EP0056073A1 - Procédé pour la préparation de tabac, et tabac ainsi préparé - Google Patents
Procédé pour la préparation de tabac, et tabac ainsi préparé Download PDFInfo
- Publication number
- EP0056073A1 EP0056073A1 EP81107416A EP81107416A EP0056073A1 EP 0056073 A1 EP0056073 A1 EP 0056073A1 EP 81107416 A EP81107416 A EP 81107416A EP 81107416 A EP81107416 A EP 81107416A EP 0056073 A1 EP0056073 A1 EP 0056073A1
- Authority
- EP
- European Patent Office
- Prior art keywords
- tobacco
- protein
- solution
- enzyme
- biomass
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
- 241000208125 Nicotiana Species 0.000 title claims abstract description 60
- 235000002637 Nicotiana tabacum Nutrition 0.000 title claims abstract description 60
- 238000000034 method Methods 0.000 title claims description 17
- 238000002360 preparation method Methods 0.000 title claims description 5
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 24
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 21
- 238000011282 treatment Methods 0.000 claims abstract description 14
- 230000002255 enzymatic effect Effects 0.000 claims abstract description 11
- 230000002503 metabolic effect Effects 0.000 claims abstract description 11
- 102000004190 Enzymes Human genes 0.000 claims description 30
- 108090000790 Enzymes Proteins 0.000 claims description 30
- 235000018102 proteins Nutrition 0.000 claims description 23
- 150000001413 amino acids Chemical class 0.000 claims description 17
- 239000002028 Biomass Substances 0.000 claims description 16
- 108010001267 Protein Subunits Proteins 0.000 claims description 15
- 150000001875 compounds Chemical class 0.000 claims description 14
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 14
- 102000002067 Protein Subunits Human genes 0.000 claims description 12
- 244000005700 microbiome Species 0.000 claims description 10
- 235000004252 protein component Nutrition 0.000 claims description 10
- 239000000470 constituent Substances 0.000 claims description 8
- 238000007792 addition Methods 0.000 claims description 4
- 238000006243 chemical reaction Methods 0.000 claims description 4
- 238000001035 drying Methods 0.000 claims description 4
- 230000000694 effects Effects 0.000 claims description 4
- 239000000796 flavoring agent Substances 0.000 claims description 4
- 235000019634 flavors Nutrition 0.000 claims description 4
- 239000012634 fragment Substances 0.000 claims description 4
- 239000002002 slurry Substances 0.000 claims description 4
- 238000003756 stirring Methods 0.000 claims description 4
- 239000000126 substance Substances 0.000 claims description 4
- 230000002797 proteolythic effect Effects 0.000 claims description 3
- 239000012736 aqueous medium Substances 0.000 claims description 2
- 239000004566 building material Substances 0.000 claims description 2
- 230000002349 favourable effect Effects 0.000 claims description 2
- 238000010438 heat treatment Methods 0.000 claims description 2
- 238000000926 separation method Methods 0.000 claims description 2
- 238000005979 thermal decomposition reaction Methods 0.000 claims description 2
- 238000012958 reprocessing Methods 0.000 claims 1
- 230000001960 triggered effect Effects 0.000 abstract 1
- 229940088598 enzyme Drugs 0.000 description 26
- 235000001014 amino acid Nutrition 0.000 description 14
- KWYUFKZDYYNOTN-UHFFFAOYSA-M Potassium hydroxide Chemical compound [OH-].[K+] KWYUFKZDYYNOTN-UHFFFAOYSA-M 0.000 description 10
- 239000000203 mixture Substances 0.000 description 9
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical class N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 5
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 4
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 4
- 241000235646 Cyberlindnera jadinii Species 0.000 description 3
- 108091005804 Peptidases Proteins 0.000 description 3
- 102000035195 Peptidases Human genes 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
- 230000003698 anagen phase Effects 0.000 description 3
- 230000015556 catabolic process Effects 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- SNICXCGAKADSCV-JTQLQIEISA-N (-)-Nicotine Chemical compound CN1CCC[C@H]1C1=CC=CN=C1 SNICXCGAKADSCV-JTQLQIEISA-N 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 230000032683 aging Effects 0.000 description 2
- 229930013930 alkaloid Natural products 0.000 description 2
- 150000001412 amines Chemical class 0.000 description 2
- 229910021529 ammonia Inorganic materials 0.000 description 2
- 239000008346 aqueous phase Substances 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 239000004615 ingredient Substances 0.000 description 2
- SNICXCGAKADSCV-UHFFFAOYSA-N nicotine Natural products CN1CCCC1C1=CC=CN=C1 SNICXCGAKADSCV-UHFFFAOYSA-N 0.000 description 2
- 229960002715 nicotine Drugs 0.000 description 2
- 229910052757 nitrogen Inorganic materials 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 238000010992 reflux Methods 0.000 description 2
- -1 tryptophan Chemical class 0.000 description 2
- VHUUQVKOLVNVRT-UHFFFAOYSA-N Ammonium hydroxide Chemical compound [NH4+].[OH-] VHUUQVKOLVNVRT-UHFFFAOYSA-N 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 239000007836 KH2PO4 Substances 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 229910002651 NO3 Inorganic materials 0.000 description 1
- NHNBFGGVMKEFGY-UHFFFAOYSA-N Nitrate Chemical compound [O-][N+]([O-])=O NHNBFGGVMKEFGY-UHFFFAOYSA-N 0.000 description 1
- IOVCWXUNBOPUCH-UHFFFAOYSA-M Nitrite anion Chemical compound [O-]N=O IOVCWXUNBOPUCH-UHFFFAOYSA-M 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- MMDJDBSEMBIJBB-UHFFFAOYSA-N [O-][N+]([O-])=O.[O-][N+]([O-])=O.[O-][N+]([O-])=O.[NH6+3] Chemical compound [O-][N+]([O-])=O.[O-][N+]([O-])=O.[O-][N+]([O-])=O.[NH6+3] MMDJDBSEMBIJBB-UHFFFAOYSA-N 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 238000005273 aeration Methods 0.000 description 1
- 150000003797 alkaloid derivatives Chemical class 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 239000000908 ammonium hydroxide Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 238000007664 blowing Methods 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 235000019504 cigarettes Nutrition 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 229910000402 monopotassium phosphate Inorganic materials 0.000 description 1
- 150000002823 nitrates Chemical class 0.000 description 1
- 150000002826 nitrites Chemical class 0.000 description 1
- 229910017464 nitrogen compound Inorganic materials 0.000 description 1
- 150000002830 nitrogen compounds Chemical class 0.000 description 1
- 238000011369 optimal treatment Methods 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- GNSKLFRGEWLPPA-UHFFFAOYSA-M potassium dihydrogen phosphate Chemical compound [K+].OP(O)([O-])=O GNSKLFRGEWLPPA-UHFFFAOYSA-M 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000004080 punching Methods 0.000 description 1
- 239000000779 smoke Substances 0.000 description 1
- 230000000391 smoking effect Effects 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000005507 spraying Methods 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 235000019505 tobacco product Nutrition 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A24—TOBACCO; CIGARS; CIGARETTES; SIMULATED SMOKING DEVICES; SMOKERS' REQUISITES
- A24B—MANUFACTURE OR PREPARATION OF TOBACCO FOR SMOKING OR CHEWING; TOBACCO; SNUFF
- A24B15/00—Chemical features or treatment of tobacco; Tobacco substitutes, e.g. in liquid form
- A24B15/18—Treatment of tobacco products or tobacco substitutes
- A24B15/20—Biochemical treatment
Definitions
- the invention relates to a process for the preparation of tobacco in which initially insoluble protein constituents and protein subunits are broken down into soluble protein fragments by enzymatic treatment and then the soluble constituents are dissolved in water and the solution obtained is separated from the treated tobacco and tobacco, prepared by this process .
- the object of the inventive method is to achieve a processed tobacco whose content of protein components and their subunits is considerably reduced, but whose content of other soluble components is not reduced as far as possible.
- the inventive method is characterized in that from the separated solution by metabolic assimilation caused by microorganisms and subsequent separation of the Biomass protein components and protein subunits and low molecular nitrogen compounds are eliminated and the solution components remaining in the residual solution are added to pretreated tobacco.
- low-molecular nitrogen compounds such as amines, ammonia, nitrate and, if present, nitrite
- the enzymatic treatment is advantageously carried out in a mixture of crushed tobacco and water in a weight ratio of 1: 3 to 1:12, preferably 1: 5. Crushed, dried, green tobacco or shredded tobacco waste can be used. If the tobacco is used in powder form, a weight ratio of tobacco to water of 1: 3 to 1: 5 is sufficient.
- the enzymatic treatment in a slurry is advantageous because it promotes an intensive action of the enzyme on the protein components and protein subunits. On the other hand, if you use whole tobacco leaves or strips - that is, stripped tobacco leaves - you need a weight ratio of tobacco to water from 1: 8 to 1:12, preferably 1:10.
- the optimal conditions for enzymatic treatment with regard to the tobacco-water ratio, the pH value, the solution and the treatment temperature depend on the enzyme used in each case. You may find them by trying.
- the optimal treatment temperature for most enzymes is between 30 0 C (degrees Celsius) and 70 ° C. Many enzymes, including proteases, have an optimum at 37 ° C. There are also proteases that are most active at much higher temperatures, such as detergent enzymes.
- the optimum pH value for many enzymes is between pH 7.0 and pH 7.5. However, the exception of the P ro- acidic proteases, such as pepsin, the pH optimum is between 1.5 and 4.
- the optimal pH is preferably adjusted with 1 N KOH ( 1 normal potassium hydroxide solution) or 85% H 3 PO 4 (phosphoric acid).
- the enzyme is used at a concentration which is selected so large that at the optimum for the used active enzyme treatment temperature ranging between 30 0 C and 70 ° C, optimum pH and stirring continuously before the enzyme 9/10 lost its original activity, the tobacco content of insoluble proteins and protein subunits is reduced to 20 to 40% (percent), preferably 33%, of the initial value.
- the desired protein reduction is not achieved by the specified enzyme breakdown, then a higher enzyme concentration is expediently used; if the desired protein reduction is achieved before the specified enzyme degradation has taken place, then the enzyme concentration was set unnecessarily high and can be reduced for later batches. So it is easy to find the concentration that is advantageous for the enzyme used by trying. If the enzyme concentration is found to be optimal, the protein reduction can be done less by stopping the treatment prematurely. Then the enzyme was not used.
- Enzymes with proteolitic activity can be used; most bacterially and mycologically formed proteolitic enzymes are suitable here. It can be pure enzymes or enzyme mixtures. A selection of suitable enzymes is given in TABLE 1 at the end of the description.
- the separated solution is expediently sterilized and then inoculated with a culture of microorganisms which has the ability to assimilate protein and protein subunits, mainly amino acids, and has been brought into its exponential growth phase and, with the addition of sugar, favorable living conditions for them Culture is kept until at least 95% of the dissolved protein fragments and other low-molecular nitrogen compounds are used as building materials for the cell's own protein of the microorganisms. Then the metabolic assimilation is stopped by separating the biomass.
- Sterilization and use in the exponential growth phase ensure that the selected culture is selective and is not contaminated by other microorganisms. Stopping metabolic assimilation ensures that only the desired reactions are caused.
- Flavorings desired in tobacco smoke are formed when the tobacco burns off through the decomposition of certain amadori compounds, which in turn arise during the thermal reaction of certain amino acids with sugar. These amino acids may not be present in the tobacco treated and mixed with the residual solution in amounts sufficient for optimum aroma formation. The salaries could be replenished by adding such amino acids or Amadori compounds. But from the viewpoint that as no F remd- the tobacco materials are to be added, and also from a cost point unfavorable.
- the invention therefore proposes to destructively hydrolyze the proteins contained in the separated biomass, the hydrolysis conditions being chosen so that those amino acids, such as tryptophan, which cannot be converted into such amadori compounds with reducing sugar and heating (Maillard reaction), which release tobacco flavors during thermal decomposition, are selectively destroyed, and then the other amino acids are reacted with reducing sugar in amadori compounds, such as, for example, aspartic acid, leucine, arginine, threonine, glutamine, glycine and valine, and that the amadori compounds thus obtained are pretreated Tobacco can be added.
- amadori compounds such as, for example, aspartic acid, leucine, arginine, threonine, glutamine, glycine and valine
- the solution constituents remaining in the residual solution and / or the amino acids separated from the biomass and / or the amadori compounds obtained therefrom are preferably added to the pretreated tobacco in finely divided form in an aqueous medium with subsequent drying of the enriched, pretreated tobacco.
- a recycled, suitably as a smoking product tobacco is achieved, which is characterized by a protein content of from 2 up to 1 0, preferably 3, dry weight per cent and a AmadoriENSsgehalt from 0.1 to 10, preferably 5.0, dry weight per cent.
- the amadori compounds are those that release tobacco flavors when thermally decayed.
- Cigarettes made from such tobacco gave the analytical values given in TABLE 2 at the end of the description.
- the pretreated tobacco that is the pressed strips, was dried in flowing warm air to a residual moisture content of 18% (percent) and stored.
- the tobacco mixture to be prepared, the solution and the pretreated tobacco were analyzed analytically. This resulted in analytical values as in TABLE 3.
- TABLE 3 shows that 58 percent by dry weight of the proteins present in the tobacco mixture to be processed has been broken down and the breakdown products have been converted into the solution.
- the solution prepared in this way was sterilized in an autoclave at 105 ° C. under pressure and then relieved of pressure and cooled to 30 ° C. and transferred to a 20 l fermenter.
- the 30 ° C, prepared solution was inoculated with 600 ml (milliliter) of a culture of Candida utilis NCYC 707 which is in its exponential growth phase.
- the inoculated solution was left in the fermenter for 8 hours with aeration and stirring.
- the pH was first stabilized to pH 5.5 with KOH (potassium hydroxide) and later with citric acid.
- the proteins, amino acids, nitrates and nitrites were broken down by metabolic assimilation.
- the biomass was centrifuged off. This gave 2.25 l of biomass with a solids content of 16%, corresponding to 360 g of anhydrous biomass.
- the supernatant obtained by centrifugation - the so-called residual solution - contained the tobacco alkaloids in the originally present concentration, but beyond that only traces of soluble nitrogen compounds.
- the total volume of the residual solution was 9.75 liters, which were kept at 20 ° C. until later use.
- the filtered-off biomass was boiled with 1 1 6N hydrochloric acid under reflux for 15 hours in a round bottom flask.
- the biomass disintegrated and the proteins were destructively hydrolyzed, the amino acid tryptophan being destroyed to such an extent that it was no longer detectable analytically after the hydrolysis.
- the hydrolyzate was separated from the biomass residues by filtration, the excess hydrochloric acid escaping.
- the dry residue which consisted largely of amino acids, was mixed with 100 ml of water and the insoluble residue was filtered off. An amino acid mixture with a water content of about 50% was obtained.
- This amino acid mixture was adjusted to pH 7 with NH 4 0H (ammonium hydroxide) and 100 g of glucose were added and the mixture was boiled under reflux in a round-bottomed flask for 2 hours, the round-bottomed flask browning and amadori compounds being formed. The still hot contents of the flask were washed out with the previously obtained residual solution, so that the soluble amadori compounds passed into the residual solution.
- NH 4 0H ammonium hydroxide
- the tobacco thus obtained had or had its full original aroma and contained alkaloid nitrogen, that is to say nicotine, in the original concentration.
- alkaloid nitrogen that is to say nicotine
- the content of protein nitrogen was reduced by 58% and the content of amine, ammonia and nitrate nitrogen by 90% compared to the original content in the tobacco used.
- Example 1 the Candida utilis NCYC 707 were used as microorganisms.
- Other microorganisms which have the ability to assimilate proteins and protein subunits and which can be used instead of the Candida utilis NCYC 707 are in TABLE 5
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Biochemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Manufacture Of Tobacco Products (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE3100715 | 1981-01-13 | ||
| DE3100715A DE3100715A1 (de) | 1981-01-13 | 1981-01-13 | Verfahren zur aufbereitung von tabak und tabak, aufbereitet nach diesem verfahren |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| EP0056073A1 true EP0056073A1 (fr) | 1982-07-21 |
| EP0056073B1 EP0056073B1 (fr) | 1984-11-07 |
Family
ID=6122481
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| EP81107416A Expired EP0056073B1 (fr) | 1981-01-13 | 1981-09-18 | Procédé pour la préparation de tabac, et tabac ainsi préparé |
| EP82100112A Expired EP0056268B1 (fr) | 1981-01-13 | 1982-01-09 | Procédé pour la préparation de tabac |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| EP82100112A Expired EP0056268B1 (fr) | 1981-01-13 | 1982-01-09 | Procédé pour la préparation de tabac |
Country Status (3)
| Country | Link |
|---|---|
| US (2) | US4407307A (fr) |
| EP (2) | EP0056073B1 (fr) |
| DE (3) | DE3100715A1 (fr) |
Families Citing this family (65)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3100715A1 (de) * | 1981-01-13 | 1982-07-22 | Fabriques de Tabac Réunies S.A., 2003 Neuchâtel | Verfahren zur aufbereitung von tabak und tabak, aufbereitet nach diesem verfahren |
| US4685478A (en) * | 1981-10-01 | 1987-08-11 | Philip Morris Incorporated | Thermophilic denitrification of tobacco |
| US4651759A (en) * | 1983-04-12 | 1987-03-24 | Philip Morris Incorporated | Start-up process for the thermophilic denitrification of tobacco |
| US4476881A (en) * | 1983-05-09 | 1984-10-16 | Brown & Williamson Tobacco Corporation | Microbial digestion of tobacco materials using mixed cultures |
| US4700727A (en) * | 1985-12-20 | 1987-10-20 | Challenger Industries, Ltd. | Method of treating lettuce and other leafy vegetable plants and products produced therefrom |
| US4716911A (en) * | 1986-04-08 | 1988-01-05 | Genencor, Inc. | Method for protein removal from tobacco |
| US4887618A (en) * | 1988-05-19 | 1989-12-19 | R. J. Reynolds Tobacco Company | Tobacco processing |
| US4941484A (en) * | 1989-05-30 | 1990-07-17 | R. J. Reynolds Tobacco Company | Tobacco processing |
| US5060669A (en) * | 1989-12-18 | 1991-10-29 | R. J. Reynolds Tobacco Company | Tobacco treatment process |
| US5099862A (en) * | 1990-04-05 | 1992-03-31 | R. J. Reynolds Tobacco Company | Tobacco extraction process |
| US5343879A (en) * | 1991-06-21 | 1994-09-06 | R. J. Reynolds Tobacco Company | Tobacco treatment process |
| US5311886A (en) * | 1991-12-31 | 1994-05-17 | Imasco Limited | Tobacco extract treatment with insoluble adsorbent |
| US5413122A (en) * | 1992-02-18 | 1995-05-09 | R. J. Reynolds Tobacco Company | Method of providing flavorful and aromatic compounds |
| US5839447A (en) * | 1993-01-11 | 1998-11-24 | Lesser; Craig | Cigarette filter containing microcapsules and sodium pyroglutamate |
| US5501238A (en) * | 1993-01-11 | 1996-03-26 | Von Borstel; Reid W. | Cigarette filter containing a humectant |
| US5746231A (en) | 1993-01-11 | 1998-05-05 | Craig Lesser | Tobacco smoke filter for removing toxic compounds |
| US6591841B1 (en) | 1996-08-01 | 2003-07-15 | Jackie Lee White | Method of providing flavorful and aromatic tobacco suspension |
| US6053175A (en) * | 1998-03-03 | 2000-04-25 | D'angelo; Carmen A. | Method for treating smoking article |
| US6048404A (en) * | 1998-05-07 | 2000-04-11 | R.J. Reynolds Tobacco Company | Tobacco flavoring components of enhanced aromatic content and method of providing same |
| US6030462A (en) * | 1998-10-22 | 2000-02-29 | R.J. Reynolds Tobacco Company | Smoking article having increased amino acid content |
| US6298858B1 (en) | 1998-11-18 | 2001-10-09 | R. J. Reynolds Tobacco Company | Tobacco flavoring components of enhanced aromatic content and method of providing same |
| US6428624B1 (en) | 1998-12-07 | 2002-08-06 | R. J. Reynolds Tobacco Co. | Method of providing flavorful and aromatic compounds |
| US6325860B1 (en) | 2000-02-15 | 2001-12-04 | R. J. Reynolds Tobacco Company | Method of providing flavorful and aromatic compounds in absence of reducing sugars |
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| CN113349415B (zh) * | 2021-07-14 | 2023-04-28 | 云南中烟工业有限责任公司 | 提升抽吸品质的低温馏分的制备及其在加热卷烟中的应用 |
| CN114788576B (zh) * | 2022-04-07 | 2023-05-16 | 河南中烟工业有限责任公司 | 一种烤甜香突出的豫烟浸膏美拉德反应香料及其制备方法和应用 |
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| US3478015A (en) * | 1966-11-14 | 1969-11-11 | Yuki Gosei Yakuhin Kogyo Kk | Process for reacting amino acid and an active carbonyl sugar in a polyhydric alcohol |
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-
1981
- 1981-01-13 DE DE3100715A patent/DE3100715A1/de not_active Ceased
- 1981-09-18 EP EP81107416A patent/EP0056073B1/fr not_active Expired
- 1981-09-18 DE DE8181107416T patent/DE3167104D1/de not_active Expired
-
1982
- 1982-01-07 US US06/337,807 patent/US4407307A/en not_active Expired - Lifetime
- 1982-01-09 EP EP82100112A patent/EP0056268B1/fr not_active Expired
- 1982-01-09 DE DE8282100112T patent/DE3260912D1/de not_active Expired
-
1983
- 1983-01-10 US US06/456,868 patent/US4537204A/en not_active Expired - Lifetime
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3478015A (en) * | 1966-11-14 | 1969-11-11 | Yuki Gosei Yakuhin Kogyo Kk | Process for reacting amino acid and an active carbonyl sugar in a polyhydric alcohol |
| LU64076A1 (fr) * | 1970-10-16 | 1972-04-21 | ||
| US3920026A (en) * | 1972-03-07 | 1975-11-18 | Liggett & Myers Inc | Tobacco with flavor enhancer |
| FR2389341A1 (fr) * | 1977-05-06 | 1978-12-01 | Tabac Fab Reunies Sa | |
| EP0024152A2 (fr) * | 1979-08-20 | 1981-02-25 | Fabriques De Tabac Reunies S.A. | Procédé en continu pour la dénitrification d'extraits de tabac |
Also Published As
| Publication number | Publication date |
|---|---|
| US4537204A (en) | 1985-08-27 |
| DE3100715A1 (de) | 1982-07-22 |
| EP0056268B1 (fr) | 1984-10-10 |
| EP0056073B1 (fr) | 1984-11-07 |
| US4407307A (en) | 1983-10-04 |
| EP0056268A1 (fr) | 1982-07-21 |
| DE3260912D1 (en) | 1984-11-15 |
| DE3167104D1 (en) | 1984-12-13 |
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