CN113862321A - Method for extracting nutritional ingredients from cattle hair or cattle hide leftover - Google Patents
Method for extracting nutritional ingredients from cattle hair or cattle hide leftover Download PDFInfo
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- CN113862321A CN113862321A CN202111181236.6A CN202111181236A CN113862321A CN 113862321 A CN113862321 A CN 113862321A CN 202111181236 A CN202111181236 A CN 202111181236A CN 113862321 A CN113862321 A CN 113862321A
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Abstract
The invention relates to a method for extracting nutritional components from cattle hair or cattle hide leftover, and belongs to the field of resource utilization of tanning solid waste. The method comprises the following steps: taking cow hair and cow leather leftover materials generated in the tanning unhairing liming procedure as raw materials, and extracting nutritional ingredients such as protein, fat, saccharides and the like in the raw materials under the action of a complex enzyme preparation; the compound enzyme preparation comprises the following components: including protease, lipase, glycosidase. The invention successfully solves the problem of hair solid waste treatment generated in unhairing liming and the problem of cowhide leftover solid waste treatment generated in unhairing liming; effectively controls the content and molecular weight of nutritional components in the beverage, and is beneficial to subsequent application.
Description
Technical Field
The invention relates to a method for extracting nutritional components from cattle hair or cattle hide leftover, and belongs to the field of resource utilization of tanning solid waste.
Background
The cow leather is widely applied to preparing sofa leather, instep leather, bag leather and the like at present, and is the most main leather type for producing the original leather. The unhairing liming process is an essential ring in leather productionOne of the sections. In this process, the epidermal layer of hair in the hide is removed, thus producing a large amount of hair; in addition, a large amount of cowhide scraps are produced during the fleshing process. The main components of the solid wastes are hair keratin and skin collagen, and the solid wastes also contain partial fat and glycoprotein components; furthermore, in view of the leather production process, these solid wastes may contain small amounts of chemical components: such as sodium chloride (NaCl), calcium hydroxide (Ca (OH)2) Sodium carbonate (Na)2CO3) And the like, all inorganic components harmless to living bodies. Therefore, the solid waste of the cattle hair and the cattle hide leftover has potential nutrient utilization value. Effective nutritional ingredients such as protein, fat, glycoprotein and the like in the biomass are extracted in a targeted manner, so that the resource recycling of animal biomass components is facilitated.
The hair keratin and the skin collagen both belong to scleroprotein, and the structure of the hair keratin and the skin collagen is relatively stable and not easy to recycle. The traditional incineration decrement treatment mode causes resource waste. The biological enzyme has high efficiency for the degradation treatment of biomass, and the enzyme preparation is used for extracting the nutrient substances such as protein, fat, saccharides and the like in the cattle hair and cattle hide leftover solid waste, so that the high-efficiency clean extraction effect can be achieved.
Disclosure of Invention
The invention provides a method for extracting nutritional ingredients from cow hair or cow leather leftover materials, and particularly relates to a method for extracting effective nutritional ingredients such as protein, sugar, fat and the like from two types of solid wastes of cow hair and cow leather leftover materials generated in a cow leather unhairing and liming process by using a complex enzyme preparation, so that resource utilization of tanning wastes is realized. The technical scheme of the invention is as follows:
a method for extracting nutritional ingredients from cattle hair or cattle hide leftover materials comprises the following steps:
taking cow hair and cow leather leftover materials generated in the tanning unhairing liming procedure as raw materials, and extracting nutritional ingredients such as protein, fat, saccharides and the like in the raw materials under the action of a complex enzyme preparation;
the compound enzyme preparation comprises the following components: including proteases, lipases, glycosidases; wherein the content of the first and second substances,
the protease is selected from Bacillus (Bacillus) fermentation, and the protease activity is 15000-100000U/g; or Aspergillus (Aspergillus) fermentation, protease activity is at least one of 18000U/g-80000U/g;
the lipase is selected from at least one of fungi (fungus) fermentation, the lipase activity is 20000U/g-50000U/g, yeast (Sccharomycetes) fermentation, the lipase activity is 15000U/g-30000U/g, or Bacillus (Bacillus) fermentation, and the lipase activity is 15000-50000U/g;
the glycosidase is selected from at least one of Bacillus (Bacillus) fermentation, the glycosidase activity is 12000U/g-25000U/g, Aspergillus (Aspergillus) fermentation, the glycosidase activity is 13000-28000U/g, or Trichoderma (Trichoderma) fermentation, and the glycosidase activity is 90000-110000U/g.
Further, the extraction method comprises the following specific steps:
(1) degrading the ox hair by using a complex enzyme preparation of alkaline protease and glycosidase under the condition that the pH value is more than 10; wherein the total enzyme activity of the alkaline protease is 40U/ml-300U/ml, the total enzyme activity of the glycosidase is 20U/ml-100U/ml, and hydrolysate A is obtained; preferably, the pH is adjusted using sodium hydroxide; the total enzyme activity of the alkaline protease is 150U/ml, and the total enzyme activity of the glycosidase is 50U/ml.
(2) Degrading and extracting the cowhide leftover materials in an alkaline environment or an acidic environment; under alkaline environment, pH >10, using alkaline protease; in an acidic environment, pH <5, an acidic protease is used. The total enzyme activity of the acid protease or the alkaline protease is 40U/ml-300U/ml, the total enzyme activity of the lipase is 30-150U/ml, and the total enzyme activity of the glycosidase is 20U/ml-100U/ml, so as to obtain hydrolysate B; preferably, the alkaline environment is adjusted by sodium hydroxide, and the acidic environment is adjusted by citric acid; the total enzyme activity of the acid protease or the alkaline protease is 200U/ml, the total enzyme activity of the lipase is 30U/ml, and the total enzyme activity of the glycosidase is 60U/ml.
(3) Mixing the hydrolysate A and the hydrolysate B in a ratio of 3:1-6:1, filtering, regulating the molecular weight to 2000-6000 by using a neutral or alkaline protease preparation according to the pH value after mixing, wherein the acting enzyme activity is 20-150U/ml, the reaction temperature is 20-60 ℃, the mixing time is 4-24h, and the effective extraction of the nutritional ingredients can be realized by spraying or freeze drying. Preferably, the acting enzyme activity is 100U/ml, and the reaction temperature is 60 ℃.
Compared with the prior art, the invention has the following advantages:
(1) successfully solves the problem of hair solid waste treatment generated in unhairing liming;
(2) successfully solves the problem of processing the solid wastes of the cowhide leftover materials generated in the unhairing liming;
(3) effectively control the content and molecular weight of nutritional components in the beverage, and is beneficial to subsequent application.
Drawings
FIG. 1 shows the microscopic morphology and the distribution of the major elements of the extracted solid;
FIG. 2 is a liquid chromatogram of the amino acid profile after extraction, wherein 1,2, and 3 are the peaks of the derivatizing reagent in the liquid phase assay.
Detailed Description
The invention will be further described with reference to specific embodiments, and the advantages and features of the invention will become apparent as the description proceeds. The examples are illustrative only and do not limit the scope of the present invention in any way. It will be understood by those skilled in the art that various changes in form and details may be made therein without departing from the spirit and scope of the invention, and that such changes and modifications may be made without departing from the spirit and scope of the invention.
Example 1: method for extracting nutritional ingredients from cattle hair or cattle hide leftover
(1) Primary degradation of cow hair: adjusting the pH value to 10.5 by using sodium hydroxide, and using a complex enzyme preparation A of alkaline protease and glycosidase, wherein the enzyme activity of the alkaline protease is 150U/ml, the enzyme activity of the glycosidase is 50U/ml, the action temperature is 60 ℃, and the reaction time is 8 hours, so as to obtain a hydrolysate A for primary degradation of the cow hair;
(2) primary degradation of cowhide leftover materials: adjusting the pH value to 13 by using sodium hydroxide, boiling at high temperature, and adding a complex enzyme preparation B, wherein the activity of alkaline protease is 200U/ml, the activity of lipase is 30U/ml, the activity of glycosidase is 60U/ml, the action temperature is 60 ℃, and the reaction time is 24 hours to obtain hydrolysate B for primary degradation of the cowhide leftover;
(3) mixing the hydrolysate A and the hydrolysate B in a ratio of 6:1, performing secondary degradation on the mixture by using an alkaline protease preparation with the activity of 100U/ml, wherein the reaction temperature is 60 ℃, the action time is 10 hours, observing that suspended matters are completely dissolved, collecting hydrolysate, cooling and drying to realize effective extraction of nutritional ingredients;
the alkaline protease preparation is fermented by Bacillus subtilis, and the activity of the protease is 60000U/g.
Example 2: method for extracting nutritional ingredients from cattle hair or cattle hide leftover
(1) Primary degradation of cow hair: adjusting the pH value to 13 by using sodium hydroxide, boiling for 12 hours, and using a complex enzyme preparation A of alkaline protease and glycosidase for the cooling liquid, wherein the alkaline protease contains bacillus, the enzyme activity is 100U/ml, the glycosidase activity is 25U/ml, the action temperature is 40 ℃, and the reaction time is 8 hours, so as to obtain a hydrolysate A for primary degradation of the cow hair;
the alkaline protease is fermented by Bacillus subtilis, and the activity of the protease is 45000U/g; the glycosidase is fermented by Trichoderma (Trichoderma), and the activity of the glycosidase is 95000U/g;
(2) primary degradation of cowhide leftover materials: adjusting the pH value to 2 by using citric acid, boiling at high temperature, and adding a complex enzyme preparation B, wherein the activity of acid protease is 100U/ml, the activity of lipase is 20U/ml, the activity of glycosidase is 40U/ml, the action temperature is 40 ℃, and the reaction time is 24 hours to obtain hydrolysate B for primary degradation of the cowhide leftover;
the acid protease is fermented by Aspergillus niger (Aspergillus niger), and the protease activity is 30000U/g; the lipase is fermented by Bacillus (Bacillus), and the activity of the lipase is 35000U/g; the glycosidase is fermented by Bacillus (Bacillus), and the activity of the glycosidase is 15000U/g;
(3) mixing the hydrolysate A and the hydrolysate B in a ratio of 3:1, performing secondary degradation on the mixture by using a neutral protease preparation, wherein the reaction temperature is 40 ℃, the action time is 18 hours, observing that suspended matters are completely dissolved, collecting hydrolysate, cooling and drying to realize effective extraction of nutritional ingredients;
the neutral protease preparation is fermented by Bacillus (Bacillus), and the activity of the protease is 60000U/g.
Example 3: method for extracting nutritional ingredients from cattle hair or cattle hide leftover
(1) Primary degradation of cow hair: adjusting the pH value to 10.5 by using sodium hydroxide, and using a complex enzyme preparation A of complex alkaline protease and glycosidase, wherein the enzyme activity of the alkaline protease is 150U/ml, the enzyme activity of the glycosidase is 50U/ml, the action temperature is 60 ℃, and the reaction time is 8 hours, so as to obtain hydrolysate A for primary degradation of the cow hair;
the composite alkaline protease is fermented by Bacillus subtilis and Bacillus amyloliquefaciens, the total activity of the protease is 40000U/g, and the ratio of the activity to the activity is 1: 1; the lipase is fermented by Aspergillus (Aspergillus), and the lipase activity is 30000U/g; the glycosidase is fermented by Bacillus subtilis, and the activity of the glycosidase is 15000U/g;
(2) primary degradation of cowhide leftover materials: adjusting the pH value to 13 by using sodium hydroxide, boiling at high temperature, and adding a complex enzyme preparation B, wherein the activity of alkaline protease is 200U/ml, the activity of lipase is 30U/ml, the activity of glycosidase is 60U/ml, the action temperature is 60 ℃, and the reaction time is 24 hours to obtain hydrolysate B for primary degradation of the cowhide leftover;
the alkaline protease is fermented by Bacillus amyloliquefaciens (Bacillus amyloliquefaciens), the activity of the protease is 30000U/g, the lipase is fermented by Aspergillus (Aspergillus), and the activity of the lipase is 30000U/g; the glycosidase is fermented by Bacillus subtilis, and the activity of the glycosidase is 15000U/g;
(3) mixing the hydrolysate A and the hydrolysate B in a ratio of 3:1, performing secondary degradation on the mixture by using an alkaline protease preparation with the activity of 100U/ml, wherein the reaction temperature is 60 ℃, the action time is 12 hours, observing that suspended matters are completely dissolved, collecting hydrolysate, cooling and drying to realize effective extraction of nutritional ingredients;
the alkaline protease preparation is fermented by Bacillus subtilis, and the activity of the protease is 60000U/g.
Test example: the extract is subjected to heavy metal content detection, and the detection of toxic and harmful heavy metals meets the detection limit requirement. The results are shown in Table 1; the microstructure and the distribution of main elements of the extract are shown in figure 1; the liquid chromatogram of the amino acid distribution in the extract is shown in FIG. 2, and the amino acid content is shown in Table 2. Wherein, 1,2 and 3 are derived reagent peaks in a liquid phase test. As can be seen from the figure, the extracted product contains 12 amino acids, including five kinds of essential amino acids (valine (Val), leucine (Leu), isoleucine (Ile), phenylalanine (Phe), lysine (Lys)) and seven kinds of common amino acids (aspartic acid (Asp), glutamic acid (Glu), hydroxyproline (Hyp), glycine (Gly), proline (Pro), alanine (Ala), tyrosine (Tyr)), and thus has high nutritional properties.
TABLE 1 table of the content of heavy metals extracted
Claims (7)
1. A method for extracting nutritional ingredients from cattle hair or cattle hide leftover materials is characterized by comprising the following steps:
taking cow hair and cow leather leftover materials generated in the tanning unhairing liming procedure as raw materials, and extracting nutritional ingredients such as protein, fat, saccharides and the like in the raw materials under the action of a complex enzyme preparation;
the compound enzyme preparation comprises the following components: including proteases, lipases, glycosidases; wherein the content of the first and second substances,
the protease is selected from Bacillus (Bacillus) fermentation, and the protease activity is 15000-100000U/g; or Aspergillus (Aspergillus) fermentation, protease activity is at least one of 18000U/g-80000U/g;
the lipase is selected from at least one of fungi (fungus) fermentation, the lipase activity is 20000U/g-50000U/g, yeast (Sccharomycetes) fermentation, the lipase activity is 15000U/g-30000U/g, or Bacillus (Bacillus) fermentation, and the lipase activity is 15000-50000U/g;
the glycosidase is selected from at least one of Bacillus (Bacillus) fermentation, the glycosidase activity is 12000U/g-25000U/g, Aspergillus (Aspergillus) fermentation, the glycosidase activity is 13000-28000U/g, or Trichoderma (Trichoderma) fermentation, and the glycosidase activity is 90000-110000U/g.
2. The method according to claim 1, characterized in that the method comprises the following specific steps:
(1) degrading the ox hair by using a complex enzyme preparation of alkaline protease and glycosidase under the condition that the pH value is more than 10; wherein the total enzyme activity of the alkaline protease is 40U/ml-300U/ml, the total enzyme activity of the glycosidase is 20U/ml-100U/ml, and hydrolysate A is obtained;
(2) degrading and extracting the cowhide leftover materials in an alkaline environment or an acidic environment; under alkaline environment, pH >10, using alkaline protease; in an acidic environment, pH <5, an acidic protease is used. The total enzyme activity of the acid protease or the alkaline protease is 40U/ml-300U/ml, the total enzyme activity of the lipase is 30-150U/ml, and the total enzyme activity of the glycosidase is 20U/ml-100U/ml, so as to obtain hydrolysate B;
(3) mixing the hydrolysate A and the hydrolysate B in a ratio of 3:1-6:1, filtering, regulating the molecular weight to 2000-6000 by using a neutral or alkaline protease preparation according to the pH value after mixing, wherein the acting enzyme activity is 20-150U/ml, the reaction temperature is 20-60 ℃, the mixing time is 4-24h, and the effective extraction of the nutritional ingredients can be realized by spraying or freeze drying.
3. The method according to claim 2, wherein the pH in step (1) is adjusted by using sodium hydroxide.
4. The method according to claim 2, wherein the total activity of alkaline protease on the enzyme in step (1) is 150U/ml, and the total activity of glycosidase on the enzyme is 50U/ml.
5. The method of claim 2, wherein in the step (2), the alkaline environment is adjusted by sodium hydroxide, and the acidic environment is adjusted by citric acid.
6. The method according to claim 2, wherein the total activity of acid protease or alkaline protease in step (2) is 200U/ml, the total activity of lipase in step (2) is 30U/ml, and the total activity of glycosidase in step (2) is 60U/ml.
7. The method according to claim 2, wherein the enzyme activity in step (3) is 100U/ml, and the reaction temperature is 60 ℃.
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Citations (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN109609484A (en) * | 2018-12-06 | 2019-04-12 | 河北省微生物研究所 | The preparation method of compound depilation enzyme preparation and its application in losing hair or feathers containing small Mao import cattle hide |
CN109645211A (en) * | 2017-10-12 | 2019-04-19 | 孙强 | The extracting method of collagen in a kind of ox-hide |
CN110742824A (en) * | 2019-10-29 | 2020-02-04 | 南宁学院 | Preparation and application of cow hide composite extract |
CN111944866A (en) * | 2020-07-31 | 2020-11-17 | 青海瑞肽生物科技有限公司 | Method for preparing yak hide small molecule collagen peptide by continuous rotary evaporation, desolventizing and double enzymolysis |
CN113307860A (en) * | 2021-06-11 | 2021-08-27 | 四川大学 | Method for extracting keratin from cow hair recovered from tanning based on biological enzymolysis |
-
2021
- 2021-10-11 CN CN202111181236.6A patent/CN113862321A/en active Pending
Patent Citations (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN109645211A (en) * | 2017-10-12 | 2019-04-19 | 孙强 | The extracting method of collagen in a kind of ox-hide |
CN109609484A (en) * | 2018-12-06 | 2019-04-12 | 河北省微生物研究所 | The preparation method of compound depilation enzyme preparation and its application in losing hair or feathers containing small Mao import cattle hide |
CN110742824A (en) * | 2019-10-29 | 2020-02-04 | 南宁学院 | Preparation and application of cow hide composite extract |
CN111944866A (en) * | 2020-07-31 | 2020-11-17 | 青海瑞肽生物科技有限公司 | Method for preparing yak hide small molecule collagen peptide by continuous rotary evaporation, desolventizing and double enzymolysis |
CN113307860A (en) * | 2021-06-11 | 2021-08-27 | 四川大学 | Method for extracting keratin from cow hair recovered from tanning based on biological enzymolysis |
Non-Patent Citations (1)
Title |
---|
张骞等: "牛皮毛蛋白粉对AA肉鸡屠宰性能和肉品质的影响" * |
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