Classifications

• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
  • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
  • C12N9/14—Hydrolases (3)
  • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
  • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
  • C12N9/2468—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1) acting on beta-galactose-glycoside bonds, e.g. carrageenases (3.2.1.83; 3.2.1.157); beta-agarase (3.2.1.81)
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; PREPARATION THEREOF
  • A23C9/00—Milk preparations; Milk powder or milk powder preparations
  • A23C9/12—Fermented milk preparations; Treatment using microorganisms or enzymes
  • A23C9/1203—Addition of, or treatment with, enzymes or microorganisms other than lactobacteriaceae
  • A23C9/1206—Lactose hydrolysing enzymes, e.g. lactase, beta-galactosidase
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
  • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
  • C12N9/14—Hydrolases (3)
  • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
  • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
  • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
  • C12N9/14—Hydrolases (3)
  • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
  • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
  • C12N9/2468—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1) acting on beta-galactose-glycoside bonds, e.g. carrageenases (3.2.1.83; 3.2.1.157); beta-agarase (3.2.1.81)
  • C12N9/2471—Beta-galactosidase (3.2.1.23), i.e. exo-(1-->4)-beta-D-galactanase
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
  • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
  • C12N9/96—Stabilising an enzyme by forming an adduct or a composition; Forming enzyme conjugates
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12Y—ENZYMES
  • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
  • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
  • C12Y302/01023—Beta-galactosidase (3.2.1.23), i.e. exo-(1-->4)-beta-D-galactanase
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12Y—ENZYMES
  • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
  • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
  • C12Y302/01108—Lactase (3.2.1.108)
• • Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
  • Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
  • Y02P—CLIMATE CHANGE MITIGATION TECHNOLOGIES IN THE PRODUCTION OR PROCESSING OF GOODS
  • Y02P60/00—Technologies relating to agriculture, livestock or agroalimentary industries
  • Y02P60/80—Food processing, e.g. use of renewable energies or variable speed drives in handling, conveying or stacking
  • Y02P60/87—Re-use of by-products of food processing for fodder production

Definitions

• the present invention relates to a lactase solution that improves filter clogging.
• Lactose intolerance is a condition in which lactose ingestion causes various symptoms such as abdominal pain and diarrhea. The reason for this is that the body cannot properly decompose lactose. In the food manufacturing industry, lactose is used to decompose lactose contained in milk or the like into galactose and glucose.
• a lactase solution can be used to decompose the lactose contained in milk, etc.
• a lactase solution is produced by culturing a lactase-producing microorganism and removing contaminants derived from the culture.
• the lactase solution contains less protease, which is a contaminating enzyme.
• Methods for reducing the amount of protease contained in a lactase solution include, for example, a method of thermally inactivating protease (for example, Patent Document 1) and a method of selectively adsorbing protease with an ion-exchange resin (for example, Patent Document 2).
• Arylsulfatase is known as a contaminant enzyme other than protease contained in a lactase solution (eg, Patent Document 3). Arylsulfatase tends to develop off-flavours over time when added to milk.
• An object of the present invention is to provide a lactase solution having good permeability of a filtration filter.
• An object of the present invention is to provide a lactase solution having good filter permeability and good residual lactase activity.
• An object of the present invention is to provide a lactase solution having good filter permeability and lactase residual activity even when a lactase solution with low protease activity and arylsulfatase activity, which are contaminating enzymes, is used.
• the present invention solves the problems of the present invention by having the following technical configuration.
• the (i) unsaturated fatty acid is at least one selected from oleic acid, vaccenic acid, linoleic acid, linolenic acid, eleostearic acid, mead acid, arachidonic acid, and nervonic acid. Lactase solution as described.
• a lactase solution having good filter permeability According to the present invention, it is possible to provide a lactase solution with good filter permeability and good residual lactase activity. According to the present invention, even when a lactase solution with low protease activity and arylsulfatase activity, which are contaminating enzymes, is used, it is possible to provide a lactase solution with good filter permeability and lactase residual activity.
• lactase solution of the present invention contains any one of the following (i) to (iii). (i) 0.0001 to 0.1% by mass of unsaturated fatty acid or a salt thereof (ii) 0.0001 to 0.1% by mass of saturated fatty acid salt (iii) 0.01 to 10% by mass of at least one selected from yeast extract, soybean peptone, pea protein or corn steep liquor
• a lactase solution having good filter permeability can be provided.
• An unsaturated fatty acid salt can be obtained by adding a base to an unsaturated fatty acid.
• a base for example, a hydroxide of an alkali metal salt can be used, and specifically sodium hydroxide or potassium hydroxide can be used.
• the unsaturated fatty acid salt it is preferable to use one having excellent dispersibility and solubility in the lactase solution, and it is preferable to use unsaturated fatty acid sodium or unsaturated fatty acid potassium.
• the unsaturated fatty acid salt may be added directly to the lactase solution. Both unsaturated fatty acids and unsaturated fatty acid salts improve the permeability of filtration filters for lactase solutions. It is believed that the unsaturated fatty acids dispersed or dissolved in the lactase solution have some effect. It is presumed that this unsaturated fatty acid masks the factor that deteriorates the permeability of the filtration filter.
• Unsaturated fatty acids are so-called oils and it was surprising that they improve the permeability of filtration filters for lactase solutions. Both unsaturated fatty acids and unsaturated fatty acid salts can provide lactase solutions with good residual lactase activity.
• the unsaturated fatty acid or unsaturated fatty acid salt contained in the lactase solution is preferably 0.0001 to 0.1% by mass, more preferably in the range of 0.0005 to 0.05% by mass. It is more preferably in the range of 0.001 to 0.01 mass %, particularly preferably in the range of 0.005 to 0.01 mass %.
• unsaturated fatty acids examples include oleic acid, vaccenic acid, linoleic acid, linolenic acid, eleostearic acid, mead acid, arachidonic acid, and nervonic acid. These may be used singly or in combination. Among these, it is preferable to use unsaturated fatty acids having 18 carbon atoms. Excellent in filter permeability and storage stability of lactase activity.
• the number of unsaturated bonds that constitute the unsaturated fatty acid is not particularly limited. Equivalent effects can be obtained regardless of the number of unsaturated bonds. The number of unsaturated bonds can be selected from, for example, 1-6, 1-3 or 1-2.
• a mixture of unsaturated fatty acids and saturated fatty acids may be used, or oils derived from natural products containing a plurality of these may be used.
• oils derived from natural products for example, soybean oil, corn oil, rice oil, rapeseed oil, sunflower oil and the like can be used.
• unsaturated fatty acid When unsaturated fatty acid is added directly to the lactase solution, it tends to become cloudy.
• unsaturated fatty acid it is preferable to add the unsaturated fatty acid to the lactase solution after dispersing it in a dispersant.
• Glycerin or ethanol can be used as a dispersing agent for dispersing the unsaturated fatty acid.
• the amount of the dispersant added is preferably 1 to 100,000 parts by weight per 1 part by weight of the unsaturated fatty acid.
• the unsaturated fatty acid need not be dissolved in the dispersant and may be cloudy. After the unsaturated fatty acid is dispersed in the dispersant, it may be mixed with the lactase solution to cause turbidity in the lactase solution.
• glycerin is used as a dispersant, it is preferably in the range of 100 to 10,000 parts by mass, more preferably in the range of 1,000 to 5,000 parts by mass, relative to 1 part by mass of unsaturated fatty acid.
• When ethanol is used as a dispersant it is preferably in the range of 5 to 1,000 parts by mass, more preferably in the range of 10 to 500 parts by mass, per 1 part by mass of the unsaturated fatty acid.
• the saturated fatty acid may be solid at room temperature. Addition of solid saturated fatty acid to the lactase solution hardly dissolves it and cannot improve the permeability of the filtration filter. Rather, the permeability of the filtration filter deteriorates.
• a saturated fatty acid salt can be obtained by adding a base to a saturated fatty acid and reacting it. As this base, the same bases as those mentioned above for unsaturated fatty acids can be used. Addition of a saturated fatty acid salt to the lactase solution can improve the permeability of the filtration filter. Saturated fatty acids dispersed or dissolved in the lactase solution are considered to have some effect. It is presumed that this saturated fatty acid masks the factor that deteriorates the permeability of the filtration filter. Saturated fatty acids are so-called oils and it was surprising that they improve the permeability of filtration filters for lactase solutions.
• the unsaturated fatty acid salt contained in the lactase solution is preferably 0.0001 to 0.1% by mass, more preferably 0.0005 to 0.05% by mass, and more preferably 0.001 to 0.05% by mass. It is more preferably in the range of 0.01% by weight, particularly preferably in the range of 0.005 to 0.01% by weight.
• saturated fatty acids examples include butyric acid, valeric acid, caproic acid, enanthic acid, caprylic acid, pelargonic acid, capric acid, lauric acid, myristic acid, pentadecyl acid, palmitic acid, margaric acid, stearic acid, arachidic acid, and behenic acid. , lignoceric acid, cerotic acid, montanic acid, melissic acid and the like can be used. These may be used singly or in combination.
• the saturated fatty acid preferably has 8 to 20 carbon atoms, more preferably 10 to 16 carbon atoms, and even more preferably 12 to 14 carbon atoms.
• the permeability of the filtration filter can be further increased by setting the number of carbon atoms of the saturated fatty acids to 8 or more.
• the solubility of the saturated fatty acid can be sufficiently ensured, and the permeability of the filtration filter can be further increased.
• yeast extract etc.
• yeast extract soy peptone, pea protein, casein hydrolyzate or corn steep liquor
• pea protein a protein
• casein hydrolyzate a protein
• corn steep liquor may be used as is or may be subjected to some treatment to increase the proportion required.
• an amino acid alone or a tripeptide was added to the lactase solution, no effect of increasing the permeability of the filtration filter of the lactase solution was observed. It is preferable to obtain peptides or proteins with large molecular weights by molecular weight fractionation or the like.
• the amount of yeast extract, soybean peptone, pea protein, casein hydrolyzate or corn steep liquor added to the lactase solution is preferably 0.01 to 10% by mass.
• the permeability of the filter for the lactase solution can be further increased.
• the cost can be reduced by setting the upper limit of the addition amount to the above value.
• the lactase solution in the present invention may contain the same amount of protease as the conventional one, but it preferably has lower protease activity than the conventional one. Since multiple proteases are often produced during culture, it is preferable to target the protease activity value contained in the lactase solution.
• the protease activity of the lactase solution in the present invention is preferably 20 U/g or less, more preferably 5 U/g or less, 3 U/g or less, further preferably 1 U/g or less. In the measurement method described later, it is particularly preferable that the concentration is less than the lower limit of detection.
• the above protease activity means a value measured by a casein hydrolysis-UV method.
• the lactase solution in the present invention may contain the same amount of arylsulfatase as in the past, but preferably has a lower arylsulfatase activity than in the past.
• the arylsulfatase activity of the lactase solution in the present invention is preferably 50 U/g or less, more preferably 10 U/g or less, and even more preferably 5 U/g or less and 3 U/g or less. In the measurement method described later, it is particularly preferable that the amount is less than the lower limit of detection (about 3 U/g).
• lactases produced by Aspergillus oryzae.
• acid lactase There is also a lactase from Bifidobacterium bifidum that acts at neutral and acidic (pH 4-10).
• Hosts include, for example, Aspergillus, Kluyveromyces, Trichoderma, Escherichia coli, Pichia, Saccharomyces, Yarrowia, Microorganisms of the genera Neurospora, Lactococcus or Bacillus are included.
• neutral lactase and acid lactase it is preferable to use neutral lactase and acid lactase, and it is particularly preferable to use neutral lactase derived from the genus Kluyveromyces, acid lactase derived from the genus Aspergillus, and lactase derived from Bifidobacterium.
• the lactase solution of the present invention may contain various components as necessary. Specific examples include metal salts, various sugars, ascorbic acid, glycerin, etc. that contribute to the stabilization of lactase, starch, dextrin, and inorganic salts with a buffering effect, which are excipients for improving usability. can be done.
• the activity of the lactase solution is preferably in the range of 100 to 1,000,000 U/g, more preferably in the range of 1,000 to 500,000 U/g, as determined by the measurement method described later. More preferably, it is in the range of ⁇ 110,000 U/g. It is preferably within this range both before and after transporting the packaged lactase solution. The lower the activity of the lactase solution, the worse the permeability of the filtration filter after transporting the packaged lactase solution.
• the lactase solution is preferably substantially transparent. This is because if the lactase solution becomes cloudy, the lactase solution tends to clog the filtration filter. Substantially clear means that the lactase solution is not turbid when visually observed.
• the lactase solution may be colored. Specifically, it may be a light yellow to light brown solution.
• a packaged lactase solution can be obtained by packaging the lactase solution.
• the temperature of the packaged lactase solution is preferably above 0°C and 20°C or less. Aggregates tend to form in the lactase solution as the temperature during storage and transportation increases. Although protein aggregates are not contained in the lactase solution immediately after the lactase solution is produced, the protein aggregates increase as the storage period increases and the lactase solution undergoes transportation. Protein aggregates include aggregates between lactase protein molecules, aggregates between lactase protein molecules and other protein molecules, and aggregates between other protein molecules.
• the amount of the stabilizer contained in the lactase solution is preferably 10% by mass to 90% by mass, more preferably 20% by mass to 80% by mass, and 30% by mass to 70% by mass. More preferably, it is particularly preferably 40% by mass to 60% by mass.
• the amount of stabilizer is at least the lower limit, it becomes easier to maintain the lactase activity of the lactase solution over a long period of time. If the amount of the stabilizer exceeds the upper limit, the viscosity of the lactase solution will increase, resulting in a longer filtration time and lower workability.
• Stabilizers include, for example, glycerin and sorbitol.
• the method for producing a lactase solution includes, for example, (1) a lactase extraction step that involves cell wall destruction after culturing a microorganism such as yeast; and a purification step to remove the like. (3) the step of adding an additive to the above lactase (which may be prepared immediately before or a commercially available product) as necessary, and (4) the step of filtering for sterilization. good.
• a container-packed lactase solution can be obtained by filling a predetermined container with a predetermined amount of the filtered lactase solution.
• the method for producing lactose-decomposed fermented milk includes: 1. 1. A method of adding lactase to milk before sterilization to decompose lactose and then inactivating the lactase at the same time as sterilizing the milk by heating (JP-A-5-501197); 2. a method of adding lactase to pasteurized milk to decompose lactose, and then inactivating the lactase by heat treatment, and then fermenting the milk; 4.
• the lactase solution of the present invention is used in the production of long-life milk.
• Long-life milk is long-term storage milk, and the manufacturing process consists of a sterilization process and a continuous aseptic packaging process. Paper containers sterilized in advance with hydrogen peroxide are filled in a process that enables aseptic packaging.
• the lactase solution added to long-life milk is generally added after filter sterilization when filling milk after ultra-high temperature short-time sterilization.
• the lactase solution according to the invention is particularly suitable for dairy production.
• dairy products include ice, milk such as long-life milk, yogurt, fresh cream, sour cream, cheese, and the like.
• the lactase solution according to the invention is suitable for the production of long-life milk.
• GODO-YNL2LS manufactured by Godo Shusei Co., Ltd.
• GODO-YNL2LS is a neutral lactase derived from Kluyveromyces, and has a lactase activity of 60,000 U/g, an arylsulfatase activity of less than the detection limit by the following measurement method, and a protease activity of less than the detection limit by the following measurement method. It had a specific gravity of 1.18 (g/mL) and contained 50% (v/v) of glycerin.
• a 25 mm stainless steel filter holder manufactured by PALL, product number 1209 (effective membrane area 3.7 cm 2 ) was connected to a stainless steel holder with a 47 mm tank (manufactured by Advantech Toyo Co., Ltd., product name "KST-47").
• the device was used as a device.
• the sample transmission part in the filter holder has an O-ring, a membrane, a support screen, and an underdrain disk from the entrance side of the measurement sample (in the test of the present invention, the filter of the stainless steel holder with tank And the parts of the filter holding part (support screen and its support) were not attached).
• the membrane was rinsed with a 50% glycerin aqueous solution and attached to a stainless steel filter holder.
• a lactase solution sample (sample) diluted in was put into a stainless steel holder with a tank. 5.
• an air compressor manufactured by Yaesaki Kuatsu Co., Ltd., product name "KAPSEL-CON YC-3R" or "PC4-15HLM"
• a pressure of 0.2 MPa was applied to the stainless steel holder with tank, and the enzyme solution was pumped. bottom.
• the permeated liquid is received in a container such as a beaker, and the amount of permeated liquid is recorded every 10 seconds . kg/min ⁇ m 2 )) was obtained by the following method.
• the lactase activity of the lactase solution described later was measured by the following method immediately after preparation and after storage at 50° C. for 3 days.
• the lactase activity immediately after preparation was defined as 100%, and the lactase activity after storage at 50°C for 3 days was shown as a relative value (%).
• an aqueous solution containing p-nitrophenol at a concentration of 0 to 0.5 mM was prepared.
• aqueous solution containing p-nitrophenol at a concentration of 0 to 0.5 mM was prepared.
• 0.5 mL of 100 mM potassium phosphate buffer (pH 6.5) solution was added, and 1.5 mL of 1.5 N sodium hydroxide aqueous solution was further added to obtain samples for measurement.
• Absorbance at 410 nm was measured to prepare a calibration curve.
• a predetermined amount of a predetermined additive was added to GODO-YNL2LS, and the slope (-a) indicating filter permeability and residual lactase activity were measured.
• the type of additive, amount added, slope and residual activity are shown in the table.
• Table 1 shows the results of using fatty acids or fatty acid salts as additives
• Table 2 shows the results of using proteins, peptides or amino acids as additives.
• Additives shown in the table were added to 60,000 U/g of GODO-YNL2LS in predetermined amounts to obtain respective lactase solutions. Each lactase solution immediately after preparation was subjected to filter permeability test and lactase activity measurement by the above method.
• the lactase activity was measured after storage at 50°C for 3 days. After putting 60 g of each lactase solution into a 1000 mL eyeboy (wide mouth (manufactured by AS ONE, product number 5-002-02)), the mixture was shaken at 20° C. with an amplitude of 30 mm and 100 spm for 1 hour. The lactase solution after shaking was allowed to stand for 1 hour, and the filter permeability test was performed by the method described above.
• the saturated fatty acids listed in the table are solid at room temperature and do not dissolve when added to the lactase solution.
• a saturated fatty acid was converted to a saturated fatty acid salt by the following method (saponification), and then added to the lactase solution. 0.03 g of saturated fatty acid and 1 mL of 1 M sodium hydroxide aqueous solution were mixed in a container, and 4 mL of distilled water was added. After saponification treatment in boiling water at 100° C. for 5 minutes, it was allowed to cool to room temperature, and the reaction product was added to 294 g of total lactase solution (GODO-YNL2LS) (addition amount 0.01%). The filtrate obtained by filtering this was subjected to a filter permeability test and lactase residual activity.
• the slope after shaking (-a) is preferably less than 0.5000, more preferably less than 0.1000, and more preferably less than 0.0500, considering actual product transactions. , is more preferably less than 0.0300, and most preferably less than 0.0100.
• the residual lactase activity is preferably 60% or more, more preferably 70% or more, even more preferably 80% or more, and 90% or more. is particularly preferred. The closer the residual activity of lactase activity is to 100%, the better.
• oleic acid, linoleic acid, and linolenic acid which were particularly promising, the following storage stability tests were conducted.
• Oleic acid, linoleic acid, and linolenic acid were added to 60,000 U/g of lactase solution to 0.005% and 0.01%, and after storage at 12°C for 30 days, the above filter permeability test and lactase activity were performed. When the residual activity was measured, it was confirmed that both were at a practical level.

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