CN116459800B - Protein-based adsorbent for selectively adsorbing metal rhenium ions and application thereof - Google Patents
Protein-based adsorbent for selectively adsorbing metal rhenium ions and application thereof Download PDFInfo
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- CN116459800B CN116459800B CN202310475015.2A CN202310475015A CN116459800B CN 116459800 B CN116459800 B CN 116459800B CN 202310475015 A CN202310475015 A CN 202310475015A CN 116459800 B CN116459800 B CN 116459800B
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- protein
- rhenium
- based adsorbent
- adsorbent
- reducing agent
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- 229910052702 rhenium Inorganic materials 0.000 title claims abstract description 75
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 68
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 68
- 239000003463 adsorbent Substances 0.000 title claims abstract description 62
- -1 rhenium ions Chemical class 0.000 title claims abstract description 59
- 229910052751 metal Inorganic materials 0.000 title claims abstract description 18
- 239000002184 metal Substances 0.000 title claims abstract description 18
- 229910052750 molybdenum Inorganic materials 0.000 claims abstract description 40
- 239000011733 molybdenum Substances 0.000 claims abstract description 40
- 238000001179 sorption measurement Methods 0.000 claims abstract description 35
- ZOKXTWBITQBERF-UHFFFAOYSA-N Molybdenum Chemical compound [Mo] ZOKXTWBITQBERF-UHFFFAOYSA-N 0.000 claims abstract description 24
- 150000003863 ammonium salts Chemical class 0.000 claims abstract description 16
- 239000003638 chemical reducing agent Substances 0.000 claims abstract description 16
- 150000003973 alkyl amines Chemical class 0.000 claims abstract description 15
- 239000011259 mixed solution Substances 0.000 claims abstract description 12
- 238000000034 method Methods 0.000 claims abstract description 9
- 238000002360 preparation method Methods 0.000 claims abstract description 7
- 230000007704 transition Effects 0.000 claims abstract description 5
- 235000018102 proteins Nutrition 0.000 claims description 65
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims description 39
- 239000000243 solution Substances 0.000 claims description 33
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 21
- 239000008367 deionised water Substances 0.000 claims description 19
- 229910021641 deionized water Inorganic materials 0.000 claims description 19
- PBVAJRFEEOIAGW-UHFFFAOYSA-N 3-[bis(2-carboxyethyl)phosphanyl]propanoic acid;hydrochloride Chemical compound Cl.OC(=O)CCP(CCC(O)=O)CCC(O)=O PBVAJRFEEOIAGW-UHFFFAOYSA-N 0.000 claims description 17
- 102100033468 Lysozyme C Human genes 0.000 claims description 14
- 108010014251 Muramidase Proteins 0.000 claims description 14
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 claims description 14
- 235000010335 lysozyme Nutrition 0.000 claims description 14
- 229960000274 lysozyme Drugs 0.000 claims description 14
- 239000004325 lysozyme Substances 0.000 claims description 14
- 239000002699 waste material Substances 0.000 claims description 10
- 238000003723 Smelting Methods 0.000 claims description 8
- 239000000779 smoke Substances 0.000 claims description 8
- RHQDFWAXVIIEBN-UHFFFAOYSA-N Trifluoroethanol Chemical compound OCC(F)(F)F RHQDFWAXVIIEBN-UHFFFAOYSA-N 0.000 claims description 7
- 108091003079 Bovine Serum Albumin Proteins 0.000 claims description 5
- 102000004407 Lactalbumin Human genes 0.000 claims description 5
- 108090000942 Lactalbumin Proteins 0.000 claims description 5
- 229940098773 bovine serum albumin Drugs 0.000 claims description 5
- 238000002156 mixing Methods 0.000 claims description 5
- 238000004108 freeze drying Methods 0.000 claims description 3
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 claims description 3
- IOQPZZOEVPZRBK-UHFFFAOYSA-N octan-1-amine Chemical compound CCCCCCCCN IOQPZZOEVPZRBK-UHFFFAOYSA-N 0.000 claims description 3
- 238000003756 stirring Methods 0.000 claims description 3
- YKGBNAGNNUEZQC-UHFFFAOYSA-N 6-methyl-n,n-bis(6-methylheptyl)heptan-1-amine Chemical compound CC(C)CCCCCN(CCCCCC(C)C)CCCCCC(C)C YKGBNAGNNUEZQC-UHFFFAOYSA-N 0.000 claims description 2
- 102000008186 Collagen Human genes 0.000 claims description 2
- 108010035532 Collagen Proteins 0.000 claims description 2
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 claims description 2
- 102000008946 Fibrinogen Human genes 0.000 claims description 2
- 108010049003 Fibrinogen Proteins 0.000 claims description 2
- 102000011782 Keratins Human genes 0.000 claims description 2
- 108010076876 Keratins Proteins 0.000 claims description 2
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 claims description 2
- 108010063045 Lactoferrin Proteins 0.000 claims description 2
- 102000010445 Lactoferrin Human genes 0.000 claims description 2
- 102000008192 Lactoglobulins Human genes 0.000 claims description 2
- 108010060630 Lactoglobulins Proteins 0.000 claims description 2
- 108010062374 Myoglobin Proteins 0.000 claims description 2
- 102000036675 Myoglobin Human genes 0.000 claims description 2
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 claims description 2
- DWIIMMWKPHMFMV-UHFFFAOYSA-N [Cl-].CC(CCCCCCC[NH+](CCCCCCCC)CCCCCCCC)(C)C Chemical compound [Cl-].CC(CCCCCCC[NH+](CCCCCCCC)CCCCCCCC)(C)C DWIIMMWKPHMFMV-UHFFFAOYSA-N 0.000 claims description 2
- 238000005119 centrifugation Methods 0.000 claims description 2
- 229920001436 collagen Polymers 0.000 claims description 2
- 229960005188 collagen Drugs 0.000 claims description 2
- 229910052802 copper Inorganic materials 0.000 claims description 2
- 239000010949 copper Substances 0.000 claims description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims description 2
- 235000018417 cysteine Nutrition 0.000 claims description 2
- LAWOZCWGWDVVSG-UHFFFAOYSA-N dioctylamine Chemical compound CCCCCCCCNCCCCCCCC LAWOZCWGWDVVSG-UHFFFAOYSA-N 0.000 claims description 2
- DDXLVDQZPFLQMZ-UHFFFAOYSA-M dodecyl(trimethyl)azanium;chloride Chemical compound [Cl-].CCCCCCCCCCCC[N+](C)(C)C DDXLVDQZPFLQMZ-UHFFFAOYSA-M 0.000 claims description 2
- 229940012952 fibrinogen Drugs 0.000 claims description 2
- CSSYQJWUGATIHM-IKGCZBKSSA-N l-phenylalanyl-l-lysyl-l-cysteinyl-l-arginyl-l-arginyl-l-tryptophyl-l-glutaminyl-l-tryptophyl-l-arginyl-l-methionyl-l-lysyl-l-lysyl-l-leucylglycyl-l-alanyl-l-prolyl-l-seryl-l-isoleucyl-l-threonyl-l-cysteinyl-l-valyl-l-arginyl-l-arginyl-l-alanyl-l-phenylal Chemical compound C([C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CS)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)C1=CC=CC=C1 CSSYQJWUGATIHM-IKGCZBKSSA-N 0.000 claims description 2
- 229940078795 lactoferrin Drugs 0.000 claims description 2
- 235000021242 lactoferrin Nutrition 0.000 claims description 2
- 239000007788 liquid Substances 0.000 claims description 2
- 229910052758 niobium Inorganic materials 0.000 claims description 2
- 239000010955 niobium Substances 0.000 claims description 2
- GUCVJGMIXFAOAE-UHFFFAOYSA-N niobium atom Chemical compound [Nb] GUCVJGMIXFAOAE-UHFFFAOYSA-N 0.000 claims description 2
- BASFCYQUMIYNBI-UHFFFAOYSA-N platinum Chemical group [Pt] BASFCYQUMIYNBI-UHFFFAOYSA-N 0.000 claims description 2
- AQZSPJRLCJSOED-UHFFFAOYSA-M trimethyl(octyl)azanium;chloride Chemical compound [Cl-].CCCCCCCC[N+](C)(C)C AQZSPJRLCJSOED-UHFFFAOYSA-M 0.000 claims description 2
- 238000005406 washing Methods 0.000 claims description 2
- 229910052725 zinc Inorganic materials 0.000 claims description 2
- 239000011701 zinc Substances 0.000 claims description 2
- 239000002893 slag Substances 0.000 claims 4
- IXIBAKNTJSCKJM-BUBXBXGNSA-N bovine insulin Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3NC=NC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)C(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 IXIBAKNTJSCKJM-BUBXBXGNSA-N 0.000 claims 1
- WUAPFZMCVAUBPE-UHFFFAOYSA-N rhenium atom Chemical compound [Re] WUAPFZMCVAUBPE-UHFFFAOYSA-N 0.000 abstract description 34
- 239000010842 industrial wastewater Substances 0.000 abstract description 5
- 238000000926 separation method Methods 0.000 abstract description 4
- 238000002336 sorption--desorption measurement Methods 0.000 abstract 1
- 239000007864 aqueous solution Substances 0.000 description 22
- 239000012086 standard solution Substances 0.000 description 16
- XKBGEWXEAPTVCK-UHFFFAOYSA-M methyltrioctylammonium chloride Chemical compound [Cl-].CCCCCCCC[N+](C)(CCCCCCCC)CCCCCCCC XKBGEWXEAPTVCK-UHFFFAOYSA-M 0.000 description 8
- 239000011521 glass Substances 0.000 description 5
- 238000010790 dilution Methods 0.000 description 4
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- 238000007865 diluting Methods 0.000 description 3
- 229910021645 metal ion Inorganic materials 0.000 description 3
- 229910052961 molybdenite Inorganic materials 0.000 description 3
- CWQXQMHSOZUFJS-UHFFFAOYSA-N molybdenum disulfide Chemical compound S=[Mo]=S CWQXQMHSOZUFJS-UHFFFAOYSA-N 0.000 description 3
- 238000009854 hydrometallurgy Methods 0.000 description 2
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
- 238000009853 pyrometallurgy Methods 0.000 description 2
- 238000000638 solvent extraction Methods 0.000 description 2
- 102000009027 Albumins Human genes 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009091 Amyloidogenic Proteins Human genes 0.000 description 1
- 108010048112 Amyloidogenic Proteins Proteins 0.000 description 1
- 239000002028 Biomass Substances 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 241000283073 Equus caballus Species 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- 241000282414 Homo sapiens Species 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 241000199919 Phaeophyceae Species 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 108090000901 Transferrin Proteins 0.000 description 1
- 102000004338 Transferrin Human genes 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 1
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- 229940050528 albumin Drugs 0.000 description 1
- 239000000956 alloy Substances 0.000 description 1
- 229910045601 alloy Inorganic materials 0.000 description 1
- 239000003957 anion exchange resin Substances 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
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- 230000002496 gastric effect Effects 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 239000002440 industrial waste Substances 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
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- 238000002844 melting Methods 0.000 description 1
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- 238000001000 micrograph Methods 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
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- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 125000001453 quaternary ammonium group Chemical group 0.000 description 1
- 238000004064 recycling Methods 0.000 description 1
- 238000001338 self-assembly Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000012581 transferrin Substances 0.000 description 1
Classifications
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J20/00—Solid sorbent compositions or filter aid compositions; Sorbents for chromatography; Processes for preparing, regenerating or reactivating thereof
- B01J20/22—Solid sorbent compositions or filter aid compositions; Sorbents for chromatography; Processes for preparing, regenerating or reactivating thereof comprising organic material
- B01J20/24—Naturally occurring macromolecular compounds, e.g. humic acids or their derivatives
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D53/00—Separation of gases or vapours; Recovering vapours of volatile solvents from gases; Chemical or biological purification of waste gases, e.g. engine exhaust gases, smoke, fumes, flue gases, aerosols
- B01D53/02—Separation of gases or vapours; Recovering vapours of volatile solvents from gases; Chemical or biological purification of waste gases, e.g. engine exhaust gases, smoke, fumes, flue gases, aerosols by adsorption, e.g. preparative gas chromatography
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J20/00—Solid sorbent compositions or filter aid compositions; Sorbents for chromatography; Processes for preparing, regenerating or reactivating thereof
- B01J20/22—Solid sorbent compositions or filter aid compositions; Sorbents for chromatography; Processes for preparing, regenerating or reactivating thereof comprising organic material
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02P—CLIMATE CHANGE MITIGATION TECHNOLOGIES IN THE PRODUCTION OR PROCESSING OF GOODS
- Y02P10/00—Technologies related to metal processing
- Y02P10/20—Recycling
Landscapes
- Chemical & Material Sciences (AREA)
- Analytical Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- General Chemical & Material Sciences (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Solid-Sorbent Or Filter-Aiding Compositions (AREA)
Abstract
本发明公开了一种选择性吸附金属铼离子的蛋白质基吸附剂及其应用，所述吸附剂是在还原剂还原蛋白质形成的相转变聚集体中包裹烷基胺或铵盐获得。其使用方法是将吸附剂投入含有铼和钼的混合溶液中实现对铼的选择性吸附。该吸附剂制备和使用方法简便，环境友好，可循环利用，对稀有金属铼具有高选择性吸附能力。该吸附剂可用于工业废水和矿石渗滤液中铼和钼的分离，并且经过吸附‑解吸循环后，仍具有较高的吸附比。
The invention discloses a protein-based adsorbent for selectively adsorbing metal rhenium ions and its application. The adsorbent is obtained by encapsulating alkylamine or ammonium salt in a phase transition aggregate formed by reducing protein with a reducing agent. The method of using the adsorbent is to put the adsorbent into a mixed solution containing rhenium and molybdenum to achieve selective adsorption of rhenium. The preparation and use methods of the adsorbent are simple, environmentally friendly, recyclable, and have a high selective adsorption capacity for rare metal rhenium. The adsorbent can be used for the separation of rhenium and molybdenum in industrial wastewater and ore leachate, and after adsorption-desorption cycles, it still has a high adsorption ratio.
Description
Technical Field
The invention belongs to the technical field of adsorbents, and particularly relates to a protein-based adsorbent for selectively adsorbing metal rhenium ions, which is formed by doping alkylamine or ammonium salt into phase-transition protein.
Background
Rhenium is a rare metal with high melting point, is widely applied to high-temperature alloy production and catalysts of oil refineries, and high-tech fields such as electronics, astrogeology, radio medical diagnosis and the like, and has increasingly demanded rhenium in the market all over the world, but the content of the rhenium in the crust of the earth is very low (only 10 -7%). The rhenium mineral is mainly derived from molybdenite, but the molybdenite contains metallic molybdenum with similar chemical property and atomic radius to rhenium, and the rhenium only contains 200-800 ppm in the molybdenite. Therefore, it is very difficult to recover and separate rhenium in a low concentration (10 to 100 ppm) from the complex containing the coexisting metal ions, particularly molybdenum.
There are many current techniques for extracting and separating rhenium from molybdenum, such as pyrometallurgy, hydrometallurgy, solvent extraction and ion exchange. However, the solvent extraction method can release a large amount of organic solvents, and the pyrometallurgy method and the hydrometallurgy method generally have the problems of high cost and secondary pollution. Adsorption, however, has been increasingly utilized as another method for extracting and separating rhenium from molybdenum, and among them, biomass materials are favored for their sustainability, environmental safety, and low cost, such as aminated corn stalk gel, brown algae-based materials, and anion exchange resins, which have been reported for adsorption of rhenium, but few mention is made of separating rhenium and molybdenum in aqueous solution. Therefore, the development of a novel biological adsorbent with adsorption capacity equivalent to that of a commercial synthetic adsorbent, so as to overcome the difficulty of effectively separating rhenium in the presence of a large amount of molybdenum, has great significance and also brings great value to rhenium related industries and materials.
Disclosure of Invention
The invention aims to provide a protein-based adsorbent which is simple in preparation method and environment-friendly, has higher adsorption efficiency and selectivity for adsorbing metal rhenium, and provides application of the adsorbent.
The protein-based adsorbent used in the present invention is obtained by wrapping alkylamine or ammonium salt in a phase-transition aggregate formed by reducing protein with a reducing agent.
The alkylamine is any one of di-n-octylamine, triisooctylamine and the like, and the ammonium salt is any one of trimethyl trioctyl ammonium chloride, octyl trimethyl ammonium chloride and dodecyl trimethyl ammonium chloride.
The protein is one of lysozyme, lactalbumin, insulin, serum albumin (human, horse, cow, rabbit, mouse, sheep), serum, thyrolactoglobulin, transferrin, lactoferrin, fibrinogen, albumin, collagen, keratin, gastric protein, beta-lactoglobulin, myoglobin, and the reducing agent is one of tri (2-carboxyethyl) phosphorus hydrochloride, cysteine, and glutathione.
Dissolving protein in trifluoroethanol, standing for more than 24 hours, then adding alkylamine or ammonium salt, uniformly mixing, then adding a reducing agent solution, stirring the obtained mixed solution at 30-40 ℃ until the protein is converted into phase transition aggregates from a dissolving state, wrapping alkylamine or ammonium salt, centrifugally washing with deionized water, and freeze-drying to obtain the protein-based adsorbent.
In the preparation method, the concentration of the reducing agent in the mixed solution is 0.1-20 mg/mL, the concentration of the protein is 30-140 mg/mL, and the concentration of the alkylamine or ammonium salt is 5-80 mg/mL.
In the preparation method, the concentration of the reducing agent in the mixed solution is preferably 0.4-10 mg/mL, the concentration of the protein is preferably 50-80 mg/mL, and the concentration of the alkylamine or ammonium salt is preferably 10-50 mg/mL.
In the preparation method, the reducing agent solution is prepared by adding the reducing agent into water and adjusting the pH value to 7 by NaOH.
The protein-based adsorbent is applied to selectively adsorbing metal rhenium ions, wherein the metal rhenium ions are derived from any one of copper ore smelting smoke dust and waste residues, platinum group ore smelting smoke dust and waste residues, niobium ore smelting smoke dust and waste residues, zinc ore smelting smoke dust and waste residues and low-grade molybdenum ore waste liquid.
The beneficial effects of the invention are as follows:
The invention dopes alkylamine or ammonium salt in protein, and utilizes reducing agent to effectively reduce disulfide bond of protein to induce rapid self-assembly of protein, so as to obtain protein-based adsorbent. The adsorbent can adsorb metal rhenium ions in aqueous solution through the adsorption of amino residues on functional adsorption sites on amyloid protein aggregates or the selective action of quaternary ammonium groups of ammonium salts on the metal rhenium ions, has good selectivity and recycling property, and realizes the separation of rhenium ions and molybdenum ions under low concentration. Compared with the prior art, the protein-based adsorbent has high selectivity on rhenium ions, the preparation and use methods are simple and green, the obtained adsorbent can be recycled, and the problem of separating rhenium ions from molybdenum ions in industrial wastewater and ore leachate can be solved.
Drawings
FIG. 1 is a digital photograph of the protein-based adsorbent prepared in example 1.
FIG. 2 is a scanning electron microscope image of the protein-based adsorbent prepared in example 1.
FIG. 3 shows the adsorption rates of rhenium and molybdenum ions at different pH values for the protein-based adsorbent of example 1.
FIG. 4 shows the adsorption rates of rhenium and molybdenum ions by different amounts of the protein-based adsorbent in example 1.
FIG. 5 shows the adsorption amount of rhenium ions by different amounts of the protein-based adsorbent in example 1.
FIG. 6 is a pseudo-second order fit of the adsorption behavior of the protein-based adsorbent of example 1.
FIG. 7 is a Freundlich isotherm fit of the adsorption behavior of the protein-based adsorbent of example 1.
FIG. 8 is a graph showing the selective adsorption of rhenium ions in rhenium/molybdenum binary solutions with different rhenium/molybdenum ratios by the protein-based adsorbent of example 1.
FIG. 9 shows the adsorption rate of rhenium ions in industrial waste solutions with different dilution factors by the protein-based adsorbent in example 1.
FIG. 10 is an adsorption ratio of the protein-based adsorbent of example 1 to rhenium ions and other competing metal ions in industrial wastewater.
Detailed Description
The present invention will be described in further detail with reference to the drawings and examples, but the scope of the present invention is not limited to these examples.
Example 1
300Mg of lysozyme was dissolved in 3mL of trifluoroethanol, placed in a 10mL glass bottle for 24 hours to prepare a lysozyme solution of 100mg/L, 1mL of 180mg/mL aqueous methyltrioctylammonium chloride solution was then added to the lysozyme solution, and shaking was carried out at 160rpm for 30 minutes, 0.3mL of 129mg/mL tris (2-carboxyethyl) phosphorus hydrochloride solution having a pH of 7 (prepared by dissolving tris (2-carboxyethyl) phosphorus hydrochloride in deionized water and adjusting the pH to 7 with 5mol/L aqueous sodium hydroxide solution) was further added, and the resulting mixed solution was stirred at 35℃for 4 hours to convert lysozyme from a dissolved state into phase-converted aggregate-coated methyltrioctylammonium chloride, and then centrifuged 3 times with deionized water at 5000rpm for 5 minutes at room temperature to remove tris (2-carboxyethyl) phosphorus hydrochloride, followed by freeze-drying for 24 hours to obtain a dry white powdery protein-based adsorbent.
Example 2
300Mg of lysozyme was dissolved in 3mL of trifluoroethanol, placed in a 10mL glass bottle for 24 hours to prepare a lysozyme solution of 100mg/L, 1mL of 180mg/mL aqueous solution of methyltrioctylammonium chloride was then added to the lysozyme solution, and the mixture was shaken at 160rpm for 30 minutes, and further 6mg/mL solution of tris (2-carboxyethyl) phosphorus hydrochloride of 0.3mLpH (prepared by dissolving tris (2-carboxyethyl) phosphorus hydrochloride in deionized water and adjusting pH to 7 with 5mol/L aqueous solution of sodium hydroxide) was added thereto, and the resulting mixed solution was stirred at 35℃for 4 hours to convert the lysozyme from a dissolved state into a phase-converted aggregate coated methyltrioctylammonium chloride, and then centrifuged 3 times at 5000rpm with deionized water for 5 minutes at room temperature to remove tris (2-carboxyethyl) phosphorus hydrochloride. After centrifugation, the material was freeze-dried for 24 hours to give a dry white powdery protein-based adsorbent.
Example 3
600Mg of bovine serum albumin was dissolved in 3mL of trifluoroethanol, placed in a 10mL glass bottle for 24 hours to prepare 200mg/L of bovine serum albumin solution, then 1mL of 180mg/mL aqueous solution of methyltrioctylammonium chloride was added to the bovine serum albumin solution, and shaking was carried out at 160rpm for 30 minutes, then 0.3mLpH of 129mg/mL solution of tris (2-carboxyethyl) phosphorus hydrochloride (prepared by dissolving tris (2-carboxyethyl) phosphorus hydrochloride in deionized water and adjusting pH to 7 with 5mol/L aqueous solution of sodium hydroxide) was added thereto, and the resulting mixed solution was stirred at 35℃for 4 hours to convert the bovine serum albumin from a dissolved state into phase-converted aggregates to encapsulate methyltrioctylammonium chloride, and then centrifuged 3 times with deionized water at 5000rpm for 5 minutes at room temperature to remove tris (2-carboxyethyl) phosphorus hydrochloride, and then freeze-dried for 24 hours to obtain a dry white powdery protein-based adsorbent.
Example 4
300Mg of lactalbumin was dissolved in 3mL of trifluoroethanol, placed in a 10mL glass bottle for 24 hours to prepare 100mg/L of lactalbumin solution, 1mL of 180mg/mL aqueous solution of methyltrioctylammonium chloride was then added, and shaking was carried out at 160rpm for 30 minutes, and then 0.3mLpH of 6mg/mL solution of tris (2-carboxyethyl) phosphorus hydrochloride (prepared by dissolving tris (2-carboxyethyl) phosphorus hydrochloride in deionized water and adjusting pH to 7 with 5mol/L aqueous solution of sodium hydroxide) was added, and the resulting mixed solution was stirred at 35℃for 4 hours to convert lactalbumin from a dissolved state into phase transition aggregates to encapsulate methyltrioctylammonium chloride, and then centrifuged 3 times at 5000rpm with deionized water for 5 minutes at room temperature to remove tris (2-carboxyethyl) phosphorus hydrochloride, and then freeze-dried for 24 hours to obtain a dry white powdery protein-based adsorbent.
Example 5
Dissolving 300mg of lysozyme in 3mL of trifluoroethanol, placing in a 10mL glass bottle for 24 hours to prepare a lysozyme solution of 100mg/L, adding 1mL of 60mg/mL of n-octylamine aqueous solution into the lysozyme solution, oscillating for 30 minutes at 160rpm, adding 0.3mLpH of 129mg/mL of tris (2-carboxyethyl) phosphorus hydrochloride solution (prepared by dissolving tris (2-carboxyethyl) phosphorus hydrochloride in deionized water and adjusting pH to 7 by using 5mol/L of sodium hydroxide aqueous solution), stirring and reacting the obtained mixed solution at 35 ℃ for 4 hours, converting the lysozyme into phase-converted aggregates to wrap n-octylamine, centrifuging for 3 times at 5000rpm with deionized water at room temperature for 5 minutes to remove the tris (2-carboxyethyl) phosphorus hydrochloride, and then freezing and drying for 24 hours to obtain a dry white powdery protein-based adsorbent.
Example 6
Application of protein-based adsorbent prepared in example 1 in selective adsorption of metal rhenium ions
1. Influence of pH on the Selective adsorption of Metal rhenium ions by protein-based adsorbents
After 5mL of 1mg/mL rhenium standard solution and 5mL of 1mg/mL molybdenum standard solution were uniformly mixed, the mixture was diluted with deionized water to a total concentration of rhenium ions and molybdenum ions of 0.01mg/mL, and then the diluted solution was adjusted to ph=1, ph=6, ph=10, ph=12 with 10mg/mL HNO 3 aqueous solution and 5mol/L NaOH aqueous solution, and 40mg of protein-based adsorbent was added per 10mL solution, respectively, and adsorbed at 298K for 24 hours. As can be seen from fig. 3, at ph=12, the separation effect of rhenium ions from molybdenum ions is optimal.
2. Influence of the amount of protein-based adsorbent added on the Selective adsorption of Metal rhenium ions
After 5mL of 1mg/mL of rhenium standard solution and 5mL of 1mg/mL of molybdenum standard solution were mixed uniformly, the mixture was diluted with deionized water until the total concentration of rhenium ions and molybdenum ions became 0.01mg/mL, and then the diluted solution was adjusted to pH=12 with 10mg/mL of HNO 3 aqueous solution and 5mol/L of NaOH aqueous solution, and then 5mg, 10mg, 20mg, 40mg, 60mg, 80mg, 100mg of protein-based adsorbent were added per 10mL of solution, respectively, and adsorbed at 298K for 24 hours. As can be seen from fig. 4 and 5, the adsorption effect on rhenium ions was best when the protein-based adsorbent was added in an amount of 10 mg.
3. Influence of rhenium and molybdenum concentration on the adsorption Performance of protein-based adsorbents
After 5mL of 1mg/mL of rhenium standard solution and 5mL of 1mg/mL of molybdenum standard solution were uniformly mixed, the mixture was diluted with deionized water to a total concentration of rhenium ion and molybdenum ion of 0.001mg/mL, 0.01mg/mL, 0.02mg/mL, and 0.05mg/mL, and then the diluted solution was adjusted to pH=12 with 10mg/mL of HNO 3 aqueous solution and 5mol/L of NaOH aqueous solution, and then 10mg of protein-based adsorbent was added per 10mL of solution, followed by adsorption at 310K for 24 hours. As can be seen from FIG. 6, the protein-based adsorbent showed the highest adsorption of rhenium ions at a total concentration of 0.01mg/mL of rhenium and molybdenum.
4. Influence of temperature on the Selective adsorption of Metal rhenium ions by protein-based adsorbents
After uniformly mixing 5mL of 1mg/mL rhenium standard solution and 5mL of 1mg/mL molybdenum standard solution, diluting with deionized water until the total concentration of rhenium ions and molybdenum ions is 0.01mg/mL, then adjusting the diluted solution to ph=12 with 10mg/mL HNO 3 aqueous solution and 5mol/L NaOH aqueous solution, adding 10mg of protein-based adsorbent per 10mL solution, and adsorbing at 298K, 310K, 333K for 24 hours, respectively. As can be seen from FIG. 7, the protein-based adsorbent has a good effect of adsorbing rhenium ions at 298-333K.
5. Effect of molybdenum concentration on Selective adsorption of Metal rhenium ions by protein-based adsorbents
Diluting 5mL of 1mg/mL of rhenium standard solution with deionized water to reach a rhenium ion concentration of 0.001mg/mL, diluting 5mL of 1mg/mL of molybdenum standard solution with deionized water to reach a molybdenum ion concentration of 0.001mg/mL, 0.1mg/mL, 0.2mg/mL, 0.5mg/mL, 0.8mg/mL and 1mg/mL respectively, then uniformly mixing 5mL of diluted rhenium standard solution with 5mL of molybdenum standard solution diluted to different molybdenum ion concentrations, obtaining solutions with rhenium ion and molybdenum ion mass ratios of 1:1, 1:100, 1:200, 1:500, 1:800 and 1:1000 respectively, adjusting the solutions to pH=12 by using 10mg/mL of HNO 3 aqueous solution and 5mol/L of NaOH aqueous solution, and adding 10mg of protein-based adsorbent per 10mL of solution, and adsorbing at 310K for 24 hours. As can be seen from FIG. 8, the adsorption rate of the protein-based adsorbent for rhenium ions was about 90%, while the adsorption rate for molybdenum ions was increased from only 5% of 0.001mg/mL to 15% of 1 mg/mL.
6. Practical application
Industrial wastewater containing molybdenum ions and rhenium ions was diluted 0, 100, 500, 1000, 2000, 5000, 10000 times with deionized water, respectively, and ph=12 was adjusted with 10mg/mL HNO 3 aqueous solution and 5mol/L NaOH aqueous solution, and 10mg of protein-based adsorbent was added per 10mL, and adsorbed at 310K for 24 hours. As can be seen from fig. 9, the adsorption rate of the protein-based adsorbent for rhenium ions is increased from 83% to 95% after the rhenium ions are diluted from 0 to 1000 times in industrial wastewater, the adsorption rate is close to 100% after the dilution is more than 1000 times, the adsorption rate of the molybdenum ions is gradually decreased from 20% to 10% after the dilution is 0 to 1000 times, and the adsorption rate of the protein-based adsorbent for rhenium ions is significantly higher than that of other metal ions, particularly molybdenum ions, after the dilution is 1000 times and further reaches below 5%.
And uniformly mixing the standard solution of rhenium with 1mg/mL and the standard solution of molybdenum with 1mg/mL according to the volume ratio of 1:1 to obtain the standard solution of rhenium and molybdenum. 10mg of the protein-based adsorbent of example 1 was directly poured into 10mL of a standard solution of rhenium and molybdenum for adsorption, the maximum amount of rhenium adsorbed per gram of adsorbent was 124mg/g, the separation coefficient (. Beta. Re/Mo) of metal rhenium ions was 2.78X10: 10 3, and the adsorption per unit area was 57.2 mg.g -1·m-2.
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