WO2013164429A1 - Solubilisation enzymatique de métaux - Google Patents

Solubilisation enzymatique de métaux Download PDF

Info

Publication number
WO2013164429A1
WO2013164429A1 PCT/EP2013/059199 EP2013059199W WO2013164429A1 WO 2013164429 A1 WO2013164429 A1 WO 2013164429A1 EP 2013059199 W EP2013059199 W EP 2013059199W WO 2013164429 A1 WO2013164429 A1 WO 2013164429A1
Authority
WO
WIPO (PCT)
Prior art keywords
haloperoxidase
metal
gold
identity
aqueous composition
Prior art date
Application number
PCT/EP2013/059199
Other languages
English (en)
Inventor
Klaus Skaalum LASSEN
Original Assignee
Novozymes A/S
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Application filed by Novozymes A/S filed Critical Novozymes A/S
Priority to PCT/EP2013/069183 priority Critical patent/WO2014041178A2/fr
Publication of WO2013164429A1 publication Critical patent/WO2013164429A1/fr

Links

Classifications

    • CCHEMISTRY; METALLURGY
    • C22METALLURGY; FERROUS OR NON-FERROUS ALLOYS; TREATMENT OF ALLOYS OR NON-FERROUS METALS
    • C22BPRODUCTION AND REFINING OF METALS; PRETREATMENT OF RAW MATERIALS
    • C22B3/00Extraction of metal compounds from ores or concentrates by wet processes
    • C22B3/18Extraction of metal compounds from ores or concentrates by wet processes with the aid of microorganisms or enzymes, e.g. bacteria or algae
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/0004Oxidoreductases (1.)
    • C12N9/0065Oxidoreductases (1.) acting on hydrogen peroxide as acceptor (1.11)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12YENZYMES
    • C12Y111/00Oxidoreductases acting on a peroxide as acceptor (1.11)
    • C12Y111/01Peroxidases (1.11.1)
    • C12Y111/0101Chloride peroxidase (1.11.1.10)
    • YGENERAL 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
    • Y02TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
    • Y02PCLIMATE CHANGE MITIGATION TECHNOLOGIES IN THE PRODUCTION OR PROCESSING OF GOODS
    • Y02P10/00Technologies related to metal processing
    • Y02P10/20Recycling

Definitions

  • This invention relates to enzymatic dissolution of metals, such as noble metals.
  • Hydrometallurgy is concerned with processes involving aqueous solutions to extract metals from ores.
  • the most common hydrometallurgical process is leaching.
  • Leaching is a widely used extractive metallurgy technique which converts metals into soluble salts in aqueous media.
  • Gold cyanidation also known as the cyanide process or the MacArthur-Forrest process
  • cyanide process is a metallurgical technique for extracting gold from low-grade ore by converting the gold to a water-soluble coordination complex. It is the most commonly used process for gold extraction. Production of reagents for mineral processing to recover gold, copper, zinc and silver represents approximately 13% of cyanide consumption globally. Due to the highly poisonous nature of cyanide, the process is controversial and its usage is banned in a number of countries and territories.
  • compositions and methods of the invention are efficient for aqueous extraction of gold and other metals from ore, and do not impose environmental problems like cyanide does, due to the non-toxic nature of enzymes.
  • the present invention provides a method for dissolving a metal in an aqueous composition, comprising contacting the metal with a haloperoxidase, hydrogen peroxide, and a source of chloride, bromide, iodide or thiocyanate ions.
  • the metal is a base metal or a noble metal.
  • the aqueous composition also includes comminuted ore.
  • the invention provides an aqueous composition
  • a dissolved noble metal a haloperoxidase
  • chloride, bromide, iodide or thiocyanate ions in another aspect, provides an aqueous composition
  • a dissolved noble metal a haloperoxidase
  • chloride, bromide, iodide or thiocyanate ions in another aspect, provides an aqueous composition
  • a dissolved noble metal a haloperoxidase
  • chloride, bromide, iodide or thiocyanate ions a haloperoxidase
  • the metals are understood to be base metals and noble metals.
  • base metal is used to refer to a metal that oxidizes or corrodes relatively easily, and reacts variably with diluted hydrochloric acid (HCI) to form hydrogen. Copper is considered a base metal as it oxidizes relatively easily, although it does not react with HCI.
  • the base metals are understood to be copper, iron, lead, nickel and zinc; and additionally, aluminum, tin, tungsten, molybdenum, tantalum, cobalt, bismuth, cadmium, titanium, zirconium, antimony, manganese, beryllium, chromium, germanium, vanadium, gallium, hafnium, indium, niobium, rhenium and thallium.
  • the base metals are selected from group consisting of copper, iron, lead, nickel, and zinc.
  • the noble metals are metals that are resistant to corrosion and oxidation in moist air, unlike most base metals.
  • the noble metals are understood to be ruthenium, osmium, rhodium, iridium, palladium, platinum, silver, and gold.
  • the noble metals are selected from group consisting of platinum, silver, and gold.
  • metals in metallic form or as insoluble salts or compounds
  • a haloperoxidase For example, on contact with a haloperoxidase, hydrogen peroxide and chloride ions, gold may be converted to chloride complexes, such as [AuCI 4 ] ⁇ , [AuCI 3 (OH 2 )], or [AuCI 3 (OH)] ⁇ .
  • Platinum may be leached as hexachloridoplatinate(2-), which on contact with an ammonium salt, such as ammonium chloride, may be converted to ammonium hexachloridoplatinate(2-), [NH 4 ] 2 [PtCI 6 ], a well- known intermediate from which elemental platinum is easily recovered.
  • Palladium may be leached as tetrachloridopalladate(2-), [PdCI 4 ] 2 ⁇ .
  • insoluble means soluble in water in a concentration of less than 0.001 M at room temperature.
  • the metals are copper, iron, lead, nickel, zinc, platinum, silver, and gold.
  • metals for example as found in ores
  • metallic form e.g., native metal
  • salts/compounds are dissolved (leached, extracted) by the methods of the invention as water-soluble coordination complexes (metal complexes).
  • metal complexes water-soluble coordination complexes
  • a native metal is a metal that is found in its metallic form, either pure or as an alloy, in nature.
  • An ore is a type of rock that contains minerals with important valuable chemical elements, including metals.
  • the ore is then referred to as metal ore.
  • the ores are extracted through mining; these are then refined to extract the valuable chemical element(s), such as silver, gold or platinum.
  • Metal ores generally comprise metal oxides, phosphides, silicates etc., or native metals (metal elements in a metallic form).
  • the ores must be processed to extract the metals of interest from the waste rock and from other minerals.
  • the ore is comminuted using grinding machinery. Water is added to the comminuted ore to produce a slurry, and depending on the ore, it may be further concentrated by froth flotation or by centrifugal (gravity) concentration.
  • General processing steps of ores are well-known in the art, and described in, for example, WO 2004/042094 and WO 2006/064350.
  • Comminution of solid materials requires different types of crushers and mills depending on the feed properties such as hardness at various size ranges and application requirements such as throughput and maintenance.
  • the most common machines for the comminution of coarse feed material are the jaw crusher (1 m > P80 > 100 mm), cone crusher (P80 > 20 mm) and hammer crusher.
  • Primary jaw crusher product in intermediate feed particle size ranges can be ground in Autogenous or Semi-Autogenous (AG or SAG) mills depending on feed properties and application requirements.
  • AG or SAG Autogenous or Semi-Autogenous
  • the ore treated with haloperoxidase, according to the invention is preferably in the fine particle size range (20mm > P80 > 30 ⁇ ).
  • haloperoxidases suitable for being incorporated in the method of the invention include chloroperoxidases, bromoperoxidases and compounds exhibiting chloroperoxidase or bromoperoxidase activity.
  • Haloperoxidases form a class of enzymes that are capable of oxidizing halides (Cl ⁇ , Br " , ⁇ ) and thiocyanate (SCN ⁇ ) in the presence of hydrogen peroxide or a hydrogen peroxide generating system to the corresponding hypohalous acids or hypohalites; or in the case of thiocyanate, to hypothiocyanous acid or hypothiocyanite.
  • Haloperoxidases are classified according to their specificity for halide ions.
  • Chloroperoxidases (E.C. 1.1 1 .1.10) catalyze formation of hypochlorite from chloride ions, hypobromite from bromide ions and hypoiodite from iodide ions; and bromoperoxidases catalyze formation of hypobromite from bromide ions and hypoiodite from iodide ions.
  • hypohalite compounds may subsequently react with other compounds forming halogenated compounds.
  • the haloperoxidase of the invention is a chloroperoxidase.
  • Haloperoxidases have been isolated from various organisms: mammals, marine animals, plants, algae, lichen, fungi and bacteria. It is generally accepted that haloperoxidases are the enzymes responsible for the formation of halogenated compounds in nature, although other enzymes may be involved.
  • Haloperoxidases have been isolated from many different fungi, in particular from the fungus group dematiaceous hyphomycetes, such as Caldariomyces, e.g., C. fumago,
  • Curvularia e.g., C. verruculosa and C. inaequalis, Drechslera, Ulocladium and Botrytis.
  • Haloperoxidases have also been isolated from bacteria such as Pseudomonas, e.g., P. pyrrocinia and Streptomyces, e.g., S. aureofaciens.
  • the haloperoxidase is a vanadium haloperoxidase, i.e. a vanadate-containing haloperoxidase.
  • the haloperoxidase is derivable from Curvularia sp., in particular Curvularia verruculosa or Curvularia inaequalis, such as C. inaequalis CBS 102.42 as described in WO 95/27046, e.g. a vanadium haloperoxidase encoded by the DNA sequence of WO 95/27046, figure 2 all incorporated by reference; or C. verruculosa CBS 147.63 or C. verruculosa CBS 444.70 as described in WO 97/04102.
  • Curvularia sp. in particular Curvularia verruculosa or Curvularia inaequalis, such as C. inaequalis CBS 102.42 as described in WO 95/27046, e.g. a vanadium haloperoxidase encoded by the DNA sequence of WO 95/27046, figure 2 all incorporated by reference; or C. verruculosa CBS 147.63 or
  • the amino acid sequence of the haloperoxidase has at least 70% identity, preferably at least 75%, more preferably at least 80%, more preferably at least 85%, more preferably at least 90%, more preferably at least 95%, and most preferably 100% identity to the amino acid sequence of a haloperoxidase obtainable from Curvularia verruculosa (see e.g. SEQ ID NO:2 in WO 97/04102; also shown as SEQ ID NO:1 in the present
  • Curvularia inequalis e.g. the mature amino acid sequence encoded by the DNA sequence in figure 2 of WO 95/27046; also shown as SEQ ID NO:2 in the present application/sequence listing.
  • the vanadium chloroperoxidase may also be derivable from Drechslera hartlebii as described in WO 01/79459, Dendryphiella salina as described in WO 01/79458,
  • sequence identity The relatedness between two amino acid sequences is described by the parameter "sequence identity".
  • sequence identity the sequence identity between two amino acid sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al, 2000, Trends Genet. 16: 276-277), preferably version 5.0.0 or later.
  • the parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix.
  • the concentration of the haloperoxidase is typically in the range of 0.01 -100 ppm enzyme protein, preferably 0.05-50 ppm enzyme protein, more preferably 0.1 -50 ppm enzyme protein, more preferably 0.1 -30 ppm enzyme protein, more preferably 0.5-20 ppm enzyme protein, and most preferably 0.5-10 ppm enzyme protein.
  • the concentration of the haloperoxidase is typically in the range of 1 -
  • ppm enzyme protein preferably 1 -20 ppm enzyme protein, more preferably 1 -10 ppm enzyme protein.
  • An assay for determining haloperoxidase activity may be carried out by mixing 100 ⁇ _ of haloperoxidase sample (containing about 0.2 ⁇ g enzyme protein/mL) and 100 ⁇ _ of a 0.3 M sodium phosphate pH 7 buffer containing 0.5 M potassium bromide and 0.008% phenol red, adding the solution to 10 ⁇ _ of 0.3% H 2 0 2 , and measuring the absorption at 595 nm as a function of time.
  • the assay is performed in an aqueous solution of 0.1 M sodium phosphate or 0.1 M sodium acetate, 50 ⁇ monochlorodimedone, 10 mM KBr/KCI, 1 mM H 2 0 2 and about 1 ⁇ g/mL haloperoxidase.
  • the hydrogen peroxide required by the haloperoxidase may be provided as an aqueous solution of hydrogen peroxide or a hydrogen peroxide precursor for in situ production of hydrogen peroxide.
  • Any solid entity which liberates upon dissolution a peroxide, which is useable by haloperoxidase, can serve as a source of hydrogen peroxide.
  • Compounds which yield hydrogen peroxide upon dissolution in water or an appropriate aqueous based medium include but are not limited to metal peroxides, percarbonates, persulphates, perphosphates, peroxyacids, alkyperoxides, acylperoxides, peroxyesters, urea peroxide, perborates and peroxycarboxylic acids or salts thereof.
  • Another source of hydrogen peroxide is a hydrogen peroxide generating enzyme system, such as an oxidase together with a substrate for the oxidase.
  • oxidase and substrate comprise, but are not limited to, amino acid oxidase (see e.g. US 6,248,575) and a suitable amino acid, glucose oxidase (see e.g. WO 95/29996) and glucose, lactate oxidase and lactate, galactose oxidase (see e.g. WO 00/50606) and galactose, and aldose oxidase (see e.g. WO 99/31990) and a suitable aldose.
  • Alternative oxidants which may be applied for haloperoxidases may be oxygen combined with a suitable hydrogen donor like ascorbic acid, dehydroascorbic acid, dihydroxyfumaric acid or cysteine.
  • a suitable hydrogen donor like ascorbic acid, dehydroascorbic acid, dihydroxyfumaric acid or cysteine.
  • Hydrogen peroxide or a source of hydrogen peroxide may be added at the beginning of or during the method of the invention, e.g. as one or more separate additions of hydrogen peroxide; or continuously as fed-batch addition.
  • Typical amounts of hydrogen peroxide correspond to levels of from 0.001 mM to 25 mM, preferably to levels of from 0.005 mM to 5 mM, and particularly to levels of from 0.01 to 1 mM or 0.02 to 2 mM hydrogen peroxide.
  • Hydrogen peroxide may also be used in an amount corresponding to levels of from 0.1 mM to 25 mM, preferably to levels of from 0.5 mM to 15 mM, more preferably to levels of from 1 mM to 10 mM, and most preferably to levels of from 2 mM to 8 mM hydrogen peroxide.
  • Chloride ions (CI " ), bromide ions (Br), iodide ions ( ⁇ ), and/or thiocyanate ions (SCN “ ) for reaction with the haloperoxidase may be provided in many different ways, such as by adding chloride salt(s), bromide salt(s), iodide salt(s), and/or thiocyanate salts to an aqueous solution.
  • the chloride salt(s) are sodium chloride (NaCI), potassium chloride (KCI), or ammonium chloride (NH 4 CI), or mixtures thereof.
  • bromide salt(s) are sodium bromide (NaBr), potassium bromide (KBr), or ammonium bromide (NH 4 Br), or mixtures thereof.
  • the iodide salt(s) are sodium iodide (Nal), potassium iodide (Kl), or ammonium iodide (NH 4 I), or mixtures thereof
  • thiocyanate salt(s) are sodium thiocyanate (NaSCN), potassium thiocyanate (KSCN), or ammonium thiocyanate (NH 4 SCN), or mixtures thereof.
  • the concentration of chloride ions, bromide ions, iodide ions, and/or thiocyanate ions are collectively or individually in the range of from 0.01 mM to 1000 mM, preferably in the range of from 0.05 mM to 500 mM, more preferably in the range of from 0.1 mM to 100 mM, most preferably in the range of from 0.1 mM to 50 mM, and in particular in the range of from 1 mM to 25 mM.
  • the collective molar concentration of chloride ions, bromide ions, iodide ions, and/or thiocyanate ions is at least the same as the concentration of ammonium ions.
  • Ammonium ions, bromide ions, iodide ions, and/or thiocyanate ions is at least the same as the concentration of ammonium ions.
  • ammonium ions for improving the efficacy of the haloperoxidase, may be provided by adding an ammonium salt.
  • the ammonium salt is ammonium sulphate ((NH 4 ) 2 S0 4 ), ammonium carbonate ((NH 4 ) 2 C0 3 ), ammonium chloride (NH 4 CI), ammonium bromide (NH 4 Br), ammonium iodide (NH 4 I), or ammonium thiocyanate (NH 4 SCN); or a mixture thereof.
  • the concentration of ammonium ions is typically in the range of from 0.01 mM to 1000 mM, preferably in the range of from 0.05 mM to 500 mM, more preferably in the range of from 0.1 mM to 100 mM, most preferably in the range of from 0.1 mM to 50 mM, and in particular in the range of from 1 mM to 25 mM.
  • the present invention provides an enzymatic method for dissolving a metal in an aqueous composition, comprising contacting the metal with a haloperoxidase, hydrogen peroxide, and a halide ion selected from chloride, bromide, iodide and thiocyanate ions.
  • the metal may also be contacted with ammonium ions.
  • the aqueous composition contains water, and the metal is converted to a water-soluble compound.
  • the aqueous composition may also contain insoluble components, such as comminuted ore.
  • the ore is in the fine particle size range (20mm > P80 > 30 ⁇ ).
  • the aqueous composition may be slurry of water and ore particles involved in mining of metals.
  • the metal is a base metal, such as copper, iron, lead, nickel and zinc.
  • the metal is a noble metal, such as platinum, silver, or gold.
  • the present invention provides an enzymatic method for dissolving platinum, silver, or gold in an aqueous composition, comprising contacting the platinum, silver, or gold with a haloperoxidase, hydrogen peroxide, and a halide ion selected from chloride, bromide, iodide and thiocyanate ions.
  • the metal may also be contacted with ammonium ions.
  • the aqueous composition contains water, and the metal is converted to a water-soluble compound.
  • the aqueous composition may also contain insoluble components, such as comminuted ore. Preferably the ore is in the fine particle size range (20mm > P80 > 30 ⁇ ).
  • the aqueous composition may be a slurry of water and ore particles involved in mining of metals.
  • the haloperoxidase is a vanadate containing haloperoxidase, preferably a chloroperoxidase (vanadium chloroperoxidase) from enzyme class EC 1.1 1.1.10.
  • the amino acid sequence of the haloperoxidase may have at least 70% identity, preferably at least 80% identity, preferably at least 85% identity, more preferably at least 90% identity, and most preferably at least 95% identity to the amino acid sequence shown in SEQ ID NO: 1 or SEQ ID NO: 2.
  • the haloperoxidase has the amino acid sequence shown in SEQ ID NO: 1 or SEQ ID NO: 2.
  • the metal is a native metal.
  • the methods also comprise separating insoluble (comminuted) ore from the remaining aqueous composition comprising the dissolved metal.
  • the method may also comprise removing excess hydrogen peroxide after dissolving the metal. Hydrogen peroxide can be removed by adding catalase to the aqueous composition, which results in disproportionation of hydrogen peroxide to oxygen and water.
  • the invention provides an aqueous composition
  • aqueous composition comprising a noble metal in solution, a haloperoxidase; and chloride, bromide, iodide or thiocyanate ions.
  • the composition also includes comminuted ore.
  • the ore is in the fine particle size range (20mm > P80 > 30 ⁇ ).
  • the aqueous composition may be a slurry of water and ore particles involved in mining of metals.
  • the haloperoxidase is a vanadate containing haloperoxidase, preferably a chloroperoxidase (vanadium chloroperoxidase) from enzyme class EC 1.1 1.1.10.
  • the amino acid sequence of the haloperoxidase may have at least 70% identity, preferably at least 80% identity, preferably at least 85% identity, more preferably at least 90% identity, and most preferably at least 95% identity to the amino acid sequence shown in SEQ ID NO: 1 or SEQ ID NO: 2.
  • the haloperoxidase has the amino acid sequence shown in SEQ ID NO: 1 or SEQ ID NO: 2.
  • the noble metal is platinum, silver, or gold.
  • the invention also provides for use of the methods and compositions above for dissolving a metal in an aqueous composition.
  • the methods according to the invention may be carried out at a temperature between 0 and 70 degrees Celsius, preferably between 5 and 60 degrees Celsius, more preferably between 5 and 50 degrees Celsius, even more preferably between 5 and 40 degrees Celsius, even more preferably between 5 and 35 degrees Celsius, most preferably between 5 and 30 degrees Celsius, and in particular between 10 and 30 degrees Celsius.
  • the methods of the invention may employ a treatment time of from 5 minutes to 120 minutes, preferably from 5 minutes to 90 minutes, more preferably from 5 minutes to 60 minutes, more preferably from 5 minutes to 45 minutes, more preferably from 5 minutes to 30 minutes, most preferably from 5 minutes to 20 minutes, and in particular from 5 minutes to 15 minutes.
  • the methods of the invention may be carried out at a pH from pH 1 to pH 1 1 , preferably pH 2 to pH 1 1 , more preferably from pH 2 to pH 10.5.
  • a pH from pH 1 to pH 1 1 , preferably pH 2 to pH 1 1 , more preferably from pH 2 to pH 10.5.
  • Examples 1 to 4 Several examples of suitable pH are shown in Examples 1 to 4 below.
  • the present invention is further described by the following examples which should not be construed as limiting the scope of the invention.
  • haloperoxidase used in the following examples has an amino acid sequence shown as SEQ ID NO: 1.
  • the bottles were incubated over night with stirring at room temperature. After incubation, the solutions were transferred to beakers, the supernatants were discarded, and the remaining solid gold in each beaker was washed with 100 ml milli Q water. The samples were dried at 60°C, and the non-dissolved gold was weighed.
  • the bottles were incubated for 4.5 hours or 20 hours, according to Table 2, with stirring at room temperature. After incubation, the solutions were transferred to beakers, the
  • the haloperoxidase treatment was carried out in test plates (micro plates) with 384 wells each of 300 ⁇ volume, which were shaken during the treatment.
  • a microfiber cloth was placed on top of the test plate, a sheet of leaf gold, silver or platin (on parchment) was mounted on top of the cloth, a thin transparent plastic film was mounted on top of the sheet of leaf metal, and finally a test plate lid was mounted on top of the whole sandwich. The lid was firmly pressed against the test plate to ensure that no fluid could travel from one well of the test plate to another.
  • microfiber cloth was used to ensure that removal of the sheet metal was not simply due to mechanical removal during shaking of the test plate. On the other hand, this also reduced the efficiency of the treatment significantly, as compared to for example agitating or stirring (see Examples 1 -3).
  • TEST 1 When the wells in the plate were filled, the plate was set aside for 15 minutes before the test was started.
  • TEST 2 When the wells in the plate were filled, the test was started immediately. Reference: 100.000 ppm HOCI adjusted to pH ⁇ 3 was used as a positive control.

Landscapes

  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Organic Chemistry (AREA)
  • Health & Medical Sciences (AREA)
  • Wood Science & Technology (AREA)
  • Biochemistry (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Zoology (AREA)
  • Genetics & Genomics (AREA)
  • Biotechnology (AREA)
  • General Health & Medical Sciences (AREA)
  • General Engineering & Computer Science (AREA)
  • Microbiology (AREA)
  • Geology (AREA)
  • General Life Sciences & Earth Sciences (AREA)
  • Geochemistry & Mineralogy (AREA)
  • Environmental & Geological Engineering (AREA)
  • Manufacturing & Machinery (AREA)
  • Materials Engineering (AREA)
  • Mechanical Engineering (AREA)
  • Metallurgy (AREA)
  • Medicinal Chemistry (AREA)
  • Molecular Biology (AREA)
  • Biomedical Technology (AREA)
  • Enzymes And Modification Thereof (AREA)

Abstract

La présente invention concerne un procédé enzymatique pour dissoudre des métaux dans une composition aqueuse.
PCT/EP2013/059199 2012-05-02 2013-05-02 Solubilisation enzymatique de métaux WO2013164429A1 (fr)

Priority Applications (1)

Application Number Priority Date Filing Date Title
PCT/EP2013/069183 WO2014041178A2 (fr) 2012-09-15 2013-09-16 Oxydation enzymatique de minéraux sulfurés

Applications Claiming Priority (4)

Application Number Priority Date Filing Date Title
EP12166490 2012-05-02
EP12166490.8 2012-05-02
EP12184601 2012-09-15
EP12184601.8 2012-09-15

Publications (1)

Publication Number Publication Date
WO2013164429A1 true WO2013164429A1 (fr) 2013-11-07

Family

ID=48289179

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/EP2013/059199 WO2013164429A1 (fr) 2012-05-02 2013-05-02 Solubilisation enzymatique de métaux

Country Status (1)

Country Link
WO (1) WO2013164429A1 (fr)

Citations (14)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0432935A1 (fr) * 1989-11-27 1991-06-19 Geobiotics Inc Procédé de récupération et reconcentration d'or de ses minerais
WO1993011226A1 (fr) * 1991-11-27 1993-06-10 Novo Nordisk A/S Activation d'une peroxydase ou d'une haloperoxydase
WO1995027046A2 (fr) 1994-03-31 1995-10-12 Unilever Nv Compositions antimicrobiennes enzymatiques comprenant des haloperoxydases
WO1995029996A1 (fr) 1994-05-03 1995-11-09 Novo Nordisk A/S Glucose-oxydase alcaline
WO1997004102A1 (fr) 1995-07-14 1997-02-06 Novo Nordisk A/S Haloperoxydases provenant de curvularia verruculosa et acides nucleiques les codant
WO1999031990A1 (fr) 1997-12-22 1999-07-01 Novo Nordisk A/S Oxydase d'hydrate de carbone et utilisation de cette derniere dans la cuisson
WO2000050606A1 (fr) 1999-02-24 2000-08-31 Novozymes Biotech, Inc. Polypeptides presentant une activite d'oxydase de galactose et acides nucleiques codant ces polypeptides
US6248575B1 (en) 1998-05-18 2001-06-19 Novozymes Biotech, Inc. Nucleic acids encoding polypeptides having L-amino acid oxidase activity
WO2001079461A2 (fr) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides a activite haloperoxydase
WO2001079460A2 (fr) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides a activite haloperoxydase
WO2001079459A2 (fr) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides ayant une activite d'haloperoxydase et acides nucleiques qui les codent
WO2001079458A2 (fr) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides ayant une activite d'haloperoxidase
WO2004042094A1 (fr) 2002-11-06 2004-05-21 Xstrata Queensland Ltd Reduction de la consommation de cyanure dans la recuperation d'or de minerais de sulfide finement broye
WO2006064350A1 (fr) 2004-12-15 2006-06-22 Maelgwyn Mineral Services Africa (Proprietary) Limited Procede d'extraction pour des metaux tels que l'or et le platine, comprenant le broyage fin, le pulpage et l'oxygenisation

Patent Citations (14)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0432935A1 (fr) * 1989-11-27 1991-06-19 Geobiotics Inc Procédé de récupération et reconcentration d'or de ses minerais
WO1993011226A1 (fr) * 1991-11-27 1993-06-10 Novo Nordisk A/S Activation d'une peroxydase ou d'une haloperoxydase
WO1995027046A2 (fr) 1994-03-31 1995-10-12 Unilever Nv Compositions antimicrobiennes enzymatiques comprenant des haloperoxydases
WO1995029996A1 (fr) 1994-05-03 1995-11-09 Novo Nordisk A/S Glucose-oxydase alcaline
WO1997004102A1 (fr) 1995-07-14 1997-02-06 Novo Nordisk A/S Haloperoxydases provenant de curvularia verruculosa et acides nucleiques les codant
WO1999031990A1 (fr) 1997-12-22 1999-07-01 Novo Nordisk A/S Oxydase d'hydrate de carbone et utilisation de cette derniere dans la cuisson
US6248575B1 (en) 1998-05-18 2001-06-19 Novozymes Biotech, Inc. Nucleic acids encoding polypeptides having L-amino acid oxidase activity
WO2000050606A1 (fr) 1999-02-24 2000-08-31 Novozymes Biotech, Inc. Polypeptides presentant une activite d'oxydase de galactose et acides nucleiques codant ces polypeptides
WO2001079461A2 (fr) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides a activite haloperoxydase
WO2001079460A2 (fr) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides a activite haloperoxydase
WO2001079459A2 (fr) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides ayant une activite d'haloperoxydase et acides nucleiques qui les codent
WO2001079458A2 (fr) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides ayant une activite d'haloperoxidase
WO2004042094A1 (fr) 2002-11-06 2004-05-21 Xstrata Queensland Ltd Reduction de la consommation de cyanure dans la recuperation d'or de minerais de sulfide finement broye
WO2006064350A1 (fr) 2004-12-15 2006-06-22 Maelgwyn Mineral Services Africa (Proprietary) Limited Procede d'extraction pour des metaux tels que l'or et le platine, comprenant le broyage fin, le pulpage et l'oxygenisation

Non-Patent Citations (3)

* Cited by examiner, † Cited by third party
Title
NEEDLEMAN; WUNSCH, J. MOL. BIOL., vol. 48, 1970, pages 443 - 453
PASTA ET AL., BIOTECHNOLOGY & BIOENGINEERING, vol. 62, no. 4, 1999, pages 489 - 493
RICE ET AL.: "EMBOSS: The European Molecular Biology Open Software Suite", TRENDS GENET., vol. 16, 2000, pages 276 - 277

Similar Documents

Publication Publication Date Title
Feng et al. Thiosulphate leaching of gold in the presence of carboxymethyl cellulose (CMC)
Peng et al. Control of grinding conditions in the flotation of galena and its separation from pyrite
KR20200096905A (ko) 전자 폐기물로부터 금속을 회수하는 방법
Sandström et al. Bioleaching of a complex sulphide ore with moderate thermophilic and extreme thermophilic microorganisms
Jones et al. The generation of toxic reactive oxygen species (ROS) from mechanically activated sulphide concentrates and its effect on thermophilic bioleaching
US10480046B2 (en) Process for copper and/or precious metal recovery
Feng et al. The effect of iron contaminants on thiosulphate leaching of gold
WO2014198690A1 (fr) Procede de biolixiviation d'un metal present dans un materiau
Ahn et al. Comparative investigations on sulfidic gold ore processing: A novel biooxidation process option
Saitoh et al. Microbial recovery of gold from neutral and acidic solutions by the baker's yeast Saccharomyces cerevisiae
CA2721235A1 (fr) Exploitation miniere ecologique : procede de biolixiviation et de bioadsorption de metaux precieux sans cyanure
US20230313336A1 (en) Method for carbon-catalysed thiosulfate leaching of gold-bearing materials
Yang et al. Effect of biological pretreatment on flotation recovery of pyrolusite
Jorjani et al. Gold leaching from ores using biogenic lixiviants–A review
Deschênes et al. Advances in the cyanidation of silver
WO2014041178A2 (fr) Oxydation enzymatique de minéraux sulfurés
Sakai et al. Laccase-mediator system for enzymatic degradation of carbonaceous matter in the sequential pretreatment of double refractory gold ore from Syama mine, Mali
WO2013164429A1 (fr) Solubilisation enzymatique de métaux
TR201816294T4 (tr) Altın içeren oksit cevherlerin ön işlemi için yöntem.
US20140348728A1 (en) Method for Improving Gold Recovery
Mahmoodi et al. Optimizing the alkaline oxidation pretreatment of a refractory gold ore using taguchi orthogonal array method
Alshehri Microbial recovery of gold metal from untreated and pretreated electronic wastes by wild and mutated cyanogenic Bacillus megaterium
Ahmad et al. Bio-extraction of metal ions from laterite ore by Penicillium chrysogenum
CN102505079A (zh) 氰化浸出前的金精矿预处理方法
John Differential oxidation of iron sulfides to modify the Au: S ratio in the flotation concentrate product at Lihir

Legal Events

Date Code Title Description
121 Ep: the epo has been informed by wipo that ep was designated in this application

Ref document number: 13720386

Country of ref document: EP

Kind code of ref document: A1

NENP Non-entry into the national phase

Ref country code: DE

122 Ep: pct application non-entry in european phase

Ref document number: 13720386

Country of ref document: EP

Kind code of ref document: A1