CN101353686B - Production method of haemachrome and decolorizing blood plasma albumen powder - Google Patents
Production method of haemachrome and decolorizing blood plasma albumen powder Download PDFInfo
- Publication number
- CN101353686B CN101353686B CN200810120963XA CN200810120963A CN101353686B CN 101353686 B CN101353686 B CN 101353686B CN 200810120963X A CN200810120963X A CN 200810120963XA CN 200810120963 A CN200810120963 A CN 200810120963A CN 101353686 B CN101353686 B CN 101353686B
- Authority
- CN
- China
- Prior art keywords
- protoheme
- production method
- enzymolysis
- water
- blood
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Fee Related
Links
- 239000000843 powder Substances 0.000 title claims abstract description 25
- 238000004519 manufacturing process Methods 0.000 title claims abstract description 14
- 210000002381 plasma Anatomy 0.000 title description 5
- 238000001556 precipitation Methods 0.000 claims abstract description 24
- 210000004369 blood Anatomy 0.000 claims abstract description 18
- 239000008280 blood Substances 0.000 claims abstract description 18
- 238000000034 method Methods 0.000 claims abstract description 18
- 238000001035 drying Methods 0.000 claims abstract description 14
- 238000002425 crystallisation Methods 0.000 claims abstract description 8
- 230000008025 crystallization Effects 0.000 claims abstract description 8
- 239000002994 raw material Substances 0.000 claims abstract description 6
- 102000001554 Hemoglobins Human genes 0.000 claims abstract description 3
- 108010054147 Hemoglobins Proteins 0.000 claims abstract description 3
- 238000003756 stirring Methods 0.000 claims description 33
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 claims description 30
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 28
- 239000000243 solution Substances 0.000 claims description 18
- 108091005804 Peptidases Proteins 0.000 claims description 14
- 102000035195 Peptidases Human genes 0.000 claims description 13
- 239000000047 product Substances 0.000 claims description 10
- 102000006395 Globulins Human genes 0.000 claims description 9
- 108010044091 Globulins Proteins 0.000 claims description 9
- 239000000706 filtrate Substances 0.000 claims description 9
- 235000013305 food Nutrition 0.000 claims description 9
- 230000001105 regulatory effect Effects 0.000 claims description 9
- 102000004190 Enzymes Human genes 0.000 claims description 8
- 108090000790 Enzymes Proteins 0.000 claims description 8
- 239000004365 Protease Substances 0.000 claims description 7
- 210000000601 blood cell Anatomy 0.000 claims description 7
- 239000000796 flavoring agent Substances 0.000 claims description 7
- 235000019634 flavors Nutrition 0.000 claims description 7
- 230000007062 hydrolysis Effects 0.000 claims description 6
- 238000006460 hydrolysis reaction Methods 0.000 claims description 6
- 230000002797 proteolythic effect Effects 0.000 claims description 6
- 244000144972 livestock Species 0.000 claims description 5
- 239000000203 mixture Substances 0.000 claims description 5
- -1 polyoxyethylene Polymers 0.000 claims description 5
- 229920000136 polysorbate Polymers 0.000 claims description 5
- 229940051841 polyoxyethylene ether Drugs 0.000 claims description 3
- 229920000056 polyoxyethylene ether Polymers 0.000 claims description 3
- 210000002784 stomach Anatomy 0.000 claims description 3
- 229920003171 Poly (ethylene oxide) Polymers 0.000 claims description 2
- 239000007864 aqueous solution Substances 0.000 claims description 2
- 238000002360 preparation method Methods 0.000 claims description 2
- 239000012460 protein solution Substances 0.000 claims description 2
- 238000012423 maintenance Methods 0.000 claims 1
- 102000004169 proteins and genes Human genes 0.000 abstract description 13
- 108090000623 proteins and genes Proteins 0.000 abstract description 13
- 239000006228 supernatant Substances 0.000 abstract description 9
- 102000018146 globin Human genes 0.000 abstract description 8
- 108060003196 globin Proteins 0.000 abstract description 8
- 239000000284 extract Substances 0.000 abstract description 4
- 238000011109 contamination Methods 0.000 abstract description 2
- 239000012535 impurity Substances 0.000 abstract description 2
- 244000144977 poultry Species 0.000 abstract description 2
- 239000002699 waste material Substances 0.000 abstract description 2
- 230000008021 deposition Effects 0.000 abstract 1
- 238000009776 industrial production Methods 0.000 abstract 1
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 18
- 238000001816 cooling Methods 0.000 description 10
- 238000009413 insulation Methods 0.000 description 9
- 241001465754 Metazoa Species 0.000 description 7
- 230000000694 effects Effects 0.000 description 7
- 229940088598 enzyme Drugs 0.000 description 7
- 238000005507 spraying Methods 0.000 description 7
- 239000012141 concentrate Substances 0.000 description 6
- 238000007710 freezing Methods 0.000 description 4
- 239000003960 organic solvent Substances 0.000 description 4
- ZWEHNKRNPOVVGH-UHFFFAOYSA-N 2-Butanone Chemical compound CCC(C)=O ZWEHNKRNPOVVGH-UHFFFAOYSA-N 0.000 description 3
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 102000019197 Superoxide Dismutase Human genes 0.000 description 3
- 108010012715 Superoxide dismutase Proteins 0.000 description 3
- 239000013543 active substance Substances 0.000 description 3
- 239000001768 carboxy methyl cellulose Substances 0.000 description 3
- 235000010948 carboxy methyl cellulose Nutrition 0.000 description 3
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 3
- 238000001914 filtration Methods 0.000 description 3
- 238000010438 heat treatment Methods 0.000 description 3
- 229940032362 superoxide dismutase Drugs 0.000 description 3
- RNMDNPCBIKJCQP-UHFFFAOYSA-N 5-nonyl-7-oxabicyclo[4.1.0]hepta-1,3,5-trien-2-ol Chemical compound C(CCCCCCCC)C1=C2C(=C(C=C1)O)O2 RNMDNPCBIKJCQP-UHFFFAOYSA-N 0.000 description 2
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 2
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 2
- 102000004506 Blood Proteins Human genes 0.000 description 2
- 108010017384 Blood Proteins Proteins 0.000 description 2
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 230000000996 additive effect Effects 0.000 description 2
- 238000000975 co-precipitation Methods 0.000 description 2
- 239000013078 crystal Substances 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 238000007750 plasma spraying Methods 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 238000000108 ultra-filtration Methods 0.000 description 2
- 102000009027 Albumins Human genes 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 241000272525 Anas platyrhynchos Species 0.000 description 1
- 241000271566 Aves Species 0.000 description 1
- 239000005996 Blood meal Substances 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 101000925662 Enterobacteria phage PRD1 Endolysin Proteins 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 206010018910 Haemolysis Diseases 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- DPDMMXDBJGCCQC-UHFFFAOYSA-N [Na].[Cl] Chemical compound [Na].[Cl] DPDMMXDBJGCCQC-UHFFFAOYSA-N 0.000 description 1
- 229960000583 acetic acid Drugs 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 235000013527 bean curd Nutrition 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 230000003749 cleanliness Effects 0.000 description 1
- IRXRGVFLQOSHOH-UHFFFAOYSA-L dipotassium;oxalate Chemical compound [K+].[K+].[O-]C(=O)C([O-])=O IRXRGVFLQOSHOH-UHFFFAOYSA-L 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 239000012362 glacial acetic acid Substances 0.000 description 1
- 150000003278 haem Chemical group 0.000 description 1
- 230000008588 hemolysis Effects 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- 239000002932 luster Substances 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 235000013372 meat Nutrition 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 235000008935 nutritious Nutrition 0.000 description 1
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
- 229920000053 polysorbate 80 Polymers 0.000 description 1
- 238000010298 pulverizing process Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 235000017557 sodium bicarbonate Nutrition 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- HRXKRNGNAMMEHJ-UHFFFAOYSA-K trisodium citrate Chemical compound [Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O HRXKRNGNAMMEHJ-UHFFFAOYSA-K 0.000 description 1
- 229940038773 trisodium citrate Drugs 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Landscapes
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
The invention discloses a manufacture method of hemachrome and discolored globin powder. The method comprises the steps that: after zymohydrolysis and equal point deposition of the raw material hemoglobin are carried out, the globin powder is prepared by supernatant by concentration and drying; and the hemachrome is prepared by precipitation and crystallization. The method of the invention can fully utilize the precious protein resources of poultry blood, jointly extract the hemachrome and eatable discolored globin powder and has not waste; the obtained discolored globin powder has good color, few impurities and high content of proteins. The method has the advantages of simple operation, low lost and clean without contamination, and being suitable for industrial production.
Description
Technical field
The present invention relates to the production method of protoheme and decolouring globulin powder, belong to food chemistry and biochemical field.
Background technology
Blood accounts for the 7%-8% of domestic birds and animals total protein concentration, and itself is nutritious, and protein content is up to about 20%, have " liquid meat " and title.Albumen has albumin, oxyphorase etc. in the blood, and wherein oxyphorase accounts for 70%-80%.But because the disgusting fishy smell of oxyphorase, except being used for blood bean curd on a small quantity, major part is dropped, and has not only wasted the protein resource of a large amount of preciousnesses but also has polluted ecotope.Oxyphorase is a homotetramer of being made up of four subunits, and each subunit contains a globin and one bonded protoheme with it.Wherein a kind of especially good hematinic of protoheme and important medicine chemical material.Therefore making full use of blood resource can protect environment again and can create good economic benefit by efficent use of resources, is subjected to domestic and international extensive concern.
Heme moiety and the globin part of fully rationally utilizing the artis of blood resource to be to separate oxyphorase have proposed a variety of separation methods now.Traditional method is utilized the organic solvent extracting, comprises the Glacial acetic acid extracting, the extracting of small molecules ketone such as acetone, methylethylketone etc., small molecular alcohol extracting such as methyl alcohol, ethanol etc.The organic solvent extracting is the extracting protoheme well, but needs very a large amount of organic solvents, and the protoheme that extracts 1kg needs the organic solvent of 800L-1000L, so inefficiency, brings huge inconvenience to operation, and also bigger to environmental hazard.U.S. Pat 4376727 proposes to adsorb protoheme with carboxymethyl cellulose, this method can solve protoheme and separate with globin, but what obtain is the mixture of protoheme and carboxymethyl cellulose, can not obtain pure protoheme, and carboxymethyl cellulose can not be regenerated, therefore this method cost is higher, has limited its use.Chinese patent ZL87101834 and ZL200610080022.9 use tensio-active agent as catalyzer crystallization protoheme, crystallization effect is better, but this method blood cell is easy to generate globin and protoheme co-precipitation in heat-processed, and address this problem just needs accurately control reaction process and utilization complicated operations equipment; The more important thing is that the protein powder that this method generates contains tensio-active agent, its person poultry safety's property is under suspicion.
Summary of the invention
The purpose of this invention is to provide a kind of simple to operate, with low cost, free of contamination protoheme and the decolouring globulin powder production method.
The production method of protoheme of the present invention and decolouring globulin powder, its step is as follows
1) the oxyphorase raw material is dissolved in water and stirs, the preparation mass concentration is at the 1%-20% haemoglobin aqueous solution, add proteolytic ferment then, the addition of proteolytic ferment is the 0.05%-10% of protein content in the hemoglobin solutions, regulate pH1.5～9.0, carry out enzymolysis under 25～70 ℃ of temperature, obtain enzymolysis solution, the enzymolysis extent control is at degree of hydrolysis 5%～40%;
2) the pH value of regulating enzymolysis solution is filtered to 2.0-6.0, collects the protoheme precipitation, gets the protoheme work in-process after the drying, and filtrate is not for containing the protein solution of protoheme;
3) add entry, concentrated hydrochloric acid and nonionogenic tenside in the protoheme work in-process, and stir, with dry weight basis, control protoheme work in-process: water: concentrated hydrochloric acid: the mass ratio of nonionogenic tenside is 1:10-200:0.1-10:0.2-5, continues to stir, and is heated to 70 ℃～95 ℃, centrifugal, collect the protoheme crystallization, wash after drying with water, get the finished product protoheme;
4) regulating step 2) pH of gained filtrate to neutral, concentrate, dry, globulin powder must decolour.
Among the present invention, said oxyphorase raw material is livestock blood or is oxyphorase, anticoagulated blood, clot, globulin powder or the blood cell of livestock blood processing.
Among the present invention, proteolytic ferment do not had special requirement, as long as the proteolytic enzyme of energy hydrolysis oxyphorase is all available, stomach en-, trypsinase as animal-origin, the papoid of plant origin, bromeline, microbe-derived animal proteolytic enzyme (production of Nanning Pang Bo bio tech ltd), food flavor enzyme or the like can be with any or its mixtures in above-mentioned.Because animal proteolytic enzyme and food flavor enzyme low price, easy to use and commercial production marketing, preferred animal proteolytic enzyme and food flavor enzyme, perhaps both mixed enzyme arranged.
In order to eliminate protease activities, to improve the quality of products, further feature of the present invention is the enzymolysis solution that step 1) obtains to be heated to keep 20 minutes inactivated proteases more than 90 ℃.
Among the present invention, said nonionogenic tenside is a kind of or its mixture among alkylphenol polyoxyethylene, fatty alcohol-polyoxyethylene ether, tween and the Si Pan.Because tween is extensive use of in daily life as foodstuff additive, its security obtains proof already, and preferred tween is as the tensio-active agent of crystallization protoheme.
The mass concentration of used concentrated hydrochloric acid is 35%～38% among the present invention.
The inventive method is before the crystallization protoheme, and the oxyphorase enzymolysis is micromolecular albumen, and thermostability improves, not can with the protoheme co-precipitation; By regulating the pH value of enzymolysis solution, most albumen is separated with protoheme, the protoheme crystallization just than being easier to, is reacted easier operation like this, and whole process does not need special equipment, does not need to add crystal seed yet.
The decolouring protein powder color and luster that the present invention obtains is good, and impurity is few, and protein content reaches about 95%, can be used for foodstuff additive.
The inventive method is simple to operate, with low cost, can utilize the oxyphorase that extracts behind the superoxide-dismutase (SOD) as raw material, unite and extract protoheme and food grade decolouring globulin powder, thereby realized the comprehensive utilization of livestock blood, do not have waste, cleanliness without any pollution is applicable to suitability for industrialized production.
Embodiment
Embodiment 1
Fresh pig blood 300L is collected in the slaughterhouse, adds the anti-freezing of 1kg Trisodium Citrate, after adding 300L water and stirring, adds the 1kg animal proteolytic enzyme, and the 1kg food flavor enzyme is regulated pH value to 7.5, is heated to 55 ℃, enzymolysis 48 hours.Heating enzymolysis solution to 90 ℃ insulation 20min inactivated proteases.Regulate the pH to 6.0 of enzymolysis solution after the cooling with hydrochloric acid, centrifugal then supernatant liquor and the precipitation of collecting respectively.Supernatant liquor is slightly yellow, regulates pH to 7 with sodium hydroxide solution, and triple effect concentrates, and spraying drying gets white protein powder 50kg; Precipitation (containing dry-matter 10kg approximately) adds 50L water and stirs, add the 1L mass concentration and be 38% concentrated hydrochloric acid, the 50kg polysorbas20, continue to stir, be heated to 70 ℃ then and stop to stir, insulation 30min, cooling back centrifugal collecting precipitation, dry after this precipitation washes with water finished product protoheme 1.5kg, purity is 91.3%, iron recovery is 91%.
Embodiment 2
Fresh ox blood 300L is collected in the slaughterhouse, adds the potassium oxalate anti-freezing, continuous centrifuge separate blood plasma 170L, blood cell 130L.The blood plasma spraying drying makes plasma protein powder 13kg.Add 200L water in the blood cell, stir 30 minutes haemolysis, regulate pH value to 9.0 with the NaOH solution of 1M, add the 4kg animal proteolytic enzyme, be heated to 65 ℃, enzymolysis to degree of hydrolysis reaches 40%.Enzymolysis solution boiled 30 minutes after enzymolysis was finished, and pH to 4.5 back press filtration is regulated with hydrochloric acid in the cooling back, gets filtrate 280kg, filter residue 50kg (about dry-matter 8kg).Filtrate is regulated pH to 6.5 with sodium hydroxide solution, ultrafiltration and concentration, and spraying drying makes protein powder 40kg.Filter residue adds water 1600L and stirs, add the 80L mass concentration and be 35% concentrated hydrochloric acid, 1.6kg tween 80, stir, being heated to 95 ℃ promptly has the protoheme crystal to separate out, to be crystallized fully after, centrifugal collection protoheme precipitation, protoheme precipitation washes with water, dry finished product protoheme 1.6kg, purity 90.3%.
Embodiment 3
Slaughterhouse chicken and duck blood condenses into clot, gets 500kg, and pulverizer adds 1000L water after pulverizing, and stirs, and regulates pH value to 7.0, adds the 60g animal proteolytic enzyme, is heated to 70 ℃, and enzymolysis 12 hours, degree of hydrolysis are 5.6%.Behind hydrochloric acid adjusting pH to 2.5, centrifugal clear liquid and the precipitation of collecting respectively, supernatant liquor is regulated pH to 5.5 with sodium hydroxide solution, and triple effect concentrates, and spraying drying gets white protein powder 105kg; Precipitation adds water 800L and stirs, and adds the 100L mass concentration and be 36% concentrated hydrochloric acid, 4kg polysorbas20,1kg Si Pan 60, stirs, be heated to 75 ℃ and stop to stir, 15min is left standstill in insulation, cooling, centrifugal collecting precipitation, precipitation dry after washing with water finished product protoheme 2.7kg, purity 90%.
Embodiment 4
Globulin powder 30kg adds 2500L water, stirs, and regulates pH value to 1.5, adds the 150g stomach en-, is heated to 37 ℃, enzymolysis 72 hours.Regulate pH to 6.0 with sodium hydroxide after enzymolysis is finished, press filtration gets filtrate 2400L.The filtrate triple effect concentrates, and spraying drying gets protein powder 26kg; Filter residue (the about 5kg of dry weight) adds water 500L and stirs, add the 40L mass concentration and be 35% concentrated hydrochloric acid, 25kg fatty alcohol-polyoxyethylene ether paregal O 15, stir, be heated to 88 ℃ and stop to stir, insulation 45min, the cooling back is centrifugal, collecting precipitation also washes with water, dry finished product protoheme 1.1kg, the purity 88% of getting.
Embodiment 5
Commercially available blood meal 200kg adds 800L water, stirs, regulate pH value to 7.8, add the 10kg food flavor enzyme, 25 ℃ of enzymolysis 12 hours, this moment, degree of hydrolysis was 5.3%, boil the 30min inactivated proteases, regulate pH4.5 with phosphoric acid, press filtration is collected filtrate respectively with filter residue, and filtrate is regulated pH to 7.0 with sodium hydrogen carbonate solution, ultrafiltration and concentration, spraying drying get white protein powder 160kg; Filter residue (the about 40kg of dry matter content) adds water 500L and stirs, add the 40L mass concentration and be 35% concentrated hydrochloric acid, the 50kg polysorbas20, the 50kg tween stirs, being heated to 95 ℃ stops to stir, insulation 5min, cooling back centrifugal collecting precipitation is after this precipitation washes with water, oven dry is finished product protoheme 5kg, purity 92%.
Embodiment 6
Anti-freezing pig blood 300L adds 300L water, stirs, and with salt acid for adjusting pH value to 5.7, adds the 1kg papoid, is heated to 58 ℃, enzymolysis 48 hours.The enzymolysis post-heating boils inactivated proteases, centrifugal supernatant liquor and the precipitation of collecting respectively in cooling back.Supernatant liquor is slightly yellow, regulates pH to 7 with sodium hydroxide solution, and triple effect concentrates, and spraying drying gets white protein powder 50kg; Precipitation adds 50L water and stirs, add the 4L mass concentration and be 35% concentrated hydrochloric acid, 10kg polyoxyethylene nonylphenol ether NP-10, continue to stir, be heated to 70 ℃ then and stop to stir, insulation 30min, cooling back centrifugal collecting precipitation, dry after this precipitation washes with water finished product protoheme 1.6kg, purity is 90%.
Embodiment 7
Anti-freezing pig blood 300L, the centrifugal blood cell 130L that gets, blood plasma 170L, the blood plasma spraying drying is made plasma protein powder 13kg, adds water 600L in the blood cell, after stirring 30min, add an amount of sodium-chlor, and with salt acid for adjusting pH value to 5.0,60 ℃ of insulation 30min, filter, the further processing of supernatant liquor can obtain superoxide-dismutase.Filter residue mainly is an oxyphorase, adds 600L water in the filter residue, regulates pH value to 7.0, adds 1kg conjugated protein lytic enzyme, and the 1kg food flavor enzyme is heated to 58 ℃, insulation enzymolysis 48 hours.Enzymolysis is finished post-heating and is boiled inactivated proteases, centrifugal supernatant liquor and the precipitation of collecting respectively in cooling back.Supernatant liquor is slightly yellow, and triple effect concentrates, and spraying drying gets white protein powder 45kg; Precipitation (containing dry-matter 10kg approximately) adds 50L water and stirs, add the 4L mass concentration and be 35% concentrated hydrochloric acid, 10kg polyoxyethylene nonylphenol ether NP-10, continue to stir, be heated to 70 ℃ then and stop to stir, insulation 60min, cooling back centrifugal collecting precipitation, dry after this precipitation washes with water finished product protoheme 1.5kg, purity is 91%.
Claims (5)
1. protoheme production method, its step is as follows:
1) the oxyphorase raw material is dissolved in water and stirs, the preparation mass concentration is at the 1%-20% haemoglobin aqueous solution, add proteolytic ferment then, the addition of proteolytic ferment is the 0.05%-10% of protein content in the hemoglobin solutions, regulate pH1.5～9.0, carry out enzymolysis under 25～70 ℃ of temperature, obtain enzymolysis solution, the enzymolysis extent control is at degree of hydrolysis 5%～40%;
2) the pH value of regulating enzymolysis solution is filtered to 2.0-6.0, collects the protoheme precipitation, gets the protoheme work in-process after the drying, and filtrate is not for containing the protein solution of protoheme;
3) add entry, concentrated hydrochloric acid and nonionogenic tenside in the protoheme work in-process, and stir, with dry weight basis, control protoheme work in-process: water: concentrated hydrochloric acid: the mass ratio of nonionogenic tenside is 1: 10-200: 0.1-10: 0.2-5, continue to stir, and be heated to 70 ℃～95 ℃, centrifugal, collect the protoheme crystallization, wash after drying with water, get the finished product protoheme.
2. protoheme production method according to claim 1 is characterized in that said oxyphorase raw material is livestock blood or is oxyphorase, anticoagulated blood, clot, globulin powder or the blood cell of livestock blood processing.
3. protoheme production method according to claim 1 is characterized in that said proteolytic ferment is a kind of or its mixture in stomach en-, trypsinase, papoid, bromeline and the food flavor enzyme.
4. according to the described protoheme production method of claim 1, it is characterized in that said nonionogenic tenside is a kind of or its mixture among alkylphenol polyoxyethylene, fatty alcohol-polyoxyethylene ether, tween and the Si Pan.
5. according to the described protoheme production method of claim 1, it is characterized in that the enzymolysis solution that step 1) obtains is heated to 20 minutes inactivated proteases of maintenance more than 90 ℃.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN200810120963XA CN101353686B (en) | 2008-09-09 | 2008-09-09 | Production method of haemachrome and decolorizing blood plasma albumen powder |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN200810120963XA CN101353686B (en) | 2008-09-09 | 2008-09-09 | Production method of haemachrome and decolorizing blood plasma albumen powder |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN101353686A CN101353686A (en) | 2009-01-28 |
| CN101353686B true CN101353686B (en) | 2011-09-21 |
Family
ID=40306703
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN200810120963XA Expired - Fee Related CN101353686B (en) | 2008-09-09 | 2008-09-09 | Production method of haemachrome and decolorizing blood plasma albumen powder |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN101353686B (en) |
Families Citing this family (14)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102125164B (en) * | 2010-10-29 | 2013-08-28 | 成都天屹生物科技有限公司 | Preparation method of pig blood fibrin polypeptide powder |
| CN102077901B (en) * | 2010-12-14 | 2013-04-24 | 成都宏安生物科技有限公司 | Swine hemoglobin enzymolysis and decoloration method |
| CN103396418A (en) * | 2013-07-23 | 2013-11-20 | 甘肃农业大学 | Enzymatic preparation method of hemin by using dried yak blood as raw material |
| CN104256199A (en) * | 2014-10-16 | 2015-01-07 | 浙江索纳克生物科技有限公司 | Loach feed added with porcine hemoglobin powder |
| CN104256198B (en) * | 2014-10-16 | 2016-08-31 | 浙江索纳克生物科技有限公司 | A kind of soft-shelled turtle feed adding proteinic powder of porcine |
| CN105385735A (en) * | 2015-11-25 | 2016-03-09 | 重庆三零三科技有限公司 | Preparation method of chicken blood antimicrobial peptide |
| CN106261817A (en) * | 2016-08-11 | 2017-01-04 | 安徽省农业科学院农产品加工研究所 | A kind of efficient enzymolysis Application way of Sanguis sus domestica |
| CN106261816A (en) * | 2016-08-11 | 2017-01-04 | 安徽省农业科学院农产品加工研究所 | A kind of Sanguis sus domestica source iron supplementary intermediate and the preparation method of finished product thereof |
| CN106107574A (en) * | 2016-08-11 | 2016-11-16 | 安徽省农业科学院农产品加工研究所 | A kind of preparation method of Sanguis sus domestica source compound microelement supplement |
| CN106554979A (en) * | 2016-11-18 | 2017-04-05 | 安徽菁硕科技有限公司 | A kind of method of the production haemachrome that combined with acid acetone extraction by enzymatic isolation method |
| CN110183497A (en) * | 2019-07-17 | 2019-08-30 | 甘肃养泰和生物科技有限公司 | A method of purifying hemin from animal blood cell |
| CN114592029A (en) * | 2022-03-09 | 2022-06-07 | 山西勰成生物科技有限公司 | Preparation method of fermented enzymatic decolorized hemoglobin |
| CN115386000A (en) * | 2022-09-14 | 2022-11-25 | 江苏省农业科学院 | Method for preparing decolorized peptide and heme peptide from poultry blood cell processing byproducts |
| CN117886826B (en) * | 2023-12-13 | 2024-09-24 | 甘肃养泰和生物科技有限公司 | Method for extracting methemoglobin by heating and pressurizing |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1300732A (en) * | 2000-12-28 | 2001-06-27 | 内蒙古草原兴发股份有限公司 | Process for extracting heme from animal blood |
| CN1450073A (en) * | 2003-04-11 | 2003-10-22 | 王利忠 | Process for extracting and puritying haem |
| CN1844123A (en) * | 2006-04-28 | 2006-10-11 | 新疆科丽生物技术有限公司 | Process for extracting protohemin by using surfactant |
| CN101194665A (en) * | 2007-11-30 | 2008-06-11 | 华南理工大学 | Apocytochrome porcine hemoglobin enzymolysis matter and method of preparing protoheme peptide |
-
2008
- 2008-09-09 CN CN200810120963XA patent/CN101353686B/en not_active Expired - Fee Related
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1300732A (en) * | 2000-12-28 | 2001-06-27 | 内蒙古草原兴发股份有限公司 | Process for extracting heme from animal blood |
| CN1450073A (en) * | 2003-04-11 | 2003-10-22 | 王利忠 | Process for extracting and puritying haem |
| CN1844123A (en) * | 2006-04-28 | 2006-10-11 | 新疆科丽生物技术有限公司 | Process for extracting protohemin by using surfactant |
| CN101194665A (en) * | 2007-11-30 | 2008-06-11 | 华南理工大学 | Apocytochrome porcine hemoglobin enzymolysis matter and method of preparing protoheme peptide |
Non-Patent Citations (3)
| Title |
|---|
| 房学军，等，.以猪血为原料制备亚铁血红素肽工艺条件的研究.《大连轻工业学院学报》.2007,第26卷(第2期),101-103. * |
| 瞿桂香,等,.不同蛋白酶水解猪血红蛋白制备血红素的对比研究.《江西农业学报》.2007,第19卷(第7期),92-93. * |
| 瞿桂香，等，.血红素制备工艺研究进展.《中央民族大学学报(自然科学版)》.2007,第16卷(第1期),19-22. * |
Also Published As
| Publication number | Publication date |
|---|---|
| CN101353686A (en) | 2009-01-28 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN101353686B (en) | Production method of haemachrome and decolorizing blood plasma albumen powder | |
| CN101307348B (en) | Method for preparing undenatured collagen from fish scale of fresh water fish | |
| CN102154424B (en) | Process for preparing micro-molecular fish scale collagen peptides | |
| CN102132857B (en) | Production process for preparing hot reaction shrimp-taste essence with macrobrachium shells | |
| CN100548150C (en) | The preparation method of coconut extractive | |
| CN102308903B (en) | Industrialized production method of corn polypeptide | |
| CN101766282B (en) | Process method for simultaneously extracting soybean function factor and therapeutic factor from bean pulp | |
| CN102732585B (en) | New method for purifying fructo oligosaccharide in chicory | |
| CN103652307B (en) | Method for extracting leaf proteins from broussonetia papyrifera leaf dry powder and comprehensive utilization of waste | |
| CN101455398B (en) | Soya-dregs water soluble diet fiber preparation method using nano filtration and spray-drying method | |
| CN101884412B (en) | Method for preparing natural compound calcium amino acid chelate | |
| CN108391747A (en) | A kind of preparation method of small molecular soybean protein peptide | |
| CN102887947A (en) | Process for producing micromolecule hemepeptide, heme iron and plasma proteins by using duck blood as raw material | |
| CN1896267B (en) | Preparation of depressor peptide by silkworm chrysalis | |
| CN110256603A (en) | A kind of-two step enzyme method coupling of shrimp and crab shells hydro-thermal prepares the methods and applications of chitin and chitosan | |
| CN106008739A (en) | Preparation method of oyster polysaccharide | |
| CN1957736B (en) | Method for producing soyabean protein (peptide) powder with NSI value equal to 100% | |
| CN101564142A (en) | Oyster juice manufacturing method | |
| CN101575369B (en) | Technique for separating and preparing rapeseed protein cogenerating rapeseed polyoses from the low-temperature cold pressing rapeseed dregs film | |
| CN102150741B (en) | Method for preparing lactalbumin hydrolysate by utilizing yak milk | |
| CN107440128A (en) | The preparation method and edible mushroom dietary fiber of a kind of edible mushroom dietary fiber | |
| CN102558377A (en) | Preparation method of soybean polysaccharide gum | |
| CN105146315A (en) | Preparation process of low-protein rice and rice peptide | |
| CN102018092B (en) | Method for extracting protein from maize germ dregs | |
| CN112142519A (en) | Utilize equipment of abandonment eggshell protein preparation amino acid calcium magnesium liquid fertilizer |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| C06 | Publication | ||
| PB01 | Publication | ||
| C10 | Entry into substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| C14 | Grant of patent or utility model | ||
| GR01 | Patent grant | ||
| ASS | Succession or assignment of patent right |
Owner name: FUSHUN DANYANG BIOTECHNOLOGY CO., LTD. Free format text: FORMER OWNER: ZHEJIANG UNIVERSITY Effective date: 20130123 |
|
| C41 | Transfer of patent application or patent right or utility model | ||
| COR | Change of bibliographic data |
Free format text: CORRECT: ADDRESS; FROM: 310027 HANGZHOU, ZHEJIANG PROVINCE TO: 113109 FUSHUN, LIAONING PROVINCE |
|
| TR01 | Transfer of patent right |
Effective date of registration: 20130123 Address after: 113109 Fushun City, Liaoning province Dongzhou District Pan Xiang Shi Fu Cun Patentee after: Fushun Danyang biological science and Technology Co Ltd Address before: 310027 Hangzhou, Zhejiang Province, Xihu District, Zhejiang Road, No. 38, No. Patentee before: Zhejiang University |
|
| C56 | Change in the name or address of the patentee | ||
| CP01 | Change in the name or title of a patent holder |
Address after: 113109 Fushun City, Liaoning province Dongzhou District Pan Xiang Shi Fu Cun Patentee after: Danyang biological Polytron Technologies Inc of Fushun Address before: 113109 Fushun City, Liaoning province Dongzhou District Pan Xiang Shi Fu Cun Patentee before: Fushun Danyang biological science and Technology Co Ltd |
|
| CF01 | Termination of patent right due to non-payment of annual fee |
Granted publication date: 20110921 Termination date: 20150909 |
|
| EXPY | Termination of patent right or utility model |