Food browning agents

Abstract

The present invention addresses the problem of providing a food-product browning agent with which it is possible to brown a food product in a step for heating and cooking the food product. The present invention provides: a food-product browning agent containing glycosidase, polyphenol oxidase, or cellulase; a food product containing the aforementioned food-product browning agent; and a food-product browning method including heating a food product after adding glycosidase, polyphenol oxidase, or cellulase thereto.

Description

Technical Field

[0001] The present invention relates to a food browning agent containing polyphenol oxidase, glycosidase or cellulase.

Background Art

[0002] In recent years, due to social issues such as food loss, reduction of environmental load, and response to diverse consumer needs, alternative meat products using plants such as soybeans and peas as raw materials have attracted worldwide attention. As a method for reproducing the blood color of alternative meat, a method of adding soy legume hemoglobin (hereinafter referred to as soy leghemoglobin) to alternative meat and a method of adding beet pigment are known.

[0003] The method using beet pigment has a long history of food experience worldwide for the raw material beet and is easily accepted by consumers. However, beet pigment is red and is required to change to brown after cooking. Although beet pigment is known to fade by heat, it does not fade sufficiently during the heat cooking process, so browning with another browning agent is not sufficient.

[0004] Patent Document 1 discloses that in a food for meat, the color of uncooked meat (the red color of beet pigment) is changed to brown by an agent released by heat treatment. Specifically, in the examples of Patent Document 1, a browning agent is bound to an inert yeast cell wall material, this is added to food, and by heat cooking, the browning agent is released from the yeast cell wall material and browned.

[0005] Non-Patent Document 1 describes that red beet has a plurality of endogenous enzymes such as β-glucosidase, polyphenol oxidase and peroxidase, and if these endogenous enzymes are not appropriately inactivated, they may cause fading (lines 12 from the bottom to 9 from the bottom in the right column on page 2368).

[0006] Patent Document 2 states that enzymatic discoloration and browning of food is said to be due to the oxidation and polymerization of pigments by the action of polyphenol oxidase, forming brown melanin pigment, and that methods to partially prevent this are used, such as heating (blanching) and inactivation of the enzyme by enzyme inhibitors (paragraph 0007). [Prior art documents] [Patent Documents]

[0007] [Patent Document 1] Special Publication No. 2018-533945 [Patent Document 2] Japanese Patent Publication No. 2001-294768 [Non-patent literature]

[0008] [Non-Patent Document 1] International Journal of Food Science and Technology 2009, 44, 2365-2376 [Overview of the Initiative] [Problems that the invention aims to solve]

[0009] It is known that polyphenol oxidases, including laccase, and β-glucosidase, a type of glycosidase, cause discoloration of beet pigment, but it is not known that cellulase causes discoloration of beet pigment. Furthermore, it is not known that adding laccase, glycosidase, or cellulase to food causes browning of the food during the cooking process.

[0010] The problem to be solved by this invention is to provide a food browning agent that can brown food during the cooking process. [Means for solving the problem]

[0011] As a result of diligent research to solve the above problems, the inventors of this invention have found that the beet pigment can be faded by adding laccase, glycosidase, or cellulase to a substitute meat containing beet pigment and then heating it. This invention was completed based on these findings.

[0012] The present invention provides the following: <1> A food browning agent containing glycosidase, polyphenol oxidase, or cellulase. <2> The food is a meat substitute. <1> A browning agent for the foods listed. <3> It causes food to brown when heated after being added to it. <1> or <2> A browning agent for the foods listed. <4> <1> Foods containing browning agents as described above. <5> A method for browning food, comprising adding polyphenol oxidase, glycosidase, or cellulase to the food and heating it. Use of glycosidase, polyphenol oxidase, or cellulase for the manufacture of food browning agents. Glycosidase, polyphenol oxidase, or cellulase for use in browning food. [Effects of the Invention]

[0013] According to the food browning agent of the present invention, food can be browned during the cooking process. [Brief explanation of the drawing]

[0014] [Figure 1] Figure 1 shows the change in the absorption spectrum accompanying the enzymatic browning of a beet solution by glycosidase, cellulase, and polyphenol oxidase. [Figure 2] Figure 2 shows the change in the appearance of a mock pate by enzymatic treatment.

Mode for Carrying Out the Invention

[0015] Hereinafter, embodiments of the present invention will be described in detail. The browning agent for foods of the present invention contains glycosidase, polyphenol oxidase, or cellulase.

[0016] Glycosidase is a general term for enzymes that cleave the glycosidic bonds of glycosides and saccharides, and includes diglycosidase and monoglycosidase depending on the number of sugar residues to be cleaved. In addition, depending on the type of bond of the sugar residues to be cleaved, β-galactosidase, α-glucosidase, β-glucosidase, etc. are included. β-Glucosidase is a general term for enzymes that catalyze the reaction of hydrolyzing the β-D-glucopyranoside bond of sugars. The origin of β-glucosidase is not particularly limited, and examples include those derived from microorganisms such as bacteria or filamentous fungi, plants, and animals. Examples of microorganisms include Asperugillus niger, Trichoderma reesei, Trichoderma viride, Penicillium multicolor, etc., and examples of plants include almonds, etc. Commercially available β-glucosidases include aromase (trade name; manufactured by Amano Enzyme Co., Ltd.) (aromase H2), Sumiteam BGA (trade name; manufactured by Shin Nippon Chemical Industry Co., Ltd.), SPEZYME Cp (trade name; manufactured by Genencor Kyowa Co., Ltd.), naringinase (trade name; manufactured by Tanabe Mitsubishi Pharma Co., Ltd.), Y-NC (trade name; manufactured by Yakult Pharmaceutical Industry Co., Ltd.), etc., and these can be used in the present invention.

[0017] Polyphenol oxidases are enzymes that promote the formation of polyphenol oxidized states, and specific examples include laccase. Laccase is a type of multi-copper protein and is an oxidase with low substrate specificity that also acts on catechols, hydroquinones, aminophenols, and phenylenediamines. Examples of such laccases include those derived from plants such as lacquer trees, and microorganisms such as bacteria and fungi. Examples of laccases derived from microorganisms include enzymes from the genera Aspergillus, Neurospora, Podospora, Botrytis, Collybia, Fomes, Lentinus, Pleurotus, Pycnoporus, Pyricularia, Trametes, Rhizoctonia, Rigidoporus, Coprinus, Psatyrella, Myceliophtera, Schtalidium, Polyporus, Phlebia, and Coriolus. Among the above, laccases derived from organisms belonging to the genus Trametes are preferred. Examples of laccase include laccase Y120 (derived from Trametes sp.; manufactured by Amano Enzyme Co., Ltd.) and laccase (derived from Trametes versicolor; manufactured by SIGMA-ALDRICH).

[0018] Cellulase is an enzyme that hydrolyzes the glucoside bond of β-1,4 glucan. The cellulase to be used is not particularly limited. For example, cellulase derived from microorganisms can be used. Examples of cellulase derived from microorganisms include cellulase derived from Trichoderma microorganisms (e.g., manufactured by Meiji Seika Pharma Co., Ltd., Novozymes A / S, Genencor International, Inc., Amano Enzyme Inc.), cellulase derived from Aspergillus microorganisms (e.g., manufactured by HBI Inc., Amano Enzyme Inc.), cellulase derived from Acremonium microorganisms (e.g., manufactured by Meiji Seika Pharma Co., Ltd.), etc. It is possible to use not only natural (wild-type) cellulase but also recombinant cellulase. Also, two or more kinds of cellulase may be used in combination. It is possible to use commercially available cellulase or cellulase preparations. Examples of commercially available cellulase or cellulase preparations include Accellerase (manufactured by Genencor International, Inc.), NS22074 (manufactured by Novozymes A / S), Meicelase, Acremozym (manufactured by Meiji Seika Pharma Co., Ltd.), Celluclast AC (manufactured by HBI Inc.), Cellulase A "Amano" 3, Cellulase T "Amano" 4 (manufactured by Amano Enzyme Inc.).

[0019] In the present invention, two or more of the enzymes among glycosidase, polyphenol oxidase, and cellulase may be used in combination.

[0020] The browning agent for the food of the present invention contains at least glycosidase, polyphenol oxidase or cellulase, but in addition to the above, it may also contain excipients, buffers, suspending agents, stabilizers, pH adjusters, preservatives, antiseptics, fragrances, thickeners, oils and fats, brighteners, binders, binder reinforcing agents, emulsion stabilizers, physiological saline, etc.

[0021] Excipients that can be used include maltose, trehalose, lactose, D-glucose, sorbitol, D-mannitol, sucrose, glycerol, etc. Buffering agents that can be used include phosphates, citrates, acetates, etc. Stabilizers that can be used include propylene glycol, ascorbic acid, etc. pH adjusters that can be used include organic acids or organic acid salts such as itaconic acid, succinic acid, tartaric acid, fumaric acid, citric acid, malic acid, adipic acid, gluconic acid, pyrophosphate, acetic acid, lactic acid, α-ketoglutaric acid, phytic acid; inorganic acids or inorganic acid salts such as carbonic acid; acidic amino acids such as aspartic acid and glutamic acid; basic amino acids such as arginine, lysine, and histidine, etc. Preservatives that can be used include phenol, benzalkonium chloride, benzyl alcohol, chlorobutanol, methylparaben, etc. Antimicrobial agents that can be used include ethanol, benzalkonium chloride, parahydroxybenzoic acid, chlorobutanol, etc. The fragrances include animal-derived fragrances such as musk, civet, castoreum, and ambergris; anise essential oil, angelica essential oil, ylang-ylang essential oil, iris essential oil, fennel essential oil, orange essential oil, cananga essential oil, carawé essential oil, cardamom essential oil, guaiac wood essential oil, cumin essential oil, black spicebush essential oil, cinnamon essential oil, geranium essential oil, copaiba balsam essential oil, coriander essential oil, perilla essential oil, cedarwood essential oil, citronella essential oil, jasmine essential oil, gingergrass essential oil, cedar essential oil, spearmint essential oil, and Western herb. Plant-derived fragrances such as kale essential oil, star anise essential oil, tuberose essential oil, clove essential oil, orange blossom essential oil, wintergreen essential oil, true balsam essential oil, patchouli essential oil, rose essential oil, palmarosa essential oil, cypress essential oil, hinoki essential oil, sandalwood essential oil, petitgrain essential oil, bay essential oil, vetiver essential oil, bergamot essential oil, Peruvian balsam essential oil, bois de rose essential oil, camphor essential oil, mandarin essential oil, eucalyptus essential oil, lime essential oil, lavender essential oil, linaloe essential oil, lemongrass essential oil, lemon essential oil, rosemary essential oil, Japanese peppermint essential oil, etc.; other synthetic fragrances may be used.Examples of oils and fats that can be used include avocado oil, linseed oil, almond oil, fennel oil, perilla oil, olive oil, orange oil, orange raspberry oil, cocoa butter, chamomile oil, carrot oil, cucumber oil, coconut oil, sesame oil, rice oil, safflower oil, shea butter, liquid shea butter, soybean oil, camellia oil, corn oil, rapeseed oil, peach kernel oil, castor oil, sunflower oil, grape seed oil, cottonseed oil, peanut oil, turtle oil, mink oil, egg yolk oil, palm oil, palm kernel oil, Japanese wax, coconut oil, beef tallow, and lard. In addition, oils and fats that have been modified by hydrogenation, fractionation, transesterification, etc., can also be used. As a glazing agent, waxes such as beeswax, carnauba wax, whale wax, lanolin, liquid lanolin, reduced lanolin, hard lanolin, candelilla wax, montan wax, shellac wax, rice wax, squalene, squalane, and pristane (regardless of whether they are plant or animal-derived); and mineral oils such as liquid paraffin, petrolatum, paraffin, ozokeride, ceresin, and microcrystalline wax can be used. As a binding agent, soy protein, egg protein, milk protein, blood protein, casein, and transglutaminase can be used. As a binding reinforcer, polyphosphates can be used. As an emulsifying stabilizer, sodium caseinate can be used. Other additives may include natural fatty acids such as lauric acid, myristic acid, palmitic acid, stearic acid, behenic acid, oleic acid, linoleic acid, linolenic acid, docosahexaenoic acid, eicosapentaenoic acid, 1 / 2-hydroxystearic acid, undecylenic acid, tall oil, and lanolin fatty acid; and synthetic fatty acids such as isononanoic acid, caproic acid, 2-ethylbutanoic acid, isopentanoic acid, 2-methylpentanoic acid, 2-ethylhexanoic acid, and isopentanoic acid.

[0022] When the food browning agent of the present invention is a mixture as described above, the content of polyphenol oxidase, glycosidase, or cellulase in the mixture is not particularly limited as long as it is within a range in which the effect can be exerted, but for example it is 0.1% by weight or more of the total mixture, preferably 1% by weight or more, more preferably 5% by weight or more, and even more preferably 10% by weight or more.

[0023] The food browning agent of the present invention can brown food when added to food and heated.

[0024] Methods for adding the food browning agent of the present invention to food generally include, but are not limited to, a method of injecting a suspension containing the food browning agent into the food and tumbling it, a method of immersing the food in a immersion solution containing the food browning agent, and a method of mixing the suspension containing the food browning agent with the food. The temperature when adding the food browning agent of the present invention to food is not particularly limited, but is generally 4°C to 40°C, preferably 4°C to 30°C, more preferably 4°C to 25°C, and most preferably 4°C to 20°C.

[0025] When adding the food browning agent of the present invention to food, the contact time between the food browning agent and the food is, for example, 10 minutes to 4 days, preferably 1 hour to 3 days, more preferably 3 hours to 2 days, and even more preferably 6 hours to 2 days. However, if the contact state is maintained during subsequent processing steps, the next processing step may be performed immediately after operations such as injection or mixing. Furthermore, if the food is stored under conditions where the browning agent does not act (such as low temperature), the contact time may be extended.

[0026] The amount of the food browning agent of the present invention added to food is not particularly limited, but is, for example, 0.001% to 10% by weight, preferably 0.01 to 2.0% by weight, more preferably 0.02 to 1.0% by weight, and even more preferably 0.05 to 0.5% by weight, as the mass of the enzyme relative to the mass of the food. The activity of the enzyme contained in the browning agent added to food is not particularly limited, but in the case of polyphenol oxidase, is, for example, 1 to 10000 U, preferably 2 to 1000 U, more preferably 5 to 500 U, and even more preferably 10 to 200 U, as the amount of enzyme activity per 1 g of food. In the case of glycosidase, is, for example, 0.01 U to 1000 U, preferably 0.05 to 100 U, more preferably 0.1 to 50 U, and even more preferably 0.5 to 10 U, as the amount of β-glucosidase activity per 1 g of food. In the case of cellulase, the enzyme activity per gram of food mass is, for example, 0.001 U to 300 U, preferably 0.003 to 30 U, more preferably 0.01 to 15 U, and even more preferably 0.03 to 6 U. The activity of the enzyme contained in the browning agent added to the food is not particularly limited, but in the case of polyphenol oxidase, the enzyme activity per gram of beet mass is, for example, 10 to 100,000 U, preferably 20 to 50,000 U, more preferably 50 to 30,000 U, and even more preferably 100 to 20,000 U. In the case of glycosidase, the β-glucosidase activity per gram of food mass is, for example, 0.2 U to 10,000 U, preferably 0.5 to 5,000 U, more preferably 1 to 3,000 U, and even more preferably 5 to 2,000 U. In the case of cellulase, the enzyme activity per gram of food mass is, for example, 0.05 U to 500 U, preferably 0.1 to 200 U, more preferably 0.3 to 100 U, and even more preferably 0.5 to 50 U.

[0027] Polyphenol oxidase activity can be measured by the following method. 1 mL of phenol reagent (0.25 mol / L) was placed in a glass cell, and 1 mL of 4-aminoantipyrine reagent (0.009 mol / L) and 0.5 mL of polyphenol oxidase activity test buffer were added and mixed. After heating at 30°C for 10 minutes, 0.5 mL of the sample solution, which had been preheated to 30°C, was added and mixed. The absorbance at a wavelength of 505 nm was measured 10 seconds and 40 seconds after the addition of the sample solution, and the change in absorbance at a wavelength of 505 nm over 30 seconds was determined. When the absorbance increased by 0.1 per minute, the amount of enzyme contained in 1 mL of the reaction solution was defined as 1 unit (1 U).

[0028] β-glucosidase activity can be measured by the following method. Weigh out 0.50 g of D(-)-salicin, dissolve it in water, and make 50 mL of solution to prepare the substrate solution. Measure 3 mL of pH 4.0 acetate buffer (0.1 mol / L) into a 50 mL Nessler tube, add 1 mL of the substrate solution, and heat at 40°C for 10 minutes. Then add 1 mL of the sample solution and immediately shake well, and heat at 40°C for 30 minutes. Add 2 mL of Somogyi reagent (I) to this solution and shake well. Lightly cap the mouth of the Nessler tube and heat in a water bath for 20 minutes. After cooling, add 1 mL of Nelson reagent to this solution and shake well until the red precipitate of cuprous oxide is completely dissolved. Let stand at room temperature for about 20 minutes, then add water to make 25 mL of solution to prepare the test solution. Separately, measure 3 mL of pH 4.0 acetate buffer (0.1 mol / L) into a 50 mL Nessler tube, add 1 mL of substrate solution, add 2 mL of Somogyi reagent (I), shake well, then add 1 mL of sample solution, lightly cap the mouth of the Nessler tube, heat in a water bath for 20 minutes, and then prepare the comparison solution by following the same procedure as for the test solution. Measure the absorbance of the test solution and the comparison solution at a wavelength of 500 nm. Create calibration curves using glucose solutions of 0.10, 0.15, 0.20, 0.25, and 0.30 mg / 5 mL. Under these conditions, the amount of enzyme that produces reducing sugar equivalent to 1 mg of glucose per minute is set to 100 units and calculated using the following formula. β-glucosidase strength (U / g) = ((A1-A2)-b) / a×1 / 30×100×n A1: Absorbance of the test solution at a wavelength of 500 nm A2: Absorbance of the comparison solution at a wavelength of 500 nm 1 / 30: Conversion factor to per minute Conversion factor to 100:100 units a: Slope of the glucose calibration curve b: Intersection of the glucose calibration curve n: Dilution factor per 1g of sample

[0029] Cellulase activity can be measured by the following method. Weigh 0.67 g of sodium carboxymethylcellulose, add 50 mL of water, and heat to dissolve. After cooling, add 10 mL of pH 5.0 acetate buffer (1 mol / L), and add water to make a total volume of 100 mL to prepare the substrate solution. Weigh 4 mL of the substrate solution, heat at 37°C for 10 minutes, then add 1 mL of the sample solution and immediately shake well. Heat at 37°C for 30 minutes, add 2 mL of Somogyi's Reagent (I) and mix, then heat in a water bath for 30 minutes. After cooling, add 2 mL of Nelson's Reagent to this solution and shake well. Add 3 mL of sodium hydroxide solution (0.5 mol / L) and shake to dissolve the precipitate. Let stand for 20 minutes, then add pH 4.5 acetate buffer (1 mol / L) to make a total volume of 25 mL. Weigh 1 mL of this solution, add 9 mL of pH 4.5 acetate buffer (1 mol / L) and mix to prepare the test solution. Separately, measure out 1 mL of sample solution, add 2 mL of Somogyi Reagent (I) and shake, then add 4 mL of substrate solution and mix, and heat in a water bath for 30 minutes. After cooling, prepare the comparison solution in the same manner as the preparation of the test solution. If the test solution and comparison solution are turbid, centrifuge and measure the supernatant. Measure the absorbance of the test solution and comparison solution at a wavelength of 750 nm with water as the control. Create calibration curves using glucose solutions of 0.10, 0.20, 0.30, 0.40, and 0.50 mg / mL. Under these conditions, the amount of enzyme that produces an increase in reducing power equivalent to 1 μmol of glucose per minute is defined as 1 unit and calculated using the following formula. Fiber saccharification capacity (U / g) = (A1-A2) / a × 1 / 30 × 1 / 0.180 × n A1: Absorbance of the test solution at a wavelength of 750 nm A2: Absorbance of the comparison solution at a wavelength of 750 nm 1 / 30: Conversion factor to per minute 1 / 0.180: 1 μmol of glucose = 0.180 mg a: Slope of the glucose calibration curve n: Dilution factor per gram of sample

[0030] The food used in this invention is not particularly limited as long as it is a food that undergoes heat treatment, but it is preferably a food that contains beet dye. For example, alternative meat containing beet dye can be used. Alternative meat is a food that does not use animal meat such as pork, beef, or chicken, but instead uses, for example, plant-derived protein (plant protein material). Specific examples of alternative meat include hamburgers, meatballs, patties, meatloaf, minced cutlets, and pâté.

[0031] The form of the plant protein material is not particularly limited and may be in powder or textured form. Textured plant protein material is well known as a material for meat substitutes (meat substitutes), and a typical example is a material that is textured to resemble meat by extruding a raw material mixture containing plant protein and water using an extruder, and then drying or freezing it. The type of plant protein material is not particularly limited, but examples include proteins from cereals such as soybeans, broad beans, peas, chickpeas, mung beans, lupin beans, and kidney beans; proteins from grains such as barley, rice, wheat, rye, oats, buckwheat, millet, foxtail millet, teff, quinoa, and corn; proteins from nuts such as hemp seeds (industrial hemp), canary seeds, flaxseed, almonds, cashews, hazelnuts, pecans, macadamia nuts, pistachios, walnuts, Brazil nuts, peanuts, coconuts, pili nuts, chestnuts, sesame seeds, and pine nuts; and proteins from algae.

[0032] In addition to plant-based proteins, insect proteins (such as those derived from crickets) and microbial proteins (such as those derived from yeast, filamentous fungi, and mushrooms) can also be used as ingredients for meat substitutes.

[0033] The pigments contained in the food are not particularly limited as long as they achieve the browning of the food. For example, they may contain a predetermined pigment compound as an ingredient. The predetermined pigment compound is selected from the group consisting of betalains, anthocyanins, curcuminoids, polyhydroxychalcones, and polyhydroxyanthraquinones. The pigments may be derived from plants such as beets (Beta vulgaris ssp. vulgaris var. Vulgaris, also known as table beet, red beet, or beetroot), red radish, purple sweet potato, red perilla, purple cabbage, safflower, and turmeric; or from organisms such as insects. More specifically, examples of pigments include beet pigment (containing betacyanin and betaxanthin as betalains), red radish pigment (containing pelargonidin and cyanidin as anthocyanins), purple sweet potato pigment (containing cyanidin and peonidin as anthocyanins), red perilla pigment (containing shisonin and malonylsisonin as anthocyanins), purple cabbage pigment (containing rubrobrasin as anthocyanin), safflower pigment (containing saflamine and carthamine as polyhydroxychalcones), turmeric pigment (containing curcumin as a curcuminoid), and cochineal pigment (containing carminic acid as a polyhydroxyanthraquinone). Beet pigment is preferred. In addition, plant protein materials containing pigments can be used as protein materials for food, but from the viewpoint of controlling the degree of browning, it is preferable to add pigments separately from the plant protein material.

[0034] The heat treatment is not particularly limited in terms of the means used, as long as it achieves the browning of the food. It may be heated on a frying pan, or internally heated using microwave heating (microwave oven) or far-infrared heating, or externally heated using dry heating with a dry heat oven or wet heating with a steam oven.

[0035] The temperature and time of the heat treatment are not particularly limited, as long as browning of the food is achieved. Generally, browning of the food can be achieved by heating from a temperature ranging from refrigeration temperature to room temperature to a temperature exceeding the temperature range in which the enzyme acts. For example, when using an oven, the temperature is 170°C to 250°C, preferably 180°C to 230°C, and more preferably 190°C to 220°C. The internal temperature of the food at the end of the heat treatment is not particularly limited, as long as browning of the food is achieved, but for example, it is 60°C to 100°C. From the viewpoint of deactivating the enzyme used, the temperature is preferably 70°C to 100°C, and more preferably 80°C to 90°C. The heating time is generally 1 to 60 minutes, preferably 1 to 30 minutes, and more preferably 1 to 15 minutes.

[0036] The present invention will be specifically described by the following examples, but the present invention is not limited to these examples. [Examples]

[0037] Example 1: Confirmation of browning effect by β-glucosidase, cellulase, and polyphenol oxidase <Method> Beet powder (commercially available: Kumamoto-produced beet powder (Kyushu Veggie & Fruit)) was dissolved in 100 mM sodium acetate buffer (pH 5.0) to prepare a 1% by mass beet solution. To the above 1% by mass beet solution, β-glucosidase (alomase H2, hereafter GLYH-2) (Amano Enzyme Co., Ltd.), cellulase (cellulase T "Amano" 4, hereafter CT-4) (Amano Enzyme Co., Ltd.), or polyphenol oxidase (laccase Y120, hereafter LC-Y120) (Amano Enzyme Co., Ltd.) was added in the activity amounts listed in Table 1 below. The above mixture was reacted at 60°C for 1 hour under conditions of 100 rpm. The color change of the mixture after the reaction was visually confirmed, and the absorbance in the visible light range (380~780 nm) was measured.

[0038] <Result> The results are shown in Table 1 and Figure 1. Based on the results in Table 1 and Figure 1, browning was observed at GLYH-2 (β-glucosidase) levels of 1.2U or higher, CT-4 (cellulase) levels of 0.3U or higher, and LC-Y120 (polyphenol oxidase) levels of 120U or higher.

[0039] [Table 1]

[0040] Example 2: Confirmation of the browning effect of other enzyme preparations <Method> A 1% by mass beet solution was prepared using commercially available beet powder (Kumamoto-produced beet powder (Kyushu Veggie & Fruit)) and dispensed into 4.5 mL test tubes. The 1% by mass beet solutions in the test tubes were cooled, and 0.5 mL each of the enzyme solution (10 mg / 1 mL) (0.1% by mass enzyme solution) was added. The mixtures were reacted at 40°C for 30 minutes, and then the absorbance at 480 nm and 538 nm was measured.

[0041] <Result> The results are shown in Table 2.

[0042] [Table 2]

[0043] <Consideration> The pigments present in beets are betalains (nitrogen pigments). Two types of betalains exist. The absorption maximum wavelengths for betaxanthin and betacyanin are 480 nm and 538 nm, respectively, and these wavelengths were measured. In this study, the degradation tendency of betacyanin, a red pigment, by cellulase and polyphenol oxidase was confirmed.

[0044] The results from Examples 1 and 2 confirmed that GLYH-2 (β-glucosidase), LC-Y120 (polyphenol oxidase), and CT-4 (cellulase) had a browning effect.

[0045] Example 3: Confirmation of the browning effect of a pseudo-putty using pea protein. <Method> The following ingredients were mixed to create a simulated putty (pH 5.0), which was then cooled to an internal temperature of 4-10°C. Next, each enzyme was added to the putty according to the activity levels shown in the table below per gram of putty weight, and the mixture was thoroughly kneaded. After that, both sides were cooked in a preheated oven at 200°C for 7 minutes per side. The internal temperature of the simulated putty immediately after cooking was confirmed to be 80-90°C using a thermometer.

[0046] The cross-sectional color of the pseudo-putty was measured using a spectrophotometer (CM-700d, Konica Minolta Sensing Co., Ltd.) and evaluated using the L*a*b* color system. The L* axis represents brightness, with values ​​closer to 100 indicating a color closer to white. The a* axis represents the range from green to red, with higher values ​​indicating a stronger red color. The b* axis represents the range from blue to yellow, with higher values ​​indicating a stronger yellow color.

[0047] [Table 3]

[0048] <Result> The results are shown in Figure 2 and Table 4.

[0049] [Table 4]

[0050] Visual inspection confirmed that the artificial putty turned brown due to enzyme addition under all conditions. Furthermore, from the spectrophotometer measurement results, a*( red While the light reflectance of the color system increased, b*( yellow A decrease in the light reflectance (of the color system) was observed, suggesting that the beet pigment was turning brown.

[0051] The enzyme activity (per gram of pseudo-putty) that was capable of browning the pseudo-putty was 1.2 U or higher for GLYH-2 (β-glucosidase), 0.03 U for CT-4 (cellulase), and 1.2 U or higher for LC-Y120 (polyphenol oxidase).

[0052] Considering that the usual method involves heating to 70°C or higher (blanching) to prevent enzymatic browning, the fact that browning can be achieved through cooking, as shown in Example 3, is an unexpected effect. [Industrial applicability]

[0053] According to this invention, since food can be browned by heating, it is possible to provide a high-value alternative meat product.

Claims

1. A food browning agent containing laccase or cellulase, A food browning agent that contains betalain in the aforementioned food.

2. A food browning agent according to claim 1, wherein the food is a meat substitute.

3. A food browning agent according to claim 1 or 2, which browns food when heated after being added to food.

4. A food containing the browning agent for food according to claim 1.

5. This includes adding laccase or cellulase to food and heating it. A method for browning a food product, wherein the food product contains betalains.

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