CN114958951A - Preparation method of casein phosphopeptide for improving digestion function of pet dogs and cats - Google Patents
Preparation method of casein phosphopeptide for improving digestion function of pet dogs and cats Download PDFInfo
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- CN114958951A CN114958951A CN202210794516.2A CN202210794516A CN114958951A CN 114958951 A CN114958951 A CN 114958951A CN 202210794516 A CN202210794516 A CN 202210794516A CN 114958951 A CN114958951 A CN 114958951A
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- 239000005018 casein Substances 0.000 title claims abstract description 43
- 235000021240 caseins Nutrition 0.000 title claims abstract description 43
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 title claims abstract description 42
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- 108010001441 Phosphopeptides Proteins 0.000 title claims abstract description 26
- 230000029087 digestion Effects 0.000 title claims abstract description 11
- 238000002360 preparation method Methods 0.000 title claims abstract description 11
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- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 claims abstract description 17
- 239000011701 zinc Substances 0.000 claims abstract description 16
- 229910052725 zinc Inorganic materials 0.000 claims abstract description 16
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims abstract description 8
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- VTYYLEPIZMXCLO-UHFFFAOYSA-L Calcium carbonate Chemical compound [Ca+2].[O-]C([O-])=O VTYYLEPIZMXCLO-UHFFFAOYSA-L 0.000 description 2
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- MSWZFWKMSRAUBD-IVMDWMLBSA-N 2-amino-2-deoxy-D-glucopyranose Chemical compound N[C@H]1C(O)O[C@H](CO)[C@@H](O)[C@@H]1O MSWZFWKMSRAUBD-IVMDWMLBSA-N 0.000 description 1
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- 239000004201 L-cysteine Substances 0.000 description 1
- LEVWYRKDKASIDU-IMJSIDKUSA-N L-cystine Chemical compound [O-]C(=O)[C@@H]([NH3+])CSSC[C@H]([NH3+])C([O-])=O LEVWYRKDKASIDU-IMJSIDKUSA-N 0.000 description 1
- 235000019393 L-cystine Nutrition 0.000 description 1
- 239000004158 L-cystine Substances 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 1
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- DWAQJAXMDSEUJJ-UHFFFAOYSA-M Sodium bisulfite Chemical compound [Na+].OS([O-])=O DWAQJAXMDSEUJJ-UHFFFAOYSA-M 0.000 description 1
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- 125000002467 phosphate group Chemical group [H]OP(=O)(O[H])O[*] 0.000 description 1
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- 108091005981 phosphorylated proteins Proteins 0.000 description 1
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- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
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Classifications
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K20/00—Accessory food factors for animal feeding-stuffs
- A23K20/10—Organic substances
- A23K20/142—Amino acids; Derivatives thereof
- A23K20/147—Polymeric derivatives, e.g. peptides or proteins
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K50/00—Feeding-stuffs specially adapted for particular animals
- A23K50/40—Feeding-stuffs specially adapted for particular animals for carnivorous animals, e.g. cats or dogs
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
- C07K1/113—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/30—Extraction; Separation; Purification by precipitation
-
- 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
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- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Polymers & Plastics (AREA)
- Zoology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Animal Husbandry (AREA)
- Analytical Chemistry (AREA)
- Biophysics (AREA)
- Food Science & Technology (AREA)
- Wood Science & Technology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
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Abstract
The invention discloses a preparation method of casein phosphopeptide for improving the digestion function of pet dogs and cats, and relates to the field of preparation of polypeptide-metal chelate. In particular to a method for preparing high-zinc casein phosphopeptide by carrying out enzymolysis on casein under an acidic condition, reducing and breaking a protein disulfide bond by using hydrogen generated by the reaction of zinc and hydrochloric acid, and utilizing the chelation effect of zinc ions, cysteine and methionine to protect free sulfydryl. The invention overcomes the defect of low enzymolysis efficiency caused by poor solubility of casein in a water-soluble environment, effectively avoids reaggregation of opened protein disulfide bonds by zinc ion chelation, and the obtained casein phosphopeptide can promote appetite of pets, dogs and cats and improve digestibility of the casein phosphopeptide to protein, fat and the like.
Description
Technical Field
The invention relates to the field of preparation of polypeptide-metal chelates, in particular to a preparation method of high-zinc casein phosphopeptide and application of the high-zinc casein phosphopeptide in pets.
Background
Zinc is one of essential trace elements for animals, and plays a significant role in the physiological processes of growth, development, immunity, endocrine and the like of the animals. Zinc has effects of improving taste, stimulating appetite, enhancing immunity, and promoting brain development. When the young dogs and cats are in the growth period, the digestive system is not completely developed, and the intestinal tracts can not effectively absorb nutrient substances. Therefore, the young dogs and cats are easy to have symptoms of gastrointestinal discomfort, dyspepsia and the like, which can cause low immunity, are easy to be ill and even influence normal growth and development. The polypeptide has the characteristics of small irritation, easy absorption and the like, so that the zinc can be chelated with the polypeptide, the absorption efficiency of the zinc can be improved, and the digestion rate of dogs and cats can be promoted.
Casein is hard and compact curd, has the defects of poor solubility, difficult full enzymolysis and digestion and the like, accounts for 80-82 percent of milk protein, wherein the alpha s 1-casein is the main component in the milk protein and is a highly phosphorylated protein (1 molecule contains 8 phosphate groups), and casein phosphopeptide can be obtained after enzymatic hydrolysis, and has the effects of reducing blood pressure, resisting oxidation, promoting the absorption of metal ions by organisms and the like. Casein is rich in cysteine (about 3%), and cysteine has functions of broad-spectrum antibacterial, chelating metal ions, protecting thiol protease and liver cells from damage, stimulating hematopoiesis function, increasing leukocyte, promoting skin injury repair, promoting liver function recovery, participating in cell reduction process and phospholipid metabolism in liver, and is also an important constituent amino acid of keratin such as hair. The thiol groups of these cysteines are mainly present in the form of disulfide bonds. The more the number of disulfide bonds of the protein is, the more the protein is tightly crosslinked and is more difficult to dissolve in water, so that the protease is difficult to attack the enzymolysis sites protected by the disulfide bonds, and the enzymolysis efficiency of the casein is low, so that the preparation of casein phosphopeptides with high content of cysteine by improving the enzymolysis efficiency becomes a research hotspot. The traditional method generally adopts two steps: the first step, the disulfide bond of the protein is reduced into free sulfhydryl group by using a reduction method (such as adding reducing agent sodium bisulfite); and secondly, carrying out proteolysis under neutral or alkaline conditions to form oligopeptide with high cysteine content. However, since the free thiol group of cysteine is easily oxidized into a disulfide bond under neutral or alkaline conditions, it is necessary to protect the free thiol group.
The zinc ions and the sulfydryl of the cysteine can be coordinated to form a finger-like structure, so that the effect of protecting the free sulfydryl is achieved. The zinc metal-hydrochloric acid reduction method is a commonly used method for preparing L-cysteine by reducing L-cystine, but the zinc is used for simultaneously realizing the reduction of casein disulfide bonds and the protection of free sulfydryl and reducing the separation difficulty of a subsequent product, namely casein phosphopeptide, and the research on the improvement of the digestion function of pet dogs and cats by using the casein phosphopeptide prepared by the method is not reported yet.
Disclosure of Invention
In order to overcome the defects of the existing methods, the invention aims to provide a preparation method of a casein phosphopeptide-zinc chelate on one hand and provide application of the casein phosphopeptide-zinc chelate in functional foods for pets on the other hand.
The invention provides a preparation method of casein phosphopeptide for improving the digestion function of pet dogs and cats, which comprises the following steps:
(1) carrying out casein enzymolysis: adding 250-500 parts of water into 10 parts of casein, adjusting the pH value to 1.5-2.0, adding 0.02-0.05 part of pepsin, maintaining the temperature at 35-42 ℃, and carrying out enzymolysis until the hydrolysis degree is 15% -20%.
(2) Zinc reduction of disulfide bonds: adding concentrated hydrochloric acid into the casein hydrolysate, adjusting the final concentration of the hydrochloric acid to 1.5-2.5 mol/L, adding 2-5 parts of zinc powder, and reacting at 50-60 ℃ for 1.5-2.5 h.
By this setting, H produced by the reaction of zinc powder with hydrochloric acid 2 Cysteine disulfide bonds in casein and casein hydrolysate can be reduced into free sulfydryl, and the free sulfydryl can be further chelated with zinc ions, so that the solubility of the polypeptide is reduced.
(3) Casein phosphopeptide precipitation: adding 0.1-0.2 part of methionine, slowly adding NaOH solid, stirring, adjusting the pH value to 5.5-6.5, cooling to 0-10 ℃, standing for at least 1h, centrifuging, removing supernatant, taking precipitate, cleaning with 95% ethanol, removing impurities, and drying to obtain casein phosphopeptide.
Through this settlement, free sulfydryl, carboxyl, amino and zinc ion chelate on a plurality of polypeptide and the amino acid side chain can further chelate with methionine and bridge, form the molecular aggregate and further reduce the solubility of complex, and when pH is 5.5 ~ 6.5, the net charge volume of complex is minimum, and the solubility is minimum this moment, through reducing the temperature, further reduces the solubility, accessible simple centrifugation obtains casein phosphopeptide.
The casein phosphopeptide obtained by the method is applied to pet food for improving the digestion function of young pet dogs and cats.
The invention has the following specific advantages:
(1) the process is as follows: the first step is to carry out enzymolysis under acidic conditions, after the reaction is finished, the protease inactivation treatment can be directly realized by adjusting the hydrochloric acid concentration to be 1.5-2.5 mol/L, and the process is simple; second step, the zinc reacts with hydrochloric acid to produce H 2 And zinc ions, the zinc ions are not required to be added in the subsequent process while the disulfide bond is reduced; the third step is that simple zinc ions are chelated with oligopeptide, the precipitate is slowly formed, the yield is low, more amino groups capable of being coordinated are provided by adding methionine, the chelation rate is obviously increased, and the precipitate formation speed and the precipitate yield are further increased (by more than 88%) by adjusting the pH value and reducing the temperature;
(2) in effect: the casein phosphopeptide prepared by the method contains organic chelated zinc, reduced cysteine and glutamine with higher proportion. The organic chelated zinc has the advantages of small irritation and high absorption rate while realizing zinc supplement, and can promote appetite and improve the digestive function of animals on protein, fat and the like. Cysteine can be used for supplementing nutrition for human body, can be further converted into taurine to participate in metabolism of human body, has the functions of diminishing inflammation, easing pain, maintaining osmotic pressure balance of organism, maintaining normal vision, promoting digestion and absorption of lipid and the like, and in addition, glutamine has a promoting effect on the biochemical synthesis of hexosamine and glucosamine which are components of epithelium of gastrointestinal mucosa, and can play a role in protecting intestinal mucosa and promoting the absorption capacity of intestinal tract. After the casein phosphopeptide diet prepared by the method is added for one week, the digestibility of the young Chinese county cat on the crude protein and the crude fat is increased by at least 21% and 22%, the digestibility of the young Chinese county cat on the crude protein and the crude fat is increased by at least 19% and 10%, and the average daily food consumption is increased by more than 10 g/d.
Detailed Description
Terms used in the present invention have generally meanings as commonly understood by one of ordinary skill in the art, unless otherwise specified. The present invention is described in further detail below with reference to specific examples and with reference to the data. It will be understood that these examples are intended to illustrate the invention and are not intended to limit the scope of the invention in any way.
In the following examples, various processes and methods not described in detail are conventional methods well known in the art. The source, trade name and composition of the reagents used are indicated at the first appearance and the same reagents used thereafter are the same as indicated for the first time unless otherwise specified.
The method for measuring the protein content in the comparative examples and the examples refers to national standard GB/T5009.5-2016.
The method for measuring the oil content in the comparative examples and the examples refers to the national standard GB/T5009.6-2016.
Reference is made to Kuang Xiaoxian, Zuisingjiin, Heguanhao, and the like, the preparation of milk-derived zinc chelate by enzymolysis and the analysis of the chelating property thereof [ J ] the food and fermentation industry, 2019,45(10):135-141.
The pepsin used in the invention is purchased from Nanning Pombo bioengineering Co., Ltd, and the unit enzyme activity is 3000NF U/mg.
Comparative example 1
Adding 10g casein into 500g water, adjusting pH to 2.0, adding 0.05g pepsin, maintaining temperature at 35 deg.C, and performing enzymolysis until hydrolysis degree is 15%.
Slowly adding NaOH solid and stirring, adjusting pH to 5.5, cooling to 10 ℃, standing for at least 1h, centrifuging, removing supernatant, taking precipitate, cleaning with 95% ethanol to remove impurities, and drying to obtain casein phosphopeptide, wherein the yield is 17%.
Example 1
(1) Adding 10g casein into 500g water, adjusting pH to 2.0, adding 0.05g pepsin, maintaining temperature at 35 deg.C, and performing enzymolysis until hydrolysis degree is 15%.
(2) Adding concentrated hydrochloric acid into casein hydrolysate, adjusting the final concentration of hydrochloric acid to 2.5mol/L, adding 2g zinc powder, and reacting at 60 deg.C for 1.5 h.
(3) Adding 0.2g of methionine, slowly adding NaOH solid, stirring, adjusting pH to 5.5, cooling to 10 ℃, standing for at least 1h, centrifuging, removing supernatant, taking precipitate, cleaning with 95% ethanol, removing impurities, and drying to obtain casein phosphopeptide with the yield of 37%.
Example 2
(1) Adding 10g casein into 250g water, adjusting pH to 1.5, adding 0.02g pepsin, maintaining temperature at 42 deg.C, and performing enzymolysis to hydrolysis degree of 20%.
(2) Adding concentrated hydrochloric acid into casein hydrolysate, adjusting the final concentration of hydrochloric acid to 1.5mol/L, adding 5g zinc powder, and reacting at 50 deg.C for 2.5 h.
(3) Adding 0.1g of methionine, slowly adding NaOH solid, stirring, adjusting pH to 6.5, cooling to 0 ℃, standing for at least 1h, centrifuging, removing supernatant, taking precipitate, cleaning with 95% ethanol, removing impurities, and drying to obtain casein phosphopeptide with yield of 32%.
Example 3
(1) Adding 10g casein into 375g water, adjusting pH to 1.5, adding 0.04g pepsin, maintaining temperature at 37.5 deg.C, and performing enzymolysis to hydrolysis degree of 18%.
(2) Adding concentrated hydrochloric acid into casein hydrolysate, adjusting the final concentration of hydrochloric acid to 2.0mol/L, adding 4g zinc powder, and reacting at 55 deg.C for 2 h.
(3) Adding 0.15g of methionine, slowly adding NaOH solid, stirring, adjusting pH to 6.0, cooling to 4 ℃, standing for at least 1h, centrifuging, removing supernatant, taking precipitate, cleaning with 95% ethanol, removing impurities, and drying to obtain casein phosphopeptide with yield of 47%.
The beneficial effects of the present invention are illustrated by the following animal experimental examples.
The experimental method comprises the following steps: selecting 40 young Chinese garden dogs (age 5-7 months, weight 5.0-7.5 kg) and 40 young Chinese garden cats (age 4-7 months, weight 1.0-3.0 kg), randomly dividing into 4 groups, wherein each group comprises 10 puppies and 10 puppies, wherein the male: female-5: 5. the control group was fed with 0.01% of the diet of comparative example 1 (see tables 1 and 2), and the experimental groups 1, 2 and 3 for dogs and cats were fed with 0.01% of the diets of examples 1, 2 and 3, respectively, and were fed freely and continuously for 7 days, and the feed intake and body weight of pet dogs and cats were measured daily, and feces were collected on day 8 to examine the digestibility of crude protein and crude oil.
The necessary immunization, anthelmintic treatment, was performed on the dogs and cats prior to the experiment, and no drug (e.g., antibiotic) that would alter the gut microflora was fed to the dogs and cats 15 days before the experiment began. Keeping the pet house clean, feeding daily ration to each dog and cat regularly every day, and ensuring free drinking and eating during the whole experiment.
TABLE 1 nutritional level of basic ration for young Chinese rural dogs
| Composition (I) | Content/% |
| Crude protein | 32.0 |
| Crude fat | 13.0 |
| Coarse fiber | 5.0 |
| Moisture content | 10.0 |
| Calcium carbonate | 1.2 |
| Total phosphorus | 1.0 |
| Lysine | 1.2 |
| Coarse ash content | 10.0 |
| Water soluble chlorides (as Cl) - Meter) | 0.4 |
TABLE 2 nutritional level of basic ration for young Chinese countryside cats
The experimental results are as follows:
as shown in Table 3, examples 1, 2 and 3 are all effective in promoting appetite of pet dogs and cats. After 7 days of feeding, the dog experimental groups 1, 2 and 3 added with the examples 1, 2 and 3 can eat at least 153.47g of daily ration on average, and compared with 142.48g of the dog control group, the difference is obvious. The experimental groups 1, 2 and 3 of cats added with examples 1, 2 and 3 can eat at least 54.56g of daily ration on average, while the control group of cats can eat 43.74g of daily ration, which is a significant difference.
TABLE 3 growth of pet dogs and cats
| Group of | Average daily food intake g/d |
| Dog control group | 142.48 |
| Dog experimental group 1 | 159.25 |
| Dog experimental group 2 | 153.47 |
| Dog experimental group 3 | 156.93 |
| Cat control group | 43.74 |
| Cat test group 1 | 59.47 |
| Cat experiment group 2 | 54.56 |
| Cat experiment group 3 | 55.93 |
As shown in Table 4, examples 1, 2 and 3 all improved the digestion of pet dogs and cats. After 7 days of feeding, the crude protein digestibility and crude fat digestibility of the dog experimental groups 1, 2 and 3 added with the examples 1, 2 and 3 are 81.68% and 84.44% at least, and are improved by 19.52% and 10.71% compared with the dog control group. The crude protein digestibility and crude fat digestibility of the cat experimental groups 1, 2 and 3 added with the examples 1, 2 and 3 are 71.87% and 73.79% at the lowest, while the crude protein digestibility and crude fat digestibility of the cat control group are 59.34% and 60.25%, and the difference is very significant.
TABLE 4 digestibility of crude protein and crude fat for pet dogs and cats
The above embodiments are only specific examples of the present invention, and the protection scope of the present invention includes but is not limited to the product forms and styles of the above embodiments, and any suitable changes or modifications made by those skilled in the art according to the claims of the present invention shall fall within the protection scope of the present invention.
Claims (1)
1. A preparation method of casein phosphopeptide for improving the digestion function of pet dogs and cats is characterized by comprising the following steps:
(1) carrying out casein enzymolysis: adding 250-500 parts of water into 10 parts of casein, adjusting the pH value to 1.5-2.0, adding 0.02-0.05 part of pepsin, maintaining the temperature at 35-42 ℃, and carrying out enzymolysis until the hydrolysis degree is 15% -20%;
(2) zinc reduction of disulfide bonds: adding concentrated hydrochloric acid into the casein hydrolysate, adjusting the final concentration of the hydrochloric acid to 1.5-2.5 mol/L, adding 2-5 parts of zinc powder, and reacting at 50-60 ℃ for 1.5-2.5 h;
(3) casein phosphopeptide precipitation: adding 0.1-0.2 part of methionine, slowly adding NaOH solid, stirring, adjusting the pH value to 5.5-6.5, cooling to 0-10 ℃, standing for at least 1h, centrifuging, removing supernatant, taking precipitate, cleaning with 95% ethanol, removing impurities, and drying to obtain casein phosphopeptide.
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| US5834427A (en) * | 1995-03-23 | 1998-11-10 | Sang Kee Han | Casein phosphopeptide, casein containing same and process for the preparation thereof |
| CN103494214A (en) * | 2013-09-29 | 2014-01-08 | 安徽农业大学 | Casein phosphopeptide and zinc chelate compound |
| CN107141240A (en) * | 2017-06-19 | 2017-09-08 | 广汉隆达饲料有限公司 | The preparation method of feed grade hydroxy methionine chelates of zinc |
| CN107557418A (en) * | 2016-06-30 | 2018-01-09 | 天津唐朝食品工业有限公司 | CPP extracting method |
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| US5834427A (en) * | 1995-03-23 | 1998-11-10 | Sang Kee Han | Casein phosphopeptide, casein containing same and process for the preparation thereof |
| CN103494214A (en) * | 2013-09-29 | 2014-01-08 | 安徽农业大学 | Casein phosphopeptide and zinc chelate compound |
| CN107557418A (en) * | 2016-06-30 | 2018-01-09 | 天津唐朝食品工业有限公司 | CPP extracting method |
| CN107141240A (en) * | 2017-06-19 | 2017-09-08 | 广汉隆达饲料有限公司 | The preparation method of feed grade hydroxy methionine chelates of zinc |
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