried foods, steamed baked foods, cooking, etc., and in recent years, they are also used as luxury delicacies.
Among such bees, male bees are known to contain abundant proteins.

In particular, in the case of bees, male bees grow into pupae just before their emergence when they grow up to about 21 days of age. However, since the individual at this time is mature but has not yet emerged, it is extremely rich in protein. Contains.
In other words, the larvae of this time have the characteristics of high protein and low fat, and are rich in various active substances such as vitamins and trace elements, sugars, choline, hormones and enzymes. .

The bee pup also contains eight types of amino acids that are essential for the human body, and the contents of glutamic acid, aspartic acid, and alanine are particularly high.
In addition, the dried bee pups contain about 50% protein and about 28.7% fat, and the bees are an excellent nutritional health food.

Here, the protein of a bee is usually present as a macromolecule.
On the other hand, a certain time is required for digestion and absorption in the human body, but the time during which food stays in the human body is limited, and the contact between digestive enzymes and food is also limited.
Therefore, proteins are not completely absorbed and used in the body, and in fact, their utilization rate is very low.

In response to such problems, the protein of bee pods is decomposed stepwise into polypeptides, oligopeptides, and amino acids using natural dedicated enzymes, etc., and the utilization rate in the human body is increased. Ingenuity has been made.
That is, by enzymatically degrading the protein of the bee pupae in this way, it is possible to increase the absorbability to the human body and to improve the health promotion effect of the bee cub.

Examples of the prior art related to the enzymatic degradation of bee protein include a method for producing a processed bee honey food and a processed bee honey food described in Patent Document 1 by the present applicant.
According to this prior art, by treating the bee pup with a protease, the protein can be decomposed to lower the molecular weight, so that the texture of the processed bee pup can be improved, and the intestinal It is possible to improve the absorptivity and increase the physiological activity.

JP 2006-21946 A

However, bee fat fat forms a mass of fat around the protein in the course of enzymatic degradation. That is, when the bees are crushed and suspended in water, the fat is not dissolved in water but is dispersed as oil droplets. It is considered that this dispersed oil envelops the bee protein and the degrading enzyme.
For this reason, the binding between the protein and its degrading enzyme is inhibited, and the enzymatic decomposition of the protein of the honeybee cannot be performed sufficiently, and there is room for improvement in this respect.

  Therefore, the present inventor has conducted extensive research, and in order to sufficiently decompose the protein of the bee, first, the fat in the body of the bee is enzymatically decomposed, and then the proteolytic enzyme is added to decompose the protein. The present invention has been completed by finding that it can be carried out sufficiently.

  That is, in the present invention, prior to protein degradation, the fat of bee cubs is decomposed into substances such as fatty acids, glycerin and unsaturated fatty acids. Then, after the protein is sufficiently exposed to the surface, it is effectively brought into contact with a protease or the like to increase the catalytic efficiency, thereby making it possible to more efficiently decompose the protein of the bee.

In addition, there is a protein that is an allergen that causes an allergic reaction in people with allergic constitutions.
According to the present invention, since the protein of the bee pod can be sufficiently decomposed, such an allergen protein can also be decomposed, and the allergenicity of the processed honey-processed food and drink can be effectively improved. It is possible.

  It is also possible to add various various effects that the protein of bees has to the bee-processed food and drink by sufficiently degrading the protein of bees and generating various peptides. It has become.

Furthermore, the carbohydrate component contained in the bee larvae includes those that cannot be properly digested by the human body.
According to the present invention, by using β-mannosidase, it is possible to decompose such a saccharide component and make it easier for the human body to absorb the oligosaccharide component.

  The present invention has been made in view of the above circumstances, and after adding a lipolytic enzyme to a suspension containing bee powder and decomposing the lipid, the protein is decomposed by adding a proteolytic enzyme. Thus, an object of the present invention is to provide a method for manufacturing a bee-processed food and drink that can sufficiently decompose the protein of the bee-child, and a bee-processed food and drink.

  In order to achieve the above-mentioned object, the method for producing processed foods and drinks for bees of the present invention is to powder dried bees and suspend them in water, and then add lipolytic enzyme to decompose the lipids of the bees. And a step of adding a proteolytic enzyme and decomposing the protein of the bee after this step.

If the manufacturing method of the processed food for bees is such a method, the mass of fat formed around the protein can be decomposed and the contact efficiency between the protein and its degrading enzyme can be increased.
For this reason, it becomes possible to decompose | degrade the protein of a bee efficiently.

Moreover, the manufacturing method of the bee pea processed food / beverage products of this invention is a method which has the process of adding a saccharide-degrading enzyme and decomposing | disassembling the sugar of a bee kid after the protein decomposition | disassembly process.
If this method is used for manufacturing bee candy processed foods and drinks, it effectively decomposes useful carbohydrates that are contained in bees and cannot be decomposed by enzymes naturally present in the human body. be able to.
For this reason, it becomes possible to make a human body effectively absorb the component obtained from such useful carbohydrates.

Moreover, the manufacturing method of the bee processed food / beverage products of this invention is a method of decomposing | disassembling lipid by adjusting the pH of suspension to 6.0-11.0 and adding a lipase in the decomposition | disassembly process of a lipid. is there.
If the manufacturing method of the processed food for bees is made in this way, the lipase can be appropriately activated and the lipid can be efficiently decomposed.
For this reason, the lump of fat formed around the protein of the bee can be removed, and the protein of the bee can be decomposed more efficiently.

Moreover, the manufacturing method of the processed food for food and drink of bees according to the present invention is a method using β-mannosidase as a saccharide-degrading enzyme.
In the carbohydrate decomposition step, the pH of the suspension is adjusted to 5.4 to 7.0, and β-mannosidase is added to decompose the carbohydrate.

  If the manufacturing method of bee candy processed foods and drinks is such a method, β-mannosidase can be activated and oligosaccharide components can be obtained efficiently, and the bee pea processed foods and drinks having high nutritional value are provided. It becomes possible to do.

In addition, the method for producing a processed food product of a bee of the present invention includes a step of heating a decomposition solution obtained by decomposing a saccharide, inactivating an enzyme contained in the decomposition solution, and filtering it. is there.
If the manufacturing method of a bee candy processed food / beverage is such a method, it becomes possible to provide the bee candy processed food / beverage products which contain an abundant active ingredient of a honey bee.

Moreover, it is preferable that the manufacturing method of the processed food and drink of the bee child of this invention uses the male child of a bee as a bee child.
Moreover, it is preferable to use a 20-23 day old cocoon as a bee male child.

The bee male is one of the few bees born only to mate with the queen bee, and contains unique hormones, etc. that are not found in the female and queen bees.
In addition, post-natal (after laying) 20-23 day male bees, especially 21-day-old pupae, are in the state of pupae just before emergence, have the highest content of nutrient sources such as amino acids, and have the most emergence hormones. Has been produced.
For this reason, it becomes possible by using such a bee child to provide the bee child processed food and drink excellent in nutritional value.

Moreover, the bee-processed food or drink of the present invention is manufactured by any one of the methods described above.
The bee-processed food / beverage product manufactured in this way is obtained by efficiently decomposing lipids, proteins, etc., and is a bee-processed food / beverage product having an excellent nutritional value.

  According to the present invention, it is possible to efficiently and sufficiently carry out proteolysis of bee pupae, and it is possible to further increase the nutritional value of processed foods and drinks for scallops.

It is a figure which shows the range of the optimal pH of the enzyme used in one Embodiment of this invention. It is a figure which shows the manufacturing process of the bee processing processed food / beverage products of one Embodiment of this invention. It is a figure which shows the MS spectrum (mass spectrum) of the peptide from the dried powder of a bee obtained by performing proteolysis after lipid degradation according to Example 1. It is a figure which shows the MS spectrum of the peptide from the dried bee powder obtained without performing a lipolysis and a protein enzyme degradation by the comparative example 1. It is a figure which shows the MS spectrum of the peptide from the dried bee powder obtained by performing proteolysis without performing lipolysis according to Comparative Example 2. 1 is a diagram showing an MS spectrum of a saccharide from dried bee powder obtained by performing proteolysis following lipid degradation in Example 1. FIG. It is a figure which shows the MS spectrum of the saccharide | sugar from the dried powder of a bee obtained by carrying out proteolysis after lipid decomposition | disassembly by Example 2, and also performing saccharide | sugar decomposition | disassembly next. It is a figure which shows the MS spectrum of the saccharide | sugar from the dried bee powder obtained by Comparative Example 1 without performing any of these enzymatic decompositions. It is a figure which shows the MS spectrum of the saccharide | sugar from the dried bee powder obtained by performing saccharide | sugar decomposition | disassembly, without performing a lipolysis and a protein decomposition | disassembly by the comparative example 3. It is a figure which shows each decomposition condition of an Example and a comparative example.

In the present invention, dried bee powder is powdered and suspended in water, the pH of this suspension is adjusted, lipolytic enzyme is added to break down the lipid, and the pH of the suspension is adjusted again. The protein is degraded by adding a proteolytic enzyme.
Hereinafter, embodiments of the present invention will be described in detail.

(Bees)
First, the bee used as a raw material in the manufacturing method of the bee processed food / beverage products of this embodiment is demonstrated.
The bee pup used in this embodiment is not particularly limited, but it is preferable to use an individual when the bee grows up to about 21 days of age.
At this time, the male bees are in a cocoon state, mature but not yet emerged, and contain an extremely rich protein.

  Next, the enzyme used in this embodiment and the decomposition | disassembly by the enzyme are demonstrated with reference to FIG. The figure shows the range of the optimum pH of the enzyme used in this embodiment.

<Lipolytic enzyme>
(Lipase)
Lipase breaks down fat into substances such as fatty acids, glycerin and unsaturated fatty acids.
The lipase is activated in a solution having a pH of 6.0 to 11.0 and a temperature of 15 to 45 ° C., and efficiently decomposes fat.

<Glycolytic enzyme>
(Β-mannosidase)
β-Mannosidase (β-mannosidase EC3.2.1.25) is an enzyme that degrades mannan into small molecular weight carbohydrates such as oligosaccharides.
β-mannosidase is activated in a solution having a pH of 5.4 to 7.0 and a temperature of 30 to 40 ° C., and efficiently decomposes mannan.

Mannan is highly hydrophilic and absorbs a large amount of water in the digestive tract of monogastric animals to increase the viscosity of the digestive tract contents, resisting gastrointestinal peristalsis, A polysaccharide that directly affects absorption.
The oligosaccharide obtained by decomposition is a kind of new type of effective oligosaccharide. This is a kind of excellent Bifidus Factor that promotes the growth of Bacillus bifidus, which is a beneficial bacterium in the intestinal tract of the human body and animals, and improves the bacterial group structure in the intestinal tract.

Mannanase is an enzyme that hydrolyzes N-linked glycosylation (N-glycosylation).
It is mainly divided into α-mannosidase and β-mannosidase according to the difference in Sites).
α-Mannosidase hydrolyzes mannose α-1,2, α-1,3, α-1,6 glucosidic bonds, and β-mannosidase hydrolyzes β-1,4 glucoside bonds. Decompose.

  This β-mannosidase is a kind of hemicellulase, which breaks down the β-1,4 glucoside bond in an exo-exo manner. β-mannosidase can degrade substrates such as glucomannan and galactomannan, and hydrolyzes mannose residues from the non-reducing end one residue at a time.

  Hemicellulases include endo-type enzymes such as β-mannanase and xylanase, β-glucosidase (also known as cellobiase), β-mannosidase, β-xylosidase (β There are exo-type enzymes such as -xylosidase, and enzymes such as α-L-arabinofuranosidase, galactosidase, and glucuronidase.

  For complete enzymatic degradation of mannan, mannan-endo-1,4-β-mannosidase (mannan-endo-1,4-β-mannosidase EC3.2.1.78), β-mannosidase EC3. 2.1.25), β-glucosidase, α-galactosidase EC3.2.1.22 and acetylesterase EC3.1.1.6 are required.

The degree of action of differently derived β-mannosidases on differently derived substrates and their hydrolysates are not the same.
That is, the method and degree of hydrolysis of the substrate by β-mannosidase is mainly related to the position and content of the main chain of the galactose and glucose residues in the substrate. To do. The physical state of the substrate itself also affects the action of the enzyme on the substrate. For example, mannan in a crystalline state is difficult to be decomposed.

Mannan is decomposed by β-mannosidase, and then subjected to HPLC or paper chromatography, oligosaccharides (Oligosaccharides, generally 2 to 10 residues) are separated as main products.
The degree of polymerization of the product is related to the origin of the enzyme / substrate, and relatively little or almost no monosaccharide (mannose mannose) is produced.
Oligosaccharides are a new type of potent oligosaccharide that promotes the growth of beneficial bacteria such as bifidobacteria in the intestinal tract of the human body and animals, and a kind of superior bifido factor that improves the binding of enterobacteria group. It is.

In addition, β-mannosidase hydrolyzes mannan, glucomannan and the like to produce mannan oligosaccharide (MOS).
This mannan oligosaccharide is also effective as a growth factor for bifidobacteria to naturally propagate beneficial bacteria in the body, improve the binding of enterobacteria group, and regulate the efficacy of the intestinal digestive system.
For this reason, mannan oligosaccharides have physiological activities such as liver retention, antitumor, immunity enhancement, peristalsis of the intestinal tract, cholesterol reduction, and anti-senescence. It can also be applied to various intestinal diseases, and is suitable for human health, especially for elderly people and children's daily health.

In addition, mannan oligosaccharide has excellent sweetness quality and is used as a kind of excellent food additive in place of sucrose in foods such as beverages, strawberries, biscuits, canned fruits, dairy products, Outside of Japan, it is also widely used for health food.
For this reason, by adding a certain amount of β-mannosidase to the food, accumulation of the nutrient substance in the intestinal tract can be reduced, and digestion and absorption of the nutrient substance can be improved.

<Proteolytic enzyme>
Proteolytic enzymes are substances that generate low-molecular peptides by degrading proteins in digestive organs or the like in the body, and can be absorbed into the body. There are various types of proteolytic enzymes as shown below, and all of them are used to obtain small molecule peptides, and it is not necessary to limit the types of the proteases in carrying out the present invention.

  A peptide generally means an amino acid chain having a molecular weight in the range of 180-5000, a peptide having a molecular weight in the range of 1000-5000 is a large peptide, and a molecule having a molecular weight in the range of 180-1000 is a small molecule peptide (low molecular peptide, Oligopeptide). In addition, small molecule active polypeptides are collectively referred to as “bioactive peptides”.

A low molecular weight peptide obtained by enzymatic degradation is absorbed and utilized by the human body more easily and more quickly than a complete free amino acid.
These low molecular peptides not only provide nutrients necessary for the growth and development of the human body, but also prevent and treat blood clots, hyperlipidemia and hypertension, delay aging, anti-fatigue effects, organisms Some have unique biological effects that can enhance immunity.
The biological efficacy of such a low molecular weight peptide is an important physiological function, not the protein of the original food or the amino acid that is its basic binding unit.

  In other words, such low molecular weight peptides have extremely strong activity and diversity as bioactive peptides, and as research progresses, they are increasingly attracting attention all over the world. , In the fields of medicine, nutrition, food, etc.

  For example, small peptides bind to special receptors in the intestinal tract to promote gastrointestinal tract development and promote digestion and absorption. In addition, some of them enter the blood circulation system, adjust the human immune function, adjust the growth of the animal through the growth axis, and fully exert the production potential of the animal. An example will be described below.

(1) Promotion of protein synthesis
According to the research results of Boza et al. (1995), Infante et al. (1992), Pullain et al. (1991), when low molecular weight peptides are used as a nitrogen source, protein deposition is determined by Higher than daily intake. An increase in protein deposition means an increase in protein synthesis rate and a relative decrease in degradation rate.

  In addition, according to the observation by Wang et al. (1994), the action of promoting the penetration of 3H-Leu into tissue proteins by several peptides derived from methionine is greater than that of methionine itself. This indicates that low molecular weight peptides are involved in and promote protein synthesis in organisms.

(2) Promotion of mineral absorption and utilization
According to a report of Found (1974), metal ions around the pentacoordinate or hexacoordinate complex are absorbed in the form of small peptides through the villi brush border of the small intestine. Lee Yongfeng et al. (2000) added low-molecular-weight peptide iron and iron-dextran to 1 to 21-day-old piglets, respectively, and measured serum iron protein content after 14 days. The addition of low molecular weight iron was higher than that of dextran iron and the control experiment. This indicates that mineral ions in the form of low molecular peptide complexes are more easily absorbed by the organism. That is, it has been clarified that low molecular weight peptides promote the absorption and utilization of minerals.

(3) Avoid absorption competition between amino acids
According to the observations of Rubino et al. (1971), peptides do not affect free amino acid absorption, and different free amino acids do not affect small peptides. According to a report by Pharasan et al. (1987), when lysine and arginine exist in free form, they compete with each other for their absorption position, and free arginine absorbs lysine into the hepatic portal vein. There is a tendency to reduce. In contrast, free arginine has no effect on lysine absorption when lysine is present in a low molecular peptide form. This indicates that low molecular weight peptides are involved in metabolism and avoid absorption competition between amino acids.

(4) Increase the immunity of organisms Low molecular weight peptides can enhance the growth of beneficial bacteria, promote the synthesis of bacterial proteins, and enhance anti-disease power. Studies have shown that small peptides effectively stimulate and induce increased intestinal choriobrush border enzyme activity and promote animal nutritional health recovery.

  The results of Jelle (1981, 1982) revealed that tripeptides and hexapeptides produced by hydrolysis with β-casein promote macrophage predation. ing. Storia (1994) states that a kind of low molecular weight peptide synthesized using porcine bone marrow cDNA as a template has an inhibitory effect on Gram-negative and positive bacteria. Andeson (1995) states that N-lysine oligopeptides (Oligopeptides) isolated from the small intestine of pigs have an inhibitory effect on colon bacilli and the like.

(5) Physiological regulation action As a neurotransmitter, a low molecular weight peptide promotes the secretion of an intestinal receptor hormone or enzyme and exerts its action.
For example, Casomorphin (7-10 amino acid residues) produced by β-casein hydrolysis is similar in amino acid sequence order to that of an endogenous opioid peptide. The purified pentapeptide “Tyr-Pro-Phe-Gly-Ile” and the tetrapeptide “Tyr-Pro-Phe-Pro” both have the activity of opioid peptides. Have.

According to the report of Rakuguni Wei et al. (1997), a precursor of opioid peptide exists in the hydrolyzate of pepsin of wheat grain protein. It enters the blood circulation and exerts a physiological activity as a neurotransmitter.
As described above, some low molecular weight peptides have various unique biological effects.

Bee pup proteins usually exist in the form of macromolecules, and it takes a certain amount of time to digest and absorb such macromolecules in the human body.
On the other hand, the time for which food stays in the human body is limited, and the contact between digestive enzymes and food is also limited.
Accordingly, proteins are generally not completely absorbed and utilized in the body, and their utilization rate is very low.

Therefore, in the method for producing a processed bee candy food or drink according to the present embodiment, the protein of the honey bee is decomposed using a specific enzyme such as the following, a polypeptide such as a bioactive peptide, an oligopeptide, or an amino acid. It produces nutrients that are suitable for human absorption.
As a result, the absorption utilization rate of the protein of the honeybee is increased, and the nutritional effect and health health effect can be increased.

(Acid protease)
Acid Protease is a proteolytic enzyme having an optimum pH on the acidic side, and has an amino acid aspartic acid at an active site, and is also called aspartic protease.
The acidic protease is activated in a solution having a pH of 2.0 to 4.0 and a temperature of 30 to 50 ° C.

(Alkaline protease)
Alkaline protease is a proteolytic enzyme having an optimum pH on the basic side.
The alkaline protease is activated in a solution having a pH of 8.0 to 11.0 and a temperature of 45 to 60 ° C.

(Neutral protease)
Neutral protease is a proteolytic enzyme having an optimum pH at neutral.
The neutral protease is activated in a solution having a pH of 6.5 to 7.5 and a temperature of 45 to 52 ° C.

(Composite protease)
The complex protease is a highly effective protein hydrolyzing complex enzyme that has been researched and developed especially for hydrolyzing various glycoproteins. This is mainly composed of endopeptidase, exopeptidase, and Flavorzyme (registered trademark) . The peptide chain inside the protein is cleaved from the middle by endopeptidase, and the amino acid is cleaved and released from the end of the polypeptide enzyme by exopeptidase. In addition, flavorzyme has the effect of improving the bitterness and flavor of hydrolyzed products, and is widely used for protein hydrolysis of animal proteins, for example, meat such as chicken, pig and cow, and fishery products such as fish and shrimp. Can do.
The complex protease is activated in a solution having a pH of 6.5 to 7.5 and a temperature of 55 to 60 ° C.

(Trypsin)
Trypsin cleaves peptide bonds on the carboxyl side of lysine or arginine.
Trypsin is activated in a solution having a pH of 5.5 to 7.0 and a temperature of 50 to 55 ° C.

(pepsin)
Pepsin cleaves a peptide bond on the carboxyl-terminal side of a protein or peptide chain from an acidic amino acid residue to an aromatic amino acid residue and the subsequent sequence.
Pepsin is activated in a solution having a pH of 1.5 to 2.0 and a temperature of 37 to 50 ° C.

(Papain)
Papain cleaves peptide bonds between basic amino acids, glycine and leucine, and subsequent amino acids of proteins and peptide chains.
Papain is activated in a solution having a pH of 3.0 to 9.0 and a temperature of 50 to 65 ° C.

(Bromelain)
Bromelin is a proteolytic enzyme classified as a cysteine protease extracted from pineapple.
Bromelain is activated in a solution having a pH of 6.0 to 6.8 and a temperature of 30 to 45 ° C.

(Peptidase)
Peptidase is an enzyme that degrades peptide bonds, and for example, a peptidase (type number: TM-G-NA) manufactured by Tianjin Xinku Science and Technology Development Co., Ltd. can be suitably used.
Peptidase is activated in a solution having a pH of 4.0 to 8.0 and a temperature of 50 to 65 ° C.

(Flavorzyme)
Flavorzyme is an industrial enzyme manufactured by Novozymes Japan K.K. and has a high hydrolysis rate.
The flavorzyme is activated in a solution having a pH of 6.0 to 6.5 and a temperature of 50 to 60 ° C.

(Plant protease)
Plant proteases are a newly developed complex enzyme preparation dedicated to plant protein hydrolysis. This is mainly composed of endopeptidase, exopeptidase, flavorzyme, and the like. The peptide chain inside the protein is cleaved from the middle by endopeptidase, and the amino acid is cleaved and released from the end of the polypeptide enzyme by exopeptidase. In addition, flavorzyme has the effect of improving the bitterness and flavor of the hydrolyzate.
The plant protease is activated in a solution having a pH of 5.5 to 7.5 and a temperature of 55 to 65 ° C.

(Animal protease)
Animal protease is a newly developed complex enzyme preparation dedicated to the hydrolysis of animal proteins. This is mainly composed of endopeptidase, exopeptidase, flavorzyme, and the like. The peptide chain inside the protein is cleaved from the middle by endopeptidase, and the amino acid is cleaved and released from the end of the polypeptide enzyme by exopeptidase. In addition, flavorzyme has the effect of improving the bitterness and flavor of the hydrolyzate.
Animal proteases are activated in solutions having a pH of 6.5-7.0 and a temperature of 55-60 ° C.

(Cathepsin A)
Cathepsin is a protease found in cells of various animal tissues (particularly the lysosome portion). The name comes from the Greek word “digestion” and was named by Virustetter (1929). There are various types of cathepsins such as cathepsins A, B, C, D, and E. These are classified based on the typical substrate on which they act, and it is considered that there are several types of isozymes (Isozyme, Isoenzyme).

A typical substrate for cathepsin A is N-benzoyloxycarbonyl-L-glutamine-L-phenylalanine, which is considered to be a kind of carboxypeptidase. It can be inactivated using diisopropylfluorophosphate (DFP) or p-chloromercuribenzoic acid (PCMB).
Cathepsin A is activated in a solution having a pH of 3.0 to 6.0 (optimal pH is about 5.5) and a temperature of 30 to 50 ° C.

(Cathepsin B)
Cathepsin B catalyzes the hydrolysis of Benzoyl-L-arginine. Presence of sulfhydryl compounds (SH compounds) is required for activity and is thought to be similar to papain's endopeptidase. There are two types already known, B1 and B2 (or B ′ and B). Cathepsin B is localized in lysosomes of various animal cells. It is a cysteine protease containing a cysteine residue in the active center and has a strong ability to reduce the molecular weight of proteins.
Cathepsin B is activated in a solution having a pH of 5.0 to 7.0 (optimum pH is about 6.0) and a temperature of 30 to 50 ° C.

(Cathepsin C)
Cathepsin C is a cysteine protease. It is activated by sulfhydryl compounds or chloride ions. Its typical substrate is glycyl-L-phenylalaninamide, which catalyzes the hydrolysis of an amido bond around pH 5. As an acceptor, catalyzing a transfer reaction, dipeptidyl aminopeptidase I (named by the first reaction), or dipeptide (dipeptide or dipeptidyl) transferase (from the second reaction) It is also called naming.
Cathepsin C is activated in a solution having a pH of 6.0 to 7.0 and a temperature of 30 to 50 ° C.

(Cathepsin D)
Cathepsin D exhibits the action of endopeptidase on digested acid-denatured haemoglobin or serum albumin when the pH is 2.5 to 4.0. The sulfhydryl compound does not affect the activity, and the activity is not suppressed by DFP (diisopropyl fluorophosphate). Cathepsin D is a lysosomal enzyme and is activated in a solution having a temperature of 30 to 50 ° C.

(Cathepsin E)
Cathepsin E exhibits the action of endopeptidase on digested acid-denatured hemoglobin or serum albumin when the pH is 2.5 to 4.0. The sulfhydryl compound and iodoacetic acid do not affect the activity, and the activity is not suppressed by DFP.
Cathepsin E is locally present in immunocompetent cells, particularly macrophages and dendritic cells that are antigen-presenting cells. Cathepsin E is activated in a solution having a temperature of 30 to 50 ° C.

(Chymotrypsin)
Chymotrypsin is a kind of serine protease and cleaves a peptide bond on the carboxyl group side of an aromatic amino acid. Secreted from the pancreas and rapidly degrades denatured proteins.
Chymotrypsin is activated in a solution having a pH of 5.5 to 7.0 and a temperature of 37 to 50 ° C.

Next, the manufacturing method of the bee processed food / beverage products of this embodiment is demonstrated with reference to FIG. The figure has shown the manufacturing process of the bee processing processed food / beverage products of this embodiment.
(A) Grinding step First, a male bee cub (hereinafter referred to as a bee cub) is dried and pulverized to 100 mesh. At this time, the bee pup can be dried by freeze drying (freeze drying). In addition, when pulverizing the male bee, it can be carried out using a crushing equipment such as a universal pulverizer, Shibata pulverizer (manufactured by Shibata Kagaku Co., Ltd.), a ball mill, a vibration mill, etc. it can.

(B) Inspection process Next, it is test | inspected whether the bee child could be grind | pulverized appropriately. At this time, a 100 mesh standard sieve is used. A passing rate of 95% is accepted.

(C) Suspension step Further, the obtained stabbling powder is placed in an enzyme decomposition tank, and 5 times volume of deionized water is added to the enzyme decomposition tank at room temperature.
Then, the mixture is sufficiently stirred to obtain a suspension containing the bee powder uniformly throughout. At this time, the stirring time is preferably 1 to 3 hours.

(D) (D ′) (D ″) pH adjustment step Next, the pH value of the aqueous solution containing male bees is adjusted using a NaOH solution and a citric acid solution having different concentrations. Therefore, the pH value of the male bee aqueous solution is adjusted to a relatively stable value by adjusting the pH value using an alkaline solution and an acidic solution having different concentrations. This is done to improve the efficiency of enzymatic degradation.
In addition, the said process is a process performed before each following decomposition | disassembly process, as shown in FIG.

(E) Lipid decomposition process By said method, while adjusting the pH value of a solution to the range of 6.0-11.0, the temperature of a solution shall be 15-45 degreeC, and 0.3-1.0% of raw materials Enzymatic degradation is performed by adding lipase. The decomposition time is preferably 0.5 to 1 h.
As a result, fat forming a mass around the protein can be removed, and in the following steps, the protein can be sufficiently brought into contact with the proteolytic enzyme.

(F) Proteolytic step Next, the pH value of the solution is adjusted by the above-described method, and a predetermined amount of proteolytic enzyme is added to perform enzymatic degradation.
At this time, the pH value, the temperature of the solution, and the proteolytic enzyme and the amount added thereof can be as follows (1) to (18), respectively.

  In this proteolysis step, one proteolytic enzyme can be used, and pH value adjustment and proteolysis can be alternately performed using a plurality of proteolytic enzymes. At this time, the order of the proteolytic enzymes used is not particularly limited.

(1) The pH value of the solution is adjusted to a range of 2.0 to 4.0, the temperature of the solution is set to 30 to 50 ° C., and 0.01 to 0.06% of acidic protease of the raw material is added to perform enzymatic degradation. I do.
(2) The pH value of the solution is adjusted to the range of 8.0 to 11.0, the temperature of the solution is set to 45 to 60 ° C., and 0.03 to 0.1% alkaline protease of the raw material is added to perform enzymatic degradation. I do.

(3) The pH value of the solution is adjusted to the range of 6.5 to 7.5, the temperature of the solution is set to 45 to 52 ° C., and neutral protease of 0.3 to 1.0% of the raw material is added to the enzyme Disassemble.
(4) The pH value of the solution is adjusted to a range of 6.5 to 7.5, the temperature of the solution is set to 55 to 60 ° C., and 0.1 to 0.6% of the complex protease is added to the enzyme decomposition. I do.

(5) The pH value of the solution is adjusted to the range of 5.5 to 7.0, the temperature of the solution is set to 50 to 55 ° C., and 0.01 to 0.06% trypsin of the raw material is added to perform enzymatic degradation. Do.
(6) While adjusting the pH value of the solution to a range of 1.5 to 2.0, the temperature of the solution is set to 37 to 50 ° C., and 0.01 to 0.03% of pepsin as a raw material is added to perform enzymatic degradation. Do.

(7) The pH value of the solution is adjusted to a range of 3.0 to 9.0, the temperature of the solution is set to 50 to 65 ° C., and 0.1 to 0.3% of papain as a raw material is added to perform enzymatic decomposition. Do.
(8) The pH value of the solution is adjusted to a range of 6.0 to 6.8, the temperature of the solution is adjusted to 30 to 45 ° C., and 0.2 to 1.0% bromelain of the raw material is added to perform enzymatic decomposition. Do.

(9) The pH value of the solution is adjusted to a range of 4.0 to 8.0, the temperature of the solution is set to 50 to 65 ° C., and 0.1 to 0.3% of peptidase as a raw material is added to perform enzymatic degradation. Do.
(10) The pH value of the solution is adjusted to a range of 6.0 to 6.5, the temperature of the solution is set to 50 to 60 ° C., and 0.1 to 0.3% of the flavorzyme of the raw material is added for enzymatic degradation. I do.

(11) The pH value of the solution is adjusted to a range of 5.5 to 7.5, the temperature of the solution is set to 55 to 65 ° C., and 0.1 to 0.6% plant protease of the raw material is added to the enzyme Disassemble.
(12) The pH value of the solution is adjusted to a range of 6.5 to 7.0, the temperature of the solution is set to 55 to 60 ° C., and 0.3 to 0.6% of animal protease of the raw material is added to the enzyme Disassemble.

(13) The pH value of the solution is adjusted to a range of 3.0 to 6.0, the temperature of the solution is adjusted to 30 to 50 ° C., and 0.1 to 0.6% of cathepsin A as a raw material is added for enzymatic degradation. I do.
(14) The pH value of the solution is adjusted to a range of 5.0 to 7.0, the temperature of the solution is set to 30 to 50 ° C., and cathepsin B of 0.1 to 0.6% of the raw material is added to perform enzymatic degradation. I do.

(15) The pH value of the solution is adjusted to a range of 6.0 to 7.0, the temperature of the solution is adjusted to 30 to 50 ° C., and cathepsin C of 0.1 to 0.6% of the raw material is added to perform enzymatic degradation. I do.
(16) The pH value of the solution is adjusted to a range of 2.5 to 4.0, the temperature of the solution is set to 30 to 50 ° C., and 0.01 to 0.06% cathepsin D of the raw material is added to perform enzymatic degradation. I do.

(17) The pH value of the solution is adjusted to a range of 2.5 to 4.0, the temperature of the solution is set to 30 to 50 ° C., and 0.01 to 0.06% cathepsin E of the raw material is added to perform enzymatic degradation. I do.
(18) The pH value of the solution is adjusted to a range of 5.5 to 7.0, the temperature of the solution is set to 37 to 50 ° C., and 0.01 to 0.03% of chymotrypsin of the raw material is added to perform enzymatic degradation. Do.
In the above decomposition step, the decomposition time is preferably 3 to 6 hours.

(G) Carbohydrate decomposition step Next, the pH value of the solution is adjusted to a range of 5.4 to 7.0 by the above method, and the temperature of the solution is set to 30 to 40 ° C. Enzymatic degradation is performed by adding 0.06% β-mannosidase. The decomposition time is preferably 1 to 3 h.

(H) Enzyme inactivation step When the enzyme decomposition step is completed, the temperature of the solution is then raised to 80 ° C., and the activity of the enzyme in the solution is extinguished (inactivated). The inactivation time is preferably at least about 30 minutes.

(I) Filtration step Next, the enzyme-decomposed solution in which the enzyme is inactivated is filtered through a filter, and the obtained filtrate is placed in a tank for 24 hours.
Then, the supernatant liquid is taken out, and the pressure filter is filled with activated carbon for food and filtered to obtain a clear filtrate.

(J) Drying process Finally, the obtained filtrate is dried with a spray dryer. At this time, the inlet temperature is preferably 185 to 200 ° C, the outlet temperature is 65 ° C to 80 ° C, and the flow rate is preferably 30 to 50 L / h.

The obtained processed bee product can be used as a product as it is, but if necessary, it can also be formed into a product by molding by means such as granulation, tableting and encapsulation.
Further, for example, it can be added to foods such as bread, fish paste products, livestock paste products, dairy products, and beverages such as soft drinks, milk drinks, protein supplement drinks for the purpose of nutritional enhancement and physiological activity.
As a product form of processed foods and drinks for bees, various forms such as tablets, capsules, powders, granules, liquids, pastes, and jellys can be used.

Example 1
100 g of dried bees were pulverized to 100 mesh and tested to see if they were properly pulverized using a 100-mesh standard sieve to confirm that they passed.
Next, the obtained bee powder is placed in an enzymatic decomposition tank, 0.5 L of deionized water is added to the enzymatic decomposition tank at room temperature, and the mixture is stirred for 1 hour. Ionic water was made into an even suspension.

  Next, the pH value of the solution is adjusted to 8.0 using a 6M NaOH solution, the temperature of the solution is adjusted to 25 ° C., and 0.5 g (0.5% of the raw material) of lipase is added. Enzymatic degradation was performed for a minute.

Next, the pH value of the solution is adjusted to 7.0 using a 2M citric acid solution, and the temperature of the solution is adjusted to 48 ° C., and the neutral protease (ZDB-G-5, Guangxi Nanning Hobo Bioprocess) 0.8 g (0.8% of the raw material) was added, and enzymatic degradation was performed for 4 hours.
Then, the temperature of the solution was set to 80 ° C., and the enzyme in the solution was inactivated for 30 minutes.

Next, the solution is filtered through a filter, the resulting filtrate is placed in a tank for 24 hours, the supernatant liquid is taken out, the activated carbon for food is filled in a pressure filter, and the filtrate is filtered. A liquid was obtained.
Finally, the obtained filtrate was dried with a spray dryer. At this time, the inlet temperature was 190 ° C., the outlet temperature was 70 ° C., and the flow rate was 40 L / h.
Through the above steps, 83 g of processed food of bee powder was obtained.

(Example 2)
In the same manner as in Example 1, 100 g of dried bee pups were pulverized and subjected to lipolysis with lipase and proteolysis with neutral protease.
Next, using a 2M citric acid solution, the pH value of the solution is adjusted to a range of 6.0, the temperature of the solution is set to 35 ° C., and 0.04 g (0.04% of the raw material) of β- Mannosidase was added and enzymatic degradation was performed for 2 hours.
Then, the temperature of the solution was set to 80 ° C., and the enzyme in the solution was inactivated for 30 minutes.

Next, the solution is filtered through a filter, the resulting filtrate is placed in a tank for 24 hours, the supernatant liquid is taken out, the activated carbon for food is filled in a pressure filter, and the filtrate is filtered. A liquid was obtained.
Finally, the obtained filtrate was dried with a spray dryer. At this time, the inlet temperature was 190 ° C., the outlet temperature was 70 ° C., and the flow rate was 40 L / h.
By the above process, 84 g of processed food of bee powder was obtained.

(Example 3)
As the proteolytic enzyme to be used, 0.05 g (0.05% of the raw material) of alkaline protease (JDB-G-NA, manufactured by Tianjin Xinku Science Development Co., Ltd.) is used, and the pH value of the solution is adjusted to 9.5. At the same time, except that the temperature of the solution was treated at 52 ° C., it was performed in the same manner as in Example 2 to obtain 83 g of processed food of bee powder.

(Example 4)
As a proteolytic enzyme to be used, 0.03 g (0.03% of the raw material) of acidic protease (SDB-G-2, manufactured by Tianjin Xinku Technology Development Co., Ltd.) is used, and the pH value of the solution is adjusted to 3, Except for treating the solution at a temperature of 40 ° C., the same procedure as in Example 2 was carried out to obtain 85 g of processed food of bee powder.

(Comparative Example 1)
100 g of dried bees were pulverized to 100 mesh and tested to see if they were properly pulverized using a 100-mesh standard sieve to confirm that they passed.
Next, the obtained bee powder is placed in an enzymatic decomposition tank, 0.5 L of deionized water is added to the enzymatic decomposition tank at room temperature, and the mixture is stirred for 1 hour. Ionic water was made into an even suspension.
This suspension was dried with a spray dryer. At this time, the inlet temperature was 190 ° C., the outlet temperature was 70 ° C., and the flow rate was 40 L / h.
By the above steps, 82 g of processed food of bee powder was obtained.

(Comparative Example 2)
The lipolysis step was omitted from the step of Example 1, and only the proteolysis step was performed as the enzymatic degradation to obtain 82 g of processed food of bee powder.

(Comparative Example 3)
The lipolysis step and the proteolysis step were omitted from the step of Example 2, and only the carbohydrate decomposition step was performed as the enzymatic decomposition to obtain 83 g of processed food of bee powder.

(Test Example 1)
Compared with dried bee powder obtained by performing proteolysis following lipid degradation according to Example 1, and dried bee powder obtained without performing any of these enzymatic degradations according to Comparative Example 1. For each dried bee powder obtained by proteolysis without performing lipolysis according to Example 2, a sample for peptide analysis was prepared by a conventional method, and a matrix-assisted laser desorption / ionization time-of-flight mass spectrometer (MALDI-TOF-MS: Matrix Assisted Laser Desorption Ionization-Time Of Flight-MS).

  The results are shown in FIG. 3, FIG. 4 and FIG. FIG. 3 is an MS spectrum of the peptide from dried bee powder obtained by performing lipolysis followed by proteolysis according to Example 1. FIG. 4 is an MS spectrum of the peptide from dried bee powder obtained in Comparative Example 1 without performing lipolysis and protein enzyme degradation. FIG. 5 is an MS spectrum of a peptide from dried bee powder obtained by proteolysis without performing lipolysis according to Comparative Example 2. In addition, in FIG. 10, the drawing number corresponding to the enzyme decomposition | disassembly conditions in each Example and a comparative example is shown.

As shown in FIG. 4, when the bees were not enzymatically decomposed, the peptides are mainly present in the vicinity of a molecular weight of 5000. On the other hand, as shown in FIGS. 3 and 5, when proteolysis is performed, those peaks disappear, and at the same time, lower molecular peptides exist.
This indicates that the protein of the bee is easily absorbed by the human body by a proteolytic enzyme and is degraded into a low molecular weight peptide that is expected to have biological efficacy.

  3 and FIG. 5 are not decomposed only in the peak of the main component of the peptide in FIG. 4 but also in the polymer component not shown in FIG. 3 and 5 are contained in the main components of the peptide.

In addition, the height of the main peak having a molecular weight of 1254 in FIG. 3 is about 10 times the height of the main peak having a molecular weight of 1875 in FIG. 5. The amount of peptide is increasing.
This indicates that the protein of bee pups is more efficiently reduced by proteolysis after lipolysis.

(Test Example 2)
Dry powder of bees obtained by proteolysis following lipid degradation according to Example 1, and proteolysis following lipid degradation according to Example 2, followed by further carbohydrate degradation (β-mannosidase degradation) Performing lipolysis and proteolysis with dried bee powder obtained by comparison, dried bee powder obtained by Comparative Example 1 without any enzymatic degradation, and Comparative Example 3 For each dried bee powder obtained by degrading saccharides, a sample for saccharide analysis was prepared by a conventional method, and a matrix-assisted laser desorption / ionization time-of-flight mass spectrometer (MALDI-TOF-MS: Matrix Assisted Laser Desorption Ionization-Time Of Flight-MS).

  The results are shown in FIG. 6, FIG. 7, FIG. 8, and FIG. FIG. 6 is an MS spectrum of carbohydrates from dried bee powder obtained by performing proteolysis following lipolysis according to Example 1. FIG. 7 is an MS spectrum of a saccharide from dried bee powder obtained in Example 2 by performing proteolysis followed by lipolysis followed by further saccharide degradation. FIG. 8 is an MS spectrum of a saccharide from dried bee powder obtained by Comparative Example 1 without any enzymatic degradation. FIG. 9 is an MS spectrum of carbohydrates from dried bee powder obtained by performing carbohydrate decomposition without performing lipolysis and proteolysis according to Comparative Example 3.

  As shown in FIG. 6 and FIG. 8, a saccharide having a molecular weight of 14700 or more exists before saccharide decomposition by β-mannosidase. On the other hand, as shown in FIG. 7 and FIG. 9, the amount of carbohydrate having a small molecular weight increases after the carbohydrate decomposition by β-mannosidase.

In FIG. 9, carbohydrates are distributed in a range from a molecular weight of about 486 to a molecular weight of about 1200 with a peak at a molecular weight of about 507 as a main peak.
On the other hand, in FIG. 7, the carbohydrate has a peak near the molecular weight 507 as the main peak, but the distribution of the carbohydrate is in the range from the molecular weight 420 to the molecular weight 958, and is present on the smaller molecule side. Yes.
This indicates that the decomposition of the sugar of the honeybee is performed more effectively by proteolysis followed by lipolysis followed by β-mannosidase degradation.

As described above, according to the method for manufacturing a bee-processed food / beverage of the present embodiment, it is possible to first decompose lipids and improve protein degradation efficiency prior to enzymatic degradation of proteins. In addition, bee processing that enables the human body to efficiently absorb each component obtained by degrading carbohydrates following protein degradation and decomposing lipids, proteins, and carbohydrates contained in bees It becomes possible to provide food and drink.
As a result, the following various effects can be obtained more appropriately.

  First, the enzymatic value of a bee kid does not reduce the nutritional value of the protein, so that it can acquire more effects on the protein and increase the nutritional characteristics than a bee kid food that has not been enzymatically decomposed.

  That is, many unexpected polypeptide effects can be obtained in the process of enzymatic degradation. In addition, the resulting polypeptide retains its natural nature and natural attributes, and does not contain any chemical substances. Furthermore, the polypeptide obtained by the enzymatic degradation of the present embodiment has no bitterness or off-flavor and has improved allergenicity.

  Moreover, it is possible to control the molecular weight of the polypeptide contained in the processed processed food for bees, and it is also possible to control the absorption rate of nutrients to the human body.

  The optimal conditions for lipolytic enzymes and proteolytic enzymes are different as described above. Even if these enzymes are mixed and decomposed, the enzymes that match the conditions are activated and both enzymes are appropriately decomposed. Can't do it. As shown in this embodiment, by first performing lipolysis and then proteolysis, the fat formed around the protein in the process of enzymatic degradation is degraded, and the protein and proteolytic enzyme are efficiently separated. It is possible to make it contact, and it is possible to make a peptide smaller.

The present invention is not limited to the above-described embodiments and examples, and it goes without saying that various modifications can be made within the scope of the present invention.
For example, a bee cub such as a wasp, a cross wasp, a wasp, and a wasp can be used. In addition, various enzymes other than those described above can be used as appropriate for the degradation enzyme.

  INDUSTRIAL APPLICABILITY The present invention can be suitably used for the production of bee-processed foods and drinks that efficiently decompose proteins, have high nutritional functions and health and health functions, and are excellent in quality without allergenicity.

(A) Grinding process (B) Inspection process (C) Suspension process (D) (D ') (D ") pH adjustment process (E) Lipid degradation process (F) Proteolysis process (G) Carbohydrate degradation process ( H) Enzyme deactivation process (I) Filtration process (J) Drying process

Claims (9)

  The dried bee powder is pulverized and suspended in water, and a lipid-degrading enzyme is added to decompose the lipid of the bee child. After this step, a proteolytic enzyme is added and the bee child is added. And a process for decomposing the protein.   2. The method for producing a processed food for a bee candy according to claim 1, further comprising a step of degrading the saccharide of the honey bee by adding a saccharide-degrading enzyme after the protein decomposition step. The method for producing a processed food product for bees according to claim 2, wherein β-mannosidase is used as the saccharide-degrading enzyme. The bee honey according to claim 3 , wherein in the step of degrading carbohydrates, the pH of the suspension is adjusted to 5.4 to 7.0, and the β-mannosidase is added to decompose the carbohydrates. The manufacturing method of child processed food and drink. The bee according to any one of claims 2 to 4, further comprising a step of heating a decomposition solution obtained by decomposing the carbohydrate, inactivating the enzyme contained in the decomposition solution, and filtering. Method for manufacturing processed food and drink. In the decomposition process of the lipids, to adjust the pH of the suspension to 6.0 to 11.0, by the addition of lipase according to any one of claims 1 to 5, wherein the decomposing the lipid Manufacturing method of processed food and drink for bees. The method for producing a processed food or drink for bees according to any one of claims 1 to 6, wherein the bee is a male bee. The method for producing a processed food product for bees according to claim 7, wherein the bees are male pupae 20 to 23 days old. A bee processed food or drink manufactured by the method for manufacturing a bee processed food or drink according to any one of claims 1 to 8 .