NO860075L - PROCESSING OF RAAP PROTEINS. - Google Patents
PROCESSING OF RAAP PROTEINS. Download PDFInfo
- Publication number
- NO860075L NO860075L NO860075A NO860075A NO860075L NO 860075 L NO860075 L NO 860075L NO 860075 A NO860075 A NO 860075A NO 860075 A NO860075 A NO 860075A NO 860075 L NO860075 L NO 860075L
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- protein
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- nucleic acid
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- 102000004169 proteins and genes Human genes 0.000 title claims description 13
- 108090000623 proteins and genes Proteins 0.000 title claims description 13
- 238000012545 processing Methods 0.000 title description 3
- 150000007523 nucleic acids Chemical class 0.000 claims description 21
- 108020004707 nucleic acids Proteins 0.000 claims description 20
- 102000039446 nucleic acids Human genes 0.000 claims description 20
- 101710163270 Nuclease Proteins 0.000 claims description 16
- 108010077805 Bacterial Proteins Proteins 0.000 claims description 11
- 108090000790 Enzymes Proteins 0.000 claims description 9
- 102000004190 Enzymes Human genes 0.000 claims description 9
- 102000004861 Phosphoric Diester Hydrolases Human genes 0.000 claims description 7
- 108090001050 Phosphoric Diester Hydrolases Proteins 0.000 claims description 7
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 7
- 235000019750 Crude protein Nutrition 0.000 claims description 6
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims description 5
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 claims description 4
- 235000019728 animal nutrition Nutrition 0.000 claims description 3
- 239000000758 substrate Substances 0.000 claims description 3
- 229910021529 ammonia Inorganic materials 0.000 claims description 2
- 230000000813 microbial effect Effects 0.000 claims description 2
- 239000003960 organic solvent Substances 0.000 claims description 2
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 claims 4
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 claims 2
- 238000003776 cleavage reaction Methods 0.000 claims 2
- WGCNASOHLSPBMP-UHFFFAOYSA-N hydroxyacetaldehyde Natural products OCC=O WGCNASOHLSPBMP-UHFFFAOYSA-N 0.000 claims 2
- 230000007017 scission Effects 0.000 claims 2
- 108010058643 Fungal Proteins Proteins 0.000 claims 1
- 241000004089 Megaselia clara Species 0.000 claims 1
- 238000000605 extraction Methods 0.000 claims 1
- 229920002477 rna polymer Polymers 0.000 description 17
- 239000002773 nucleotide Substances 0.000 description 14
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 12
- 238000006460 hydrolysis reaction Methods 0.000 description 12
- 125000003729 nucleotide group Chemical group 0.000 description 12
- 230000007062 hydrolysis Effects 0.000 description 11
- 238000000034 method Methods 0.000 description 10
- 239000002028 Biomass Substances 0.000 description 9
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 9
- 235000018102 proteins Nutrition 0.000 description 9
- 229940088598 enzyme Drugs 0.000 description 7
- 230000000694 effects Effects 0.000 description 5
- 230000000968 intestinal effect Effects 0.000 description 5
- 239000000203 mixture Substances 0.000 description 5
- 241001465754 Metazoa Species 0.000 description 4
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 4
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 4
- 235000019621 digestibility Nutrition 0.000 description 4
- 230000004151 fermentation Effects 0.000 description 4
- 150000002632 lipids Chemical class 0.000 description 4
- 238000004519 manufacturing process Methods 0.000 description 4
- 244000005700 microbiome Species 0.000 description 4
- 235000016709 nutrition Nutrition 0.000 description 4
- 210000000813 small intestine Anatomy 0.000 description 4
- 235000011121 sodium hydroxide Nutrition 0.000 description 4
- 241000287828 Gallus gallus Species 0.000 description 3
- 235000010469 Glycine max Nutrition 0.000 description 3
- KWYUFKZDYYNOTN-UHFFFAOYSA-M Potassium hydroxide Chemical compound [OH-].[K+] KWYUFKZDYYNOTN-UHFFFAOYSA-M 0.000 description 3
- 230000037396 body weight Effects 0.000 description 3
- 150000001720 carbohydrates Chemical class 0.000 description 3
- 235000014633 carbohydrates Nutrition 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 238000000855 fermentation Methods 0.000 description 3
- 238000004128 high performance liquid chromatography Methods 0.000 description 3
- 230000004060 metabolic process Effects 0.000 description 3
- 235000015097 nutrients Nutrition 0.000 description 3
- 108091033319 polynucleotide Proteins 0.000 description 3
- 102000040430 polynucleotide Human genes 0.000 description 3
- 239000002157 polynucleotide Substances 0.000 description 3
- 239000000047 product Substances 0.000 description 3
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- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 2
- 239000004470 DL Methionine Substances 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 2
- 241000589341 Methylomonas clara Species 0.000 description 2
- 241000209140 Triticum Species 0.000 description 2
- 235000021307 Triticum Nutrition 0.000 description 2
- POJWUDADGALRAB-UHFFFAOYSA-N allantoin Chemical compound NC(=O)NC1NC(=O)NC1=O POJWUDADGALRAB-UHFFFAOYSA-N 0.000 description 2
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 2
- 235000001014 amino acid Nutrition 0.000 description 2
- 229940024606 amino acid Drugs 0.000 description 2
- 150000001413 amino acids Chemical class 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
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- FFEARJCKVFRZRR-UHFFFAOYSA-N methionine Chemical compound CSCCC(N)C(O)=O FFEARJCKVFRZRR-UHFFFAOYSA-N 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- 235000006109 methionine Nutrition 0.000 description 2
- QJGQUHMNIGDVPM-UHFFFAOYSA-N nitrogen group Chemical group [N] QJGQUHMNIGDVPM-UHFFFAOYSA-N 0.000 description 2
- 150000002978 peroxides Chemical class 0.000 description 2
- 150000003212 purines Chemical class 0.000 description 2
- 150000003230 pyrimidines Chemical class 0.000 description 2
- 230000000384 rearing effect Effects 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- LSNNMFCWUKXFEE-UHFFFAOYSA-L sulfite Chemical compound [O-]S([O-])=O LSNNMFCWUKXFEE-UHFFFAOYSA-L 0.000 description 2
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- HFGHRUCCKVYFKL-UHFFFAOYSA-N 4-ethoxy-2-piperazin-1-yl-7-pyridin-4-yl-5h-pyrimido[5,4-b]indole Chemical compound C1=C2NC=3C(OCC)=NC(N4CCNCC4)=NC=3C2=CC=C1C1=CC=NC=C1 HFGHRUCCKVYFKL-UHFFFAOYSA-N 0.000 description 1
- QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 description 1
- AEOBEOJCBAYXBA-UHFFFAOYSA-N A2P5P Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(O)=O)C(O)C1OP(O)(O)=O AEOBEOJCBAYXBA-UHFFFAOYSA-N 0.000 description 1
- POJWUDADGALRAB-PVQJCKRUSA-N Allantoin Natural products NC(=O)N[C@@H]1NC(=O)NC1=O POJWUDADGALRAB-PVQJCKRUSA-N 0.000 description 1
- KWTQSFXGGICVPE-WCCKRBBISA-N Arginine hydrochloride Chemical compound Cl.OC(=O)[C@@H](N)CCCN=C(N)N KWTQSFXGGICVPE-WCCKRBBISA-N 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- IERHLVCPSMICTF-XVFCMESISA-N CMP group Chemical group P(=O)(O)(O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)N1C(=O)N=C(N)C=C1)O)O IERHLVCPSMICTF-XVFCMESISA-N 0.000 description 1
- 241000271538 Crotalus durissus Species 0.000 description 1
- 241000544061 Cuculus canorus Species 0.000 description 1
- HMFHBZSHGGEWLO-SOOFDHNKSA-N D-ribofuranose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H]1O HMFHBZSHGGEWLO-SOOFDHNKSA-N 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
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- 102000002322 Egg Proteins Human genes 0.000 description 1
- 108010000912 Egg Proteins Proteins 0.000 description 1
- 235000019733 Fish meal Nutrition 0.000 description 1
- 230000005526 G1 to G0 transition Effects 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- -1 NH^OH Substances 0.000 description 1
- 102100021969 Nucleotide pyrophosphatase Human genes 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- 241000228153 Penicillium citrinum Species 0.000 description 1
- PYMYPHUHKUWMLA-LMVFSUKVSA-N Ribose Natural products OC[C@@H](O)[C@@H](O)[C@@H](O)C=O PYMYPHUHKUWMLA-LMVFSUKVSA-N 0.000 description 1
- 241000295644 Staphylococcaceae Species 0.000 description 1
- 241001655322 Streptomycetales Species 0.000 description 1
- LEHOTFFKMJEONL-UHFFFAOYSA-N Uric Acid Chemical compound N1C(=O)NC(=O)C2=C1NC(=O)N2 LEHOTFFKMJEONL-UHFFFAOYSA-N 0.000 description 1
- TVWHNULVHGKJHS-UHFFFAOYSA-N Uric acid Natural products N1C(=O)NC(=O)C2NC(=O)NC21 TVWHNULVHGKJHS-UHFFFAOYSA-N 0.000 description 1
- DJJCXFVJDGTHFX-UHFFFAOYSA-N Uridinemonophosphate Natural products OC1C(O)C(COP(O)(O)=O)OC1N1C(=O)NC(=O)C=C1 DJJCXFVJDGTHFX-UHFFFAOYSA-N 0.000 description 1
- 241000235015 Yarrowia lipolytica Species 0.000 description 1
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 238000005903 acid hydrolysis reaction Methods 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- UDMBCSSLTHHNCD-KQYNXXCUSA-N adenosine 5'-monophosphate Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]1O UDMBCSSLTHHNCD-KQYNXXCUSA-N 0.000 description 1
- 230000000274 adsorptive effect Effects 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- 150000001447 alkali salts Chemical class 0.000 description 1
- 229960000458 allantoin Drugs 0.000 description 1
- HMFHBZSHGGEWLO-UHFFFAOYSA-N alpha-D-Furanose-Ribose Natural products OCC1OC(O)C(O)C1O HMFHBZSHGGEWLO-UHFFFAOYSA-N 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 208000010668 atopic eczema Diseases 0.000 description 1
- 230000003139 buffering effect Effects 0.000 description 1
- AXCZMVOFGPJBDE-UHFFFAOYSA-L calcium dihydroxide Chemical compound [OH-].[OH-].[Ca+2] AXCZMVOFGPJBDE-UHFFFAOYSA-L 0.000 description 1
- 239000000920 calcium hydroxide Substances 0.000 description 1
- 235000011116 calcium hydroxide Nutrition 0.000 description 1
- 229910001861 calcium hydroxide Inorganic materials 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 239000007857 degradation product Substances 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 229940079919 digestives enzyme preparation Drugs 0.000 description 1
- 235000014103 egg white Nutrition 0.000 description 1
- 210000000969 egg white Anatomy 0.000 description 1
- 235000013601 eggs Nutrition 0.000 description 1
- 239000004467 fishmeal Substances 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 239000007789 gas Substances 0.000 description 1
- 210000003736 gastrointestinal content Anatomy 0.000 description 1
- RQFCJASXJCIDSX-UUOKFMHZSA-N guanosine 5'-monophosphate Chemical compound C1=2NC(N)=NC(=O)C=2N=CN1[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]1O RQFCJASXJCIDSX-UUOKFMHZSA-N 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 238000009655 industrial fermentation Methods 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- 244000144972 livestock Species 0.000 description 1
- 159000000003 magnesium salts Chemical class 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 239000002207 metabolite Substances 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 230000035764 nutrition Effects 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 210000004798 organs belonging to the digestive system Anatomy 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 239000012188 paraffin wax Substances 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 229910052698 phosphorus Inorganic materials 0.000 description 1
- 238000009372 pisciculture Methods 0.000 description 1
- 235000011118 potassium hydroxide Nutrition 0.000 description 1
- 244000144977 poultry Species 0.000 description 1
- 235000013594 poultry meat Nutrition 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 238000002203 pretreatment Methods 0.000 description 1
- 238000011165 process development Methods 0.000 description 1
- 230000020978 protein processing Effects 0.000 description 1
- 239000013558 reference substance Substances 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000007086 side reaction Methods 0.000 description 1
- 108010027322 single cell proteins Proteins 0.000 description 1
- 239000003998 snake venom Substances 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 238000001694 spray drying Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 229940116269 uric acid Drugs 0.000 description 1
- DJJCXFVJDGTHFX-XVFCMESISA-N uridine 5'-monophosphate Chemical compound O[C@@H]1[C@H](O)[C@@H](COP(O)(O)=O)O[C@H]1N1C(=O)NC(=O)C=C1 DJJCXFVJDGTHFX-XVFCMESISA-N 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
- 150000003722 vitamin derivatives Chemical class 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y301/00—Hydrolases acting on ester bonds (3.1)
- C12Y301/04—Phosphoric diester hydrolases (3.1.4)
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K10/00—Animal feeding-stuffs
- A23K10/10—Animal feeding-stuffs obtained by microbiological or biochemical processes
- A23K10/14—Pretreatment of feeding-stuffs with enzymes
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K10/00—Animal feeding-stuffs
- A23K10/10—Animal feeding-stuffs obtained by microbiological or biochemical processes
- A23K10/16—Addition of microorganisms or extracts thereof, e.g. single-cell proteins, to feeding-stuff compositions
-
- 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
- C12N1/00—Microorganisms, e.g. protozoa; Compositions thereof; Processes of propagating, maintaining or preserving microorganisms or compositions thereof; Processes of preparing or isolating a composition containing a microorganism; Culture media therefor
- C12N1/08—Reducing the nucleic acid content
-
- 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
- C12P19/00—Preparation of compounds containing saccharide radicals
- C12P19/26—Preparation of nitrogen-containing carbohydrates
- C12P19/28—N-glycosides
- C12P19/30—Nucleotides
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Health & Medical Sciences (AREA)
- Zoology (AREA)
- Organic Chemistry (AREA)
- Microbiology (AREA)
- Wood Science & Technology (AREA)
- Biochemistry (AREA)
- Biotechnology (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Polymers & Plastics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biomedical Technology (AREA)
- General Health & Medical Sciences (AREA)
- General Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Physiology (AREA)
- Animal Husbandry (AREA)
- Virology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Medicinal Chemistry (AREA)
- Tropical Medicine & Parasitology (AREA)
- General Chemical & Material Sciences (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Feed For Specific Animals (AREA)
- Fodder In General (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Description
Industrielle fermenteringsprosesser til fremstilling av biomasse for foringsmidler har en lang tradisjon (gjærfremstiIl-ing av sulfittavlut) og var i de siste år gjenstand for nye fremgangsmåteutviklinger (bakteriefremstilling på basis metanol). Industrial fermentation processes for the production of biomass for feedstocks have a long tradition (yeast production of sulphite leachate) and in recent years have been the subject of new process developments (bacterial production based on methanol).
Biomasser fra fermenteringsfremgangsmåte for anvendelses-området av dyreernæring som kalv- og fjærkregjøing, fiske-oppdrett, rughønefor, svinegjøing og husdyrfor, betegnes også som bioproteiner, og inneholder alt etter typen av mikroorganismen (gjær, bakterie), den anvendte karbonkilde (sulfittavlut, etanol, metanol, parafinfraksjoner) samt Biomasses from the fermentation process for the application area of animal nutrition such as calf and poultry rearing, fish farming, rye hen feed, pig rearing and livestock feed are also referred to as bioproteins, and contain, depending on the type of microorganism (yeast, bacteria), the carbon source used (sulphite leachate, ethanol , methanol, paraffin fractions) as well as
typen av fermenterings- og opparbeidelsesteknologi forskjellige mengder av proteiner, lipider, karbohydrater og nukleinsyrer /ribonukleinsyrer (RNS) og desoksyribonuklein-syrer, (DNS2?. the type of fermentation and processing technology different amounts of proteins, lipids, carbohydrates and nucleic acids /ribonucleic acids (RNS) and deoxyribonucleic acids, (DNS2?.
Mens næringsverdien av biomassen i første rekke er en funk-sjon av proteininnholdet og aminosyresammensetning og -disponerbarhet, og lipid- og karbohydratfraksjonen bidrar til energibalanse av den samlede forblanding, er nuklein-syredelen en bikomponent, hvis nitrogendel ikke eller bare i liten del kan nyttes til oppbygging av kroppsstoff. While the nutritional value of the biomass is primarily a function of the protein content and amino acid composition and availability, and the lipid and carbohydrate fraction contributes to the energy balance of the overall premix, the nucleic acid part is a secondary component, the nitrogen part of which cannot or only to a small extent be used for building up body material.
Avhengig av dyretypespesifikt stoffskifte oppbygges de nitrogenholdige bygges£eder av RNS og DNS (puriner, pyrimidiner) til metabolitter, som utskilles i form av godt vannoppløselig (allantoin) eller dårlig oppløselige produkter (urinsyre). Depending on the animal type-specific metabolism, the nitrogenous building blocks of RNS and DNS (purines, pyrimidines) are built up into metabolites, which are excreted in the form of highly water-soluble (allantoin) or poorly soluble products (uric acid).
Derfor begrenses nukleininnholdet i forblandinger for å unn-gå forhøyede stoffskifte- eller organbelastninger ved nukleinsyreavbyggingsprodukter. En sammenheng mellom nukleinsyreinnhold og nutritiv disponerbarhet (fordøyelig-het og tålbarhet) av bioproteiner i avhengighet av nuklein-syrenes (RNS og DNS) molekylvekt ble derimot hittil ikke omtalt. Therefore, the nucleic content in premixes is limited in order to avoid increased metabolic or organ loads due to nucleic acid degradation products. However, a connection between nucleic acid content and nutritional availability (digestibility and tolerability) of bioproteins depending on the molecular weight of the nucleic acids (RNS and DNS) has not been discussed so far.
Det ble nå funnet at nukleinsyrer ved siden av de ovennevnte effekter i stoffskiftet, som fremkommer av den kjemiske sammensetning av RNS resp. DNS (ribose, desoksyribose, fosforsyre, puriner, pyrimidiner) har en hittil ukjent negativ innvirkning på fordøyeligheten av bioproteiner, som for-årsakes av disse forbindelsers høye molekylvekt. It was now found that nucleic acids, in addition to the above-mentioned effects in the metabolism, which arise from the chemical composition of RNS resp. DNS (ribose, deoxyribose, phosphoric acid, purines, pyrimidines) has a hitherto unknown negative effect on the digestibility of bioproteins, which is caused by the high molecular weight of these compounds.
Spesielt polynukleotidene av DNS oppnår molekylvektområder fra 1.10 5 til 1.10 7, mens de kortere polynukleotidstrenger av RNS har molekyvekter på 5.000-50.000. The polynucleotides of DNS in particular achieve molecular weight ranges from 1.10 5 to 1.10 7 , while the shorter polynucleotide strands of RNS have molecular weights of 5,000-50,000.
Innvirkningen av molekylvekten av nukleinsyre på fordøye-lighet og tålbarhet av bioproteiner ble for første gang iakttatt i foringsforsøk på kyllinger og derav utviklet en undersøkelsesmodell for bestemmelse av molekylvekteffekten på fordøyelsesorganene. The impact of the molecular weight of nucleic acid on the digestibility and tolerability of bioproteins was observed for the first time in feeding experiments on chickens, and from this a research model was developed for determining the molecular weight effect on the digestive organs.
Den nef^ jtive effekt av høymolekylære nukleinsyrer i forblandinger bevirker konsentrasjonsavhengig en økning av tarmvekten i forhold til legemsvekten og derved en generell nedgang av stoffskiftet ved negativ endring av resoropsjons-prosessene. Dårligere vekstresultater og dermed en tydelig mindre proteinverdighet av nukleinsyreholdigébioproteiner er de primært iakttatte følger. The negative effect of high-molecular nucleic acids in premixes causes a concentration-dependent increase in the intestinal weight in relation to the body weight and thereby a general decrease in metabolism due to a negative change in the resorption processes. Poorer growth results and thus a distinctly lower protein value of nucleic acid-holding bioproteins are the primarily observed consequences.
Det er kjent av molekylvekten av RNS ogDNS lar seg nedsette ved hjelp av pH-verdi, temperatur og saltinnhold i vandig miljø. Mens RNS hydrolyserer i alkalisk område kan DNS avbygges under sure betingelser. Hydrolysegraden (nedsettelse av molekylvekt) er derved avhengig av de valgte betingelser, idet selv ved høyere temperaturer (80-90°C) og pH-verdier på 8-11 for RNS resp. pH 1,5-5,4 for DNS og be-handlingstider på 1-4 timer bare oppnås en partiell hydrolyse til oligonukleotider med molekylvekter på 500-10.000 ved RNS og 1000-40.999 ved DNS. Derved påvirkes dessuten de andre bestanddeler av bioproteinet, spesielt proteinene, negativt (farge, smak, denaturering, saltinnhold, racemiser-ing) og derved nedsettes den nutritive verdi. Dessuten til- fredsstiller ikke den partielle hydrolyse av RNS og DNS for å eliminere deres ulemper på fordøyeligheten. It is known that the molecular weight of RNS and DNS can be reduced by means of pH value, temperature and salt content in an aqueous environment. While RNS hydrolyzes in an alkaline range, DNS can be degraded under acidic conditions. The degree of hydrolysis (reduction in molecular weight) is thereby dependent on the chosen conditions, as even at higher temperatures (80-90°C) and pH values of 8-11 for RNS resp. pH 1.5-5.4 for DNS and treatment times of 1-4 hours only achieve partial hydrolysis to oligonucleotides with molecular weights of 500-10,000 for RNS and 1,000-40,999 for DNS. In addition, the other components of the bioprotein, especially the proteins, are thereby negatively affected (colour, taste, denaturation, salt content, racemisation) and thereby the nutritional value is reduced. Moreover, the partial hydrolysis of RNS and DNS is not satisfactory in order to eliminate their drawbacks on digestibility.
Ulempene av høymolekylære polynukleotider på tålbarheten av råbioprotiner oppheves ifølge oppfinnelsen ved at RNS og DNS avbygges best mulig ved hjelp av enzymer under milde betingelser, fortrinnsvis kvantitativt, til oligomere, fortrinnsvis monomere, nukleotider. According to the invention, the disadvantages of high-molecular-weight polynucleotides on the tolerability of raw bioproteins are eliminated by RNS and DNS being broken down as best as possible with the help of enzymes under mild conditions, preferably quantitatively, into oligomeric, preferably monomeric, nucleotides.
Oppfinnelsen vedrører derfor anvendelsen av nukleinsyrerike råproteiner, hvori de høymolekylære nukleinsyrer ble spaltet ved behandling med nukleaser til dyreernæring. The invention therefore relates to the use of crude proteins rich in nucleic acids, in which the high molecular weight nucleic acids were cleaved by treatment with nucleases for animal nutrition.
Som råbioproteiner kommer det i første rekke i betraktning mikrobielle proteiner, fremfor alt enkeltcelleproteiner som gjær og spesielt bakterieproteiner, men også nukleinsyrerike andre materialer som fiskemel eller indreegg. As crude bioproteins, microbial proteins are primarily considered, above all single-cell proteins such as yeast and especially bacterial proteins, but also other nucleic acid-rich materials such as fishmeal or internal eggs.
y y
De anvendte enzymer er nukleaser, fremfor alt fosfordiester-aser, fortrinnsvis 5<1->fosfodiesteraser, som hydrolyser RNS o og DNS til de tilsvarende monomere 3'- resp. 5'-nukleotider. The enzymes used are nucleases, above all phosphodiesterases, preferably 5<1->phosphodiesterases, which hydrolyze RNS o and DNS to the corresponding monomers 3'- or 5' nucleotides.
Fosfodiesterasene er vidt utbredt i naturen og lar seg så vel isolere fra mikroorganismer (streptomyceter, penicillin;,! stafylokokker), dyriske.celler eller produkter (storfehjerte, storfe- og kalvemilt, slangegift) eller planteceller (hvete-kimer). The phosphodiesterases are widespread in nature and can be isolated from microorganisms (streptomycetes, penicillin, staphylococci), animal cells or products (bovine heart, bovine and calf spleen, snake venom) or plant cells (wheat germ).
Da fosfodiesterasene bare hydrolyserer den molekylare struk-tur av RNS og DNS, opptrer ingen uønskede bireaksjoner på As the phosphodiesterases only hydrolyze the molecular structure of RNS and DNS, no unwanted side reactions occur on
de andre biokomponentene (lipider, karbohydrater, eggehvite). the other biocomponents (lipids, carbohydrates, egg white).
Fosfodiesterasene kan trenge gjennom celleveggen av mikroorganismer, hvorfor det ikke er nødvendig med en spesiell forbehandling av råbioproteinet for den enzymatiske hydrolyse av RNS og DNS. Derfor lar dette fremgangsmåtetrinn seg integrere i ethvert opparbeidelsesforløp av fermenta-tivt fremstilt biomasse. The phosphodiesterases can penetrate the cell wall of microorganisms, which is why there is no need for a special pre-treatment of the raw bioprotein for the enzymatic hydrolysis of RNS and DNS. Therefore, this method step can be integrated into any processing sequence of fermentatively produced biomass.
Den nødvendige enzymkonsentrasjon (g) står til substratkon-sentrasjonen (g) i forholdet 1:1.000 til 1:500.000, fortrinnsvis 1:10.000 til 1:100.000. The required enzyme concentration (g) corresponds to the substrate concentration (g) in the ratio 1:1,000 to 1:500,000, preferably 1:10,000 to 1:100,000.
Ved siden av råenzympreparater fra mikroorganismer og planter foretrekkes handelstilgjengelige enzymer som Next to crude enzyme preparations from microorganisms and plants, commercially available enzymes such as
Enzymene kan derved alt etter fremgangsmåte anvendes i deres opprinnelige form som også i adsorptiv, ionisk eller kovalent på en bærer fiksert form. Depending on the method, the enzymes can therefore be used in their original form as well as in adsorptive, ionic or covalent form fixed on a carrier.
Reaksjonsmiljøet for den enzymatiske hydrolyse er vanni eller blandinger med vannblandbare organiske oppløsnings-midler, idet alt etter biomassekonsentrasjon og -type ligger nukleinsyrekonsentrasjonen ved 0,05-10, fortrinnsvis 0,3-7, spesielt foretrukket 1-5 vekt-%. Det foretrukkede pH-området er 4,5-6,5, spesielt pÅ 5-6, som under hydrolyse-reaksjonen holdes i det foretrukkede området ved avkpuffring av de dannede syregruppene av oligo- resp. monomere nukleotider med lut som NH^OH, NaOH, KOH, Ca(OH)2eller basiske salter. The reaction environment for the enzymatic hydrolysis is water or mixtures with water-miscible organic solvents, with the nucleic acid concentration depending on the biomass concentration and type being 0.05-10, preferably 0.3-7, particularly preferably 1-5% by weight. The preferred pH range is 4.5-6.5, especially at 5-6, which during the hydrolysis reaction is kept in the preferred range by buffering the formed acid groups of oligo- or monomeric nucleotides with alkali such as NH^OH, NaOH, KOH, Ca(OH)2 or basic salts.
Reaksjonen foregår ved en temperatur fra 30-60°C, fortrinnsvis 45-55°C. Tidsbehovet for hydrolysen er avhengig av typen av den anvendte biomasse, temperaturen og enzymet og utgjør vanligvis 0,5-8 timer. The reaction takes place at a temperature of 30-60°C, preferably 45-55°C. The time required for the hydrolysis depends on the type of biomass used, the temperature and the enzyme and usually amounts to 0.5-8 hours.
For bestemmelse av hydrolyseforløpet av RNS og DNS kan nu-kleotidenes konsentrasjon bestemmes ved hjelp av HPLC: To determine the course of hydrolysis of RNS and DNS, the concentration of the nucleotides can be determined using HPLC:
Stasjonær fase: "LiChrosorb" RP 18 7 |i (Merck)Stationary phase: "LiChrosorb" RP 18 7 |i (Merck)
Søyle 1 = 20 cm, ø 0,4 cmColumn 1 = 20 cm, ø 0.4 cm
Mobil fase: dobbeltdestillert 1^0 med kons. H^PO^Mobile phase: double distilled 1^0 with conc. H^PO^
(pH 2,1)(pH 2.1)
Strømningsgrad: 2,0 ml/min.Flow rate: 2.0 ml/min.
Trykk:~100 barPressure: ~100 bar
Bølgelengde: 254 nmWavelength: 254 nm
ReferansestofferReference substances
a) for RNS: 5'-nukleotider (5<1->CMP, 5'-UMP, 5'-AMP, 5'-GMP) b) for DNS: Desoksy-5'-nukleotider (d-5'-CMP, d-5'-AMP, d-5'-GMP, d-5'-TMP) a) for RNS: 5'-nucleotides (5<1->CMP, 5'-UMP, 5'-AMP, 5'-GMP) b) for DNS: Deoxy-5'-nucleotides (d-5'-CMP , d-5'-AMP, d-5'-GMP, d-5'-TMP)
QYE?§ksE§r^men^elle_u^de^søk^lserQYE?§ksE§r^men^elle_u^de^searches^lser
For fastslåelse av forholdet mellom tarmvekt og legemsvekt fores hønsekyllinger etter en forperiode på 4 dager med et vitamin- og sporeelementfattig for med nærings-sjef f kvaliteter kontroll- og forsøksrasjoner over ca. 9 dager. Derved er det likegyldig om forsøksperioden umiddel-bart tilslutter seg til forperioden/eller forsøksperioden forankobles en mer eller mindre lang mellomperiode med kontrollfor (f.eks. 1-21 dager). To determine the relationship between intestinal weight and body weight, broilers are fed after a pre-period of 4 days with a vitamin and trace element poor for with nutrition manager f qualities control and experimental rations of approx. 9 days. Thereby, it does not matter whether the experimental period immediately joins the pre-period/or the experimental period is preceded by a more or less long intermediate period with control (e.g. 1-21 days).
Rasjonene av de egentlige forsøksrekker inneholder ca.31% renprotein (aminosyreprotein), 1,88% Ca, 1,5% P, 0,18% Na og 0,6% K, de er beregnet isoenergetiske (på basis av den omsettbare energi, ca. 14 MJ/kg). Soyaprotein tjener i kontrollrasjonen som eneste proteinkilde. Den kompletteres behovsdekkende med DL-metionin og glycin. I forsøksrasjonen tjener bakterieprotein som eneste proteinkilde. Det er behovsdekkende supplementert med DL-metionin og L-arginin-HCl. The rations of the actual experimental series contain approx. 31% pure protein (amino acid protein), 1.88% Ca, 1.5% P, 0.18% Na and 0.6% K, they are calculated isoenergetic (on the basis of the exchangeable energy , about 14 MJ/kg). Soya protein serves in the control ration as the only protein source. It is supplemented as needed with DL-methionine and glycine. In the experimental ration, bacterial protein serves as the only protein source. It is adequately supplemented with DL-methionine and L-arginine-HCl.
Tabell I orienterer eksempelvis over rasjonssammensetningen. Table I provides information on the ration composition, for example.
Gjøkyllingene holdes i bur i trådrist ved 24 timers permanent lys. De kan oppta for og vann (fra enBeckendrikker) ad libitum. Foret administreres prinsippielt pelletert (ø 3 mm). The cuckoo chicks are kept in wire mesh cages with 24 hours of permanent light. They can take food and water (from a Beckendrikker) ad libitum. The feed is generally administered as pellets (ø 3 mm).
Som forsøksparameter tjener vektutviklingen, den absolutte og relative vekt av tynntarmen (uten tarminnhold) samt dens lengde. The weight development, the absolute and relative weight of the small intestine (without intestinal contents) and its length serve as test parameters.
ResultaterResults
I en serie av forskjellige forsøk kunne det vises at bakterieprotein, også peroksydbehandlet, fører til en nedsettelse av levendemasseøkningen sammenlignet til soyakontrollgruppen samt til en økning av tynntarmvekten. Tabell 2 orienterer over resultatene. In a series of different experiments, it could be shown that bacterial protein, also peroxide-treated, leads to a reduction in the live mass increase compared to the soy control group and to an increase in the small intestine weight. Table 2 provides information on the results.
Av sammenligningen av forsøksdataene fremgår at bakterieprotein (rått eller peroksydbehandlet) reduserte levende-masseøkningen i forsøkstidsrommet til 49% (+_ 13%) av soya-kontrollverdien. De relative tarmvekter lå ved 152 +_ 12% From the comparison of the experimental data, it appears that bacterial protein (raw or peroxide-treated) reduced the live mass increase in the experimental period to 49% (+_ 13%) of the soy control value. The relative intestinal weights were at 152 +_ 12%
av kontrollgruppeverdien.of the control group value.
Tabell 3 viser de analoge verdier ved anvendelse av nukle-asebehandlede bakterieprotein-porsjoner. Table 3 shows the analogous values when using nuclease-treated bacterial protein portions.
Av sammenligninger med -nukleasebehandlet bakterieprotein viser det seg at den relative tarmvekt med 128 _+ 16% av kontrollverdien var vesentlig mindre øket enn uten nukleasebehandling. Tas det i tillegg dessuten hensyn til den om-stendighet at den relative tarmvekt faller med økende legemsvekt, så relativerer disse forskjeller seg videre da de med bakterieprotein forede dyr alltid var tydelig lettere enn kontrolldyrene. From comparisons with -nuclease-treated bacterial protein, it appears that the relative intestinal weight with 128 _+ 16% of the control value was significantly less increased than without nuclease treatment. If, in addition, account is taken of the fact that the relative intestinal weight falls with increasing body weight, then these differences are further relativized as the animals fed with bacterial protein were always clearly lighter than the control animals.
For så vidt kunne det bioeksperimentelt belegges at nuklease-behandlingen av bioprotein er en egnet fremgangsmåte til å nedsette bieffekter som opptrer ved administrering av uvanlig høye mengder på bakterieprotein hos kyllinger. Spesielt påvirkes tynntarmvekten gunstig. De målte tynn-tarmlengder som etter inngiving av bakterieprotein uten nukleasebehandling var tydelig større enn ved kontrolldyrene, var ved nukleasebehandlet bakterieprotein tilpasset kontroll-verdiene. To that extent, it could be proven bioexperimentally that the nuclease treatment of bioprotein is a suitable method to reduce side effects that occur when unusually high amounts of bacterial protein are administered to chickens. In particular, the weight of the small intestine is favorably affected. The measured small intestine lengths, which after administration of bacterial protein without nuclease treatment were clearly greater than in the control animals, were adapted to the control values with nuclease-treated bacterial protein.
De følgende eksempler viser råprotein-foredlingen. The following examples show the crude protein processing.
Eksem2el_lj_Exem2el_lj_
Methylomonas clara (ATCC 31 226) ble dyrket i en næringsopp-løsning inneholdende metanol som eneste karbonkilde, ammoniakk som eneste nitrogenkilde, fosfat, jern- og magne-siumsalter samt andre vanlige sporelementer under aerobe betingelser (US-patent 4 166 004). Konsentrasjonen av den derved frembragte bakteriecellemasse ble øket ved separering fra 1,5 til 15 vekt-%. Methylomonas clara (ATCC 31 226) was grown in a nutrient solution containing methanol as the only carbon source, ammonia as the only nitrogen source, phosphate, iron and magnesium salts as well as other common trace elements under aerobic conditions (US patent 4 166 004). The concentration of the resulting bacterial cell mass was increased by separation from 1.5 to 15% by weight.
Av denne pasta ble 1000 g oppvarmet under langsom omrøring til 55°C, pH-verdien innstilt fra opprinnelig 6,9 med svovelsyre til 5,1 og tilsatt 1 mg nuklease (Amano RP8), oppløst i 10 ml vann. Of this paste, 1000 g were heated with slow stirring to 55°C, the pH adjusted from the original 6.9 with sulfuric acid to 5.1, and 1 mg of nuclease (Amano RP8), dissolved in 10 ml of water, was added.
Over et tidsrom på 4 timer ble under konstantholding av pH-verdien og temperaturen nukleinsyrehydrolysen gjennomført og innhold av dannet monomer 5<1->nukleotider bestemt over HPLC-måling. Etter 3,5 timer var reaksjonen praktisk talt avsluttet, dvs. innholdet av 5<1->nukleotider (i vekt-%) Over a period of 4 hours, while keeping the pH value and the temperature constant, the nucleic acid hydrolysis was carried out and the content of formed monomeric 5<1->nucleotides determined via HPLC measurement. After 3.5 hours the reaction was practically complete, i.e. the content of 5<1->nucleotides (in wt%)
av den anvendte biomasse (15 0 g) tilsvarte omtrent kvantitativt (96%) innholdet av makromolekylære nukleinsyrer (12,6 vekt-%) av biomassen. of the biomass used (150 g) roughly corresponded quantitatively (96%) to the content of macromolecular nucleic acids (12.6% by weight) of the biomass.
Deretter ble pH-verdien med natronlut innstilt på pH 6,5, omrørt 10 minutter ved 80°C og den således dannede biopro-teinmasse tørket. The pH was then adjusted to pH 6.5 with caustic soda, stirred for 10 minutes at 80°C and the bioprotein mass thus formed dried.
Eksem<pe>l_2:Eczema<pe>l_2:
Det ble gått fram som i eksempel 1, imidlertid anvendtThe procedure was the same as in example 1, however applied
0,05 mg fosfodiesterase (fra Crotalus durissus, firma Boehringer Mannheim, EC 3.1.4.1). Hydrolyseutbyttet av frie 5<1->nukleotider utgjorde 89%. 0.05 mg phosphodiesterase (from Crotalus durissus, company Boehringer Mannheim, EC 3.1.4.1). The hydrolysis yield of free 5<1->nucleotides was 89%.
Eksemp_el_3 :Example_el_3 :
Det ble gått fram som i eksempel 1, imidlertid anvendtThe procedure was the same as in example 1, however applied
0,15 mg nuklease P 1 (firmaet Sigman, fra Penicillium citrinum).Hydrolyseutbyttet utgjorde etter 3,5 timer 97%. 0.15 mg nuclease P 1 (the company Sigman, from Penicillium citrinum). The hydrolysis yield was 97% after 3.5 hours.
Eksemgel_4 j_Eczemagel_4 j_
Det ble gått fram som i eksempel 1, imidlertid anvendt 10 g hvetekim som rånukleasepreparat. Utbyttet av 5'-nukleotider utgjorde etter 3,5 timer 78%. The procedure was as in example 1, however, 10 g of wheat germ was used as crude nuclease preparation. The yield of 5' nucleotides was 78% after 3.5 hours.
Eksemp_el_5:Example_el_5:
Det ble gått fram som i eksempel 4, imidlertid med en rå-enzyminkubasjonstid på 5 timer. Utbyttet av 5<1->nukleotider utgjorde 94%. The procedure was the same as in example 4, however with a crude enzyme incubation time of 5 hours. The yield of 5<1->nucleotides was 94%.
Eksermoel_6 :Exermoel_6 :
Fremstillingen av biomassen foregikk som i eksempel 1, imidlertid ble råbioproteinet etter separering oppvarmet 10 minutter ved 85°C, avkjølt til 55°C og deretter blandet med 0,05 mg nuklease RP8 (Amano). Etter 2 timer utgjorde hydrolyseutbyttet av 5<1>mukleotider 97%. The production of the biomass proceeded as in example 1, however, after separation, the crude bioprotein was heated for 10 minutes at 85°C, cooled to 55°C and then mixed with 0.05 mg of nuclease RP8 (Amano). After 2 hours, the hydrolysis yield of 5<1>mucleotides was 97%.
Eksempel_7:Example_7:
Fra en kontinuerlig fermentering av Methylomonas claraFrom a continuous fermentation of Methylomonas clara
(ATCC 31 226) ifølge US-patent 4 166 004 med etterfølgende oppkonsentrering av biomassen til 3 0 vekt-% og forstøvnings-tørking ble 15 kg av det således dannede tørrprodukt (rest-fuktighet 4,5%, nukleinsyreinnhold 11,8%, referert til tørrstoff) suspendert i 85 1 vann under omrøring, pH-verdien innstilt med svovelsyre fra 6,8 til 5,4, temperaturen øket til 55°C og tilsatt 150 mg nuklease (Sigma, (ATCC 31 226) according to US patent 4 166 004 with subsequent concentration of the biomass to 30% by weight and spray drying, 15 kg of the thus formed dry product (residual moisture 4.5%, nucleic acid content 11.8%, referred to dry matter) suspended in 85 l of water with stirring, the pH value adjusted with sulfuric acid from 6.8 to 5.4, the temperature raised to 55°C and added 150 mg of nuclease (Sigma,
EC 3.1.30.1) , oppløst i 10 ml vann.EC 3.1.30.1), dissolved in 10 ml of water.
Under pH- (5,4) og temperaturstyring (55°C) ble det om-rørt 3 timer, pH-verdien innstilt med natronlut til 6,5 Under pH (5.4) and temperature control (55°C) it was stirred for 3 hours, the pH value adjusted with caustic soda to 6.5
og suspensjonen forstøvningstørket ved 95°C. Hydrolyseutbyttet av fritt 5'-nukleotider ble bestemt over HPLC and the suspension spray-dried at 95°C. The hydrolysis yield of free 5' nucleotides was determined via HPLC
med 97%.with 97%.
Eksemgel_8:Example gel_8:
Fremgangsmåten ble gjennomført som i eksempel 7, imidlertid ble lipidene ekstrahert fra 15 kg tørt råbioprotein i hen-hold til fremgangsmåten..: ifølge US-patent 4 206 243, eksempel 1, og den gjenblivende mengde på 13 kg avfettet bioprotein behandlet under betingelsene fra eksempel 7 med 75 mg nuklease (Sigma). Hydrolyseutbyttet av frie 5<1->nukleotider utgjorde 99%. The procedure was carried out as in example 7, however, the lipids were extracted from 15 kg of dry crude bioprotein according to the method..: according to US patent 4 206 243, example 1, and the remaining amount of 13 kg of defatted bioprotein treated under the conditions of example 7 with 75 mg nuclease (Sigma). The hydrolysis yield of free 5<1->nucleotides was 99%.
Eksemp_el_9:Example_el_9:
En hydrokarbonutnyttende stamme av gjæren Candida lipoly-tica (ATCC 20 383) ble kultivert på n-parafiner i nærvær av et vandig næringsmedium og en oksygenholdig gass (US-patent 4 206 243, eksempel 8). Gjærcellemassen ble adskilt fra næringsoppløsningen og tørket, nukleinsyreinnholdet referert til tørrstoff utgjorde 7,9%. A hydrocarbon-utilizing strain of the yeast Candida lipolytica (ATCC 20,383) was cultured on n-paraffins in the presence of an aqueous nutrient medium and an oxygen-containing gas (US Patent 4,206,243, Example 8). The yeast cell mass was separated from the nutrient solution and dried, the nucleic acid content referred to dry matter was 7.9%.
150 g av denne tørrmasse ble ved 55°C suspendert i 850 ml vann, pH-verdien innstilt med fosforsyre på 5,5, og bland-ingen inkubert under omrøring og konstantholding av pH-verdien og temperaturen 4 timer med 3 mg nuklease (Amano RP 8). Deretter ble temperaturen i 10 minutter øket 150 g of this dry mass was suspended at 55°C in 850 ml of water, the pH value adjusted with phosphoric acid to 5.5, and the mixture incubated while stirring and keeping the pH value and temperature constant for 4 hours with 3 mg of nuclease (Amano RP 8). The temperature was then increased for 10 minutes
til 90°C, pH-verdien innstilt med natronlut på 6,5 og tørket. Hydrolyseutbyttet av 5<1>nukleotider utgjorde 91%. to 90°C, pH adjusted with caustic soda to 6.5 and dried. The hydrolysis yield of 5<1>nucleotides was 91%.
Claims (10)
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
DE19853500912 DE3500912A1 (en) | 1985-01-12 | 1985-01-12 | REFINING RAW PROTEINS |
Publications (1)
Publication Number | Publication Date |
---|---|
NO860075L true NO860075L (en) | 1986-07-14 |
Family
ID=6259733
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO860075A NO860075L (en) | 1985-01-12 | 1986-01-10 | PROCESSING OF RAAP PROTEINS. |
Country Status (13)
Country | Link |
---|---|
EP (1) | EP0188004A2 (en) |
JP (1) | JPS61177951A (en) |
AU (1) | AU5219486A (en) |
DE (1) | DE3500912A1 (en) |
DK (1) | DK11786A (en) |
ES (1) | ES8704072A1 (en) |
FI (1) | FI860097A (en) |
GR (1) | GR860057B (en) |
HU (1) | HUT39988A (en) |
IL (1) | IL77562A0 (en) |
NO (1) | NO860075L (en) |
PT (1) | PT81812B (en) |
ZA (1) | ZA86194B (en) |
Families Citing this family (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
FR2646435B1 (en) * | 1989-04-26 | 1991-06-28 | Cohas Pascal | METHOD OF MANUFACTURING YEAST FOR ANIMALS |
-
1985
- 1985-01-12 DE DE19853500912 patent/DE3500912A1/en not_active Withdrawn
- 1985-12-28 EP EP85116636A patent/EP0188004A2/en not_active Withdrawn
-
1986
- 1986-01-09 HU HU8688A patent/HUT39988A/en unknown
- 1986-01-09 FI FI860097A patent/FI860097A/en not_active Application Discontinuation
- 1986-01-09 PT PT81812A patent/PT81812B/en unknown
- 1986-01-10 DK DK11786A patent/DK11786A/en not_active Application Discontinuation
- 1986-01-10 AU AU52194/86A patent/AU5219486A/en not_active Abandoned
- 1986-01-10 IL IL77562A patent/IL77562A0/en unknown
- 1986-01-10 NO NO860075A patent/NO860075L/en unknown
- 1986-01-10 JP JP61002357A patent/JPS61177951A/en active Pending
- 1986-01-10 ES ES550772A patent/ES8704072A1/en not_active Expired
- 1986-01-10 GR GR860057A patent/GR860057B/en unknown
- 1986-01-10 ZA ZA86194A patent/ZA86194B/en unknown
Also Published As
Publication number | Publication date |
---|---|
PT81812A (en) | 1986-02-01 |
EP0188004A2 (en) | 1986-07-23 |
PT81812B (en) | 1987-11-05 |
ES8704072A1 (en) | 1987-03-16 |
IL77562A0 (en) | 1986-08-31 |
AU5219486A (en) | 1986-07-17 |
ES550772A0 (en) | 1987-03-16 |
ZA86194B (en) | 1986-08-27 |
FI860097A (en) | 1986-07-13 |
DK11786A (en) | 1986-07-13 |
JPS61177951A (en) | 1986-08-09 |
DK11786D0 (en) | 1986-01-10 |
FI860097A0 (en) | 1986-01-09 |
GR860057B (en) | 1986-04-29 |
DE3500912A1 (en) | 1986-07-17 |
HUT39988A (en) | 1986-11-28 |
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