EP0407058B1 - Verfahren zur Raffination von Kohlenhydraten und gestütztes Enzym zum Gebrauch in diesem Verfahren - Google Patents
Verfahren zur Raffination von Kohlenhydraten und gestütztes Enzym zum Gebrauch in diesem Verfahren Download PDFInfo
- Publication number
- EP0407058B1 EP0407058B1 EP90306727A EP90306727A EP0407058B1 EP 0407058 B1 EP0407058 B1 EP 0407058B1 EP 90306727 A EP90306727 A EP 90306727A EP 90306727 A EP90306727 A EP 90306727A EP 0407058 B1 EP0407058 B1 EP 0407058B1
- Authority
- EP
- European Patent Office
- Prior art keywords
- enzyme
- aqueous solution
- particles
- process according
- phospholipase
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
Links
- 238000000034 method Methods 0.000 title claims abstract description 25
- 150000001720 carbohydrates Chemical class 0.000 title claims abstract description 10
- 102000004190 Enzymes Human genes 0.000 title claims description 34
- 108090000790 Enzymes Proteins 0.000 title claims description 34
- 238000007670 refining Methods 0.000 title 1
- 239000007864 aqueous solution Substances 0.000 claims abstract description 21
- 102000015439 Phospholipases Human genes 0.000 claims abstract description 20
- 108010064785 Phospholipases Proteins 0.000 claims abstract description 20
- 239000002245 particle Substances 0.000 claims abstract description 20
- 229920002472 Starch Polymers 0.000 claims abstract description 10
- 238000001914 filtration Methods 0.000 claims abstract description 10
- 235000014633 carbohydrates Nutrition 0.000 claims abstract description 9
- 239000007787 solid Substances 0.000 claims abstract description 9
- 150000001450 anions Chemical class 0.000 claims abstract description 6
- 239000011343 solid material Substances 0.000 claims abstract description 6
- 229940100445 wheat starch Drugs 0.000 claims abstract description 6
- 150000003904 phospholipids Chemical class 0.000 claims abstract description 5
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 claims description 15
- 239000000243 solution Substances 0.000 claims description 14
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 claims description 9
- 239000004793 Polystyrene Substances 0.000 claims description 7
- 229920002223 polystyrene Polymers 0.000 claims description 7
- 239000011347 resin Substances 0.000 claims description 4
- 229920005989 resin Polymers 0.000 claims description 4
- 229920002774 Maltodextrin Polymers 0.000 claims description 3
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 claims description 2
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 claims description 2
- 239000006188 syrup Substances 0.000 claims description 2
- 235000020357 syrup Nutrition 0.000 claims description 2
- 239000005913 Maltodextrin Substances 0.000 claims 1
- 229940035034 maltodextrin Drugs 0.000 claims 1
- ZIIUUSVHCHPIQD-UHFFFAOYSA-N 2,4,6-trimethyl-N-[3-(trifluoromethyl)phenyl]benzenesulfonamide Chemical compound CC1=CC(C)=CC(C)=C1S(=O)(=O)NC1=CC=CC(C(F)(F)F)=C1 ZIIUUSVHCHPIQD-UHFFFAOYSA-N 0.000 abstract description 12
- 239000000413 hydrolysate Substances 0.000 abstract description 3
- 238000013019 agitation Methods 0.000 abstract description 2
- 229940088598 enzyme Drugs 0.000 description 31
- 238000011282 treatment Methods 0.000 description 9
- 102000004169 proteins and genes Human genes 0.000 description 8
- 108090000623 proteins and genes Proteins 0.000 description 8
- ASWBNKHCZGQVJV-UHFFFAOYSA-N (3-hexadecanoyloxy-2-hydroxypropyl) 2-(trimethylazaniumyl)ethyl phosphate Chemical compound CCCCCCCCCCCCCCCC(=O)OCC(O)COP([O-])(=O)OCC[N+](C)(C)C ASWBNKHCZGQVJV-UHFFFAOYSA-N 0.000 description 6
- 230000000694 effects Effects 0.000 description 5
- 229920002125 Sokalan® Polymers 0.000 description 4
- 239000000203 mixture Substances 0.000 description 4
- 235000019698 starch Nutrition 0.000 description 4
- 239000008107 starch Substances 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 125000000129 anionic group Chemical group 0.000 description 3
- 239000000706 filtrate Substances 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 101710130006 Beta-glucanase Proteins 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- 101710121765 Endo-1,4-beta-xylanase Proteins 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- 235000014113 dietary fatty acids Nutrition 0.000 description 2
- 229930195729 fatty acid Natural products 0.000 description 2
- 239000000194 fatty acid Substances 0.000 description 2
- 150000004665 fatty acids Chemical class 0.000 description 2
- 235000021588 free fatty acids Nutrition 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 1
- 108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 description 1
- 102100022624 Glucoamylase Human genes 0.000 description 1
- 108010009736 Protein Hydrolysates Proteins 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 108090000637 alpha-Amylases Proteins 0.000 description 1
- 102000004139 alpha-Amylases Human genes 0.000 description 1
- 229940024171 alpha-amylase Drugs 0.000 description 1
- 239000003957 anion exchange resin Substances 0.000 description 1
- 238000010923 batch production Methods 0.000 description 1
- 108010019077 beta-Amylase Proteins 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 239000003729 cation exchange resin Substances 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 230000005465 channeling Effects 0.000 description 1
- 230000001143 conditioned effect Effects 0.000 description 1
- 238000010924 continuous production Methods 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 230000005484 gravity Effects 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C13—SUGAR INDUSTRY
- C13K—SACCHARIDES OBTAINED FROM NATURAL SOURCES OR BY HYDROLYSIS OF NATURALLY OCCURRING DISACCHARIDES, OLIGOSACCHARIDES OR POLYSACCHARIDES
- C13K7/00—Maltose
-
- C—CHEMISTRY; METALLURGY
- C13—SUGAR INDUSTRY
- C13K—SACCHARIDES OBTAINED FROM NATURAL SOURCES OR BY HYDROLYSIS OF NATURALLY OCCURRING DISACCHARIDES, OLIGOSACCHARIDES OR POLYSACCHARIDES
- C13K1/00—Glucose; Glucose-containing syrups
- C13K1/06—Glucose; Glucose-containing syrups obtained by saccharification of starch or raw materials containing starch
- C13K1/08—Purifying
Definitions
- the present invention relates to a process for improving the filterability of certain aqueous solutions of carbohydrate origin which contain a phospholipid and solid material and which prior to filtration are treated with a phospholipase.
- European patent application 86307549.5 publication number 219269, describes a process for the treatment of an aqueous solution of carbohydrate origin, particularly a wheat starch hydrolysate, which is difficult to filter and/or which produces a cloudy filtrate.
- the aqueous solution contains a phospholipid and the filtration and quality of the filtrate are improved by treating the solution before filtration with an enzyme composition containing a phospholipase enzyme.
- the enzyme composition which is used may contain xylanase and beta-glucanase enzymes in which case the ratio of phospholipase enzyme to total xylanase and beta-glucanase enzymes is at least 0.05:1, preferably at least 1:1; more preferably at least 5:1 and particularly at least 10:1.
- EP 219269 describes the preparation of suitable enzyme compositions for use in the treatment of the carbohydrate solutions and exemplifies a process of treatment in which a wheat starch hydrolysate is incubated with the enzyme before being filtered. Although this process is successful and is shown to give an increased filtration rate and clearer filtrate there is an increased cost to the overall process. This is made up of the enzyme cost and the plant operation time which is taken up by the incubation period necessary for the enzyme to produce its effect.
- the present invention provides a means which enables the enzyme to be used more economically and thereby reduces the cost of the treatment.
- a process in which an aqueous solution of carbohydrate origin which contains a phospholipid and difficult-to-filter solid material is treated with a phospholipase enzyme prior to filtration is characterised by the phospholipase enzyme being immobilised on and/or in the particles of a solid support and the particles bearing the enzyme being agitated in contact with the aqueous solution.
- immobilised enzymes is, in general, well known and is used in the starch industry in particular to provide continuous processes in which a starch feedstock may be treated with an alpha-amylase, beta-amylase or glucoamylase immobilised on a suitable carrier.
- alpha-amylase beta-amylase
- beta-amylase glucoamylase immobilised on a suitable carrier.
- these prior art treatments are concerned with homogeneous liquid streams which flow, usually under the effect of gravity, through fixed beds or columns of the particles of the support on which the enzyme is immobilised leaving no residue on the support.
- aqueous solutions of carbohydrate origin contain in suspension difficult-to-filter solid material (usually proteinaceous and fatty material) and, when used in conventional immobilised enzyme columns, this solid material deposits on the enzyme support, suppressing the action of the enzyme and blocking the spaces between the support particles. There is consequently a rise in the pressure drop across the bed or column leading eventually to channeling or to complete cessation of flow.
- difficult-to-filter solid material usually proteinaceous and fatty material
- the support which is used to immobilise the phospholipase in the process of the present invention may be an anion exchange resin, a cation exchange resin or a non-ionic macroporous polymer.
- the latter support is least preferred of the three types because it is our experience that a charged support provides a firmer anchorage for the enzyme which is therefore less likely to be eluted from the support when in use.
- anion exchangers rather than cation exchangers as the enzyme support since the anion exchangers absorb relatively more enzyme.
- the most suitable supports for the enzymes are weak anion exchangers which may be made from polystyrene or from phenol/formaldehyde resins, the latter being preferred.
- the particles bearing the immobilised phospholipase are agitated in contact with the aqueous solution of carbohydrate origin. Agitation may be provided by an agitator such as a stirrer but we have found that an effective way of operating the process is to use the upward flow of the aqueous solution to "fluidise" the particles of the support. In this mode of operation the particles of the support are maintained in a short column or bed with sufficient head space to enable the heavier support particles to fall back into the column or bed, while the lighter fatty and/or proteinaceous solid is carried away in the aqeuous solution.
- the majority of the support particles preferably have a diameter of 300 to 800 microns, more preferably 400 to 550 microns.
- the process of the present invention may be used in those applications described in EP 219269 and under similar conditions of pH and temperature.
- the process is particularly useful in processing various products derived from starch, particularly wheat starch hydrolysates such as maltodextrins and maltose syrups and may be operated at 20 to 110°C, preferably 50 to 100°C more preferably 40° to 70°C and at a pH up to 8 particularly 3.5 to 6.5.
- the phospholipases which are immobilised on and/or in the support are also preferably those described in EP 219269 eg.
- the enzyme compositions used to produce the supported phospholipase should suitably contain at least 5000 units phospholipase per gram total protein, preferably 15 000 units per gram, more preferably 50 000 units per gram and particularly 100 000 units per gram.
- the phospholipase is suitably of microbial origin and preferably has L1, L2, and/or C activity.
- G-ZYME phospholipase
- DUOLITE A568 (DUOLITE is a trademark) was washed with demineralised water and conditioned to pH 5 with a sodium acetate/acetic acid buffer (0.5M). The bulk of the particle size was 300 - 800 microns.
- the supported enzyme was introduced into a glass column so as to give a bed of diameter 5 cm and depth 10 cm. Means were provided to introduce aqueous solution to the base of the column and there was 400 mls free space at the top of the column above the catalyst bed.
- the aqeuous solution fed to the column was an unclarified wheat starch hydrolysate with a degree of hydrolysis corresponding to 18 DE.
- the solution had 35% dry substance and a pH of 4.8. Its temperature in the column was 50°C.
- the effectiveness of the treatment provided by the process of the invention was assessed by determining the soluble free fatty acid and soluble lysolecithin content of treated product and its filtration rate in a simulated industrial precoat drum filter (results expressed as litres filtered per square metre of filter area per hour).
- the effect of the treatment with the phospholipase is to reduce the lysolecithin content of the substrate and to increase the concentration of the free fatty acids which are the product of lysolecithin hydrolysis. Solutions with a low lysolecithin content filter better than those with a higher content.
- the substrate was fed continuously to the base of the column initially at a rate of ten bed-volumes per hour decreasing to five bed-volumes per hour.
- the support particles in the column were "fluidised” by the upward flow of the substrate which was withdrawn from the top of the column, the support particles being held in the column.
- the column was operated continuously for several days in this manner without there being any indication that the solids in the liquid feed were blocking the column or interfering in the activity of the supported enzyme.
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Emergency Medicine (AREA)
- Health & Medical Sciences (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
- Enzymes And Modification Thereof (AREA)
- Saccharide Compounds (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
Claims (10)
- Verfahren, bei dem eine ein Phospholipid und ein schwierig zu filtrierendes Feststoffmaterial enthaltende wässrige Lösung eines Kohlenhydratursprungs vor einer Filtration mit einem Phospho-lipaseenzym behandelt wird, dadurch gekennzeichnet, daß das Phospholipaseenzym auf und/oder in Teilchen eines festen Trägers immobilisiert ist und die das Enzym tragenden Teilchen in Kontakt mit der wässrigen Lösung bewegt werden.
- Verfahren nach Anspruch 1, dadurch gekennzeichnet, daß der feste Träger aus einem Anionenaustauscher besteht.
- Verfahren nach Anspruch 2, dadurch gekennzeichnet, daß der Anionenaustauscher aus einem Polystyrol or Phenol/Formaldehyd-Harz besteht.
- Verfahren nach einem der vorhergehenden Ansprüche, dadurch gekennzeichnet, daß die das Enzym tragenden Teilchen durch die Aufwärtsbewegung der wässrigen Lösung durch eine Säule oder ein Bett der Teilchen bewegt werden.
- Verfahren nach einem der vorhergehenden Ansprüche, dadurch gekennzeichnet, daß der Großteil der Teilchen des festen Trägers einen Durchmesser von 300 bis 800 µm aufweist.
- Verfahren nach einem der vorhergehenden Ansprüche, dadurch gekennzeichnet, daß die Verweilzeit der wässrigen Lösung im Verfahren bis zu etwa 12 min beträgt.
- Verfahren nach einem der vorhergehenden Ansprüche, dadurch gekennzeichnet, daß die Temperatur 40° bis 70°C beträgt.
- Verfahren nach einem der vorhergehenden Ansprüche, dadurch gekennzeichnet, daß der pH-Wert in einem Bereich von 3,5 bis 6,5 liegt.
- Verfahren nach einem der vorhergehenden Ansprüche, dadurch gekennzeichnet, daß die wässrige Lösung von Weizenstärke herrührt.
- Verfahren nach Anspruch 9, dadurch gekennzeichnet, daß die wässrige Lösung aus einer Lösung eines Maltodextrins oder eines Maltosesirups besteht.
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
GB898915299A GB8915299D0 (en) | 1989-07-04 | 1989-07-04 | Carbohydrate refining process and a supported enzyme for use therein |
GB8915299 | 1989-07-04 |
Publications (2)
Publication Number | Publication Date |
---|---|
EP0407058A1 EP0407058A1 (de) | 1991-01-09 |
EP0407058B1 true EP0407058B1 (de) | 1994-10-12 |
Family
ID=10659500
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
EP90306727A Expired - Lifetime EP0407058B1 (de) | 1989-07-04 | 1990-06-20 | Verfahren zur Raffination von Kohlenhydraten und gestütztes Enzym zum Gebrauch in diesem Verfahren |
Country Status (7)
Country | Link |
---|---|
EP (1) | EP0407058B1 (de) |
AT (1) | ATE112805T1 (de) |
DE (1) | DE69013241T2 (de) |
DK (1) | DK0407058T3 (de) |
ES (1) | ES2060952T3 (de) |
FI (1) | FI100026B (de) |
GB (1) | GB8915299D0 (de) |
Families Citing this family (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CZ286747B6 (en) * | 1995-06-27 | 2000-06-14 | Unilever Nv | Enzyme immobilization process |
DE19620649A1 (de) * | 1996-05-22 | 1997-11-27 | Roehm Gmbh | Rekombinant hergestellte Lysophospholipase aus Aspergillus |
TR199901337T2 (xx) * | 1996-12-19 | 1999-10-21 | Unilever N.V. | Hareketsizle�tirilmi� enzim ve bunun trigliserit ya�lar�n�n i�lemden ge�irilmesinde kullan�lmas�. |
KR20020043349A (ko) * | 2000-12-04 | 2002-06-10 | 김병기 | 고정화 포스포리파제 a-2 및 이를 이용한 인지질 또는그를 포함하는 레시틴의 가수분해방법 |
Family Cites Families (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
FR2372653A1 (fr) * | 1976-12-03 | 1978-06-30 | Anvar | Resines echangeuses d'ions porteuses d'enzymes, leur procede d'obtention et leur application |
GB8525012D0 (en) * | 1985-10-10 | 1985-11-13 | Cpc International Inc | Carbohydrate refining process |
-
1989
- 1989-07-04 GB GB898915299A patent/GB8915299D0/en active Pending
-
1990
- 1990-06-20 ES ES90306727T patent/ES2060952T3/es not_active Expired - Lifetime
- 1990-06-20 DK DK90306727.0T patent/DK0407058T3/da active
- 1990-06-20 AT AT90306727T patent/ATE112805T1/de not_active IP Right Cessation
- 1990-06-20 DE DE69013241T patent/DE69013241T2/de not_active Expired - Fee Related
- 1990-06-20 EP EP90306727A patent/EP0407058B1/de not_active Expired - Lifetime
- 1990-07-02 FI FI903329A patent/FI100026B/fi not_active IP Right Cessation
Also Published As
Publication number | Publication date |
---|---|
ES2060952T3 (es) | 1994-12-01 |
GB8915299D0 (en) | 1989-08-23 |
FI903329A0 (fi) | 1990-07-02 |
EP0407058A1 (de) | 1991-01-09 |
DE69013241T2 (de) | 1995-02-23 |
DE69013241D1 (de) | 1994-11-17 |
DK0407058T3 (da) | 1995-02-27 |
FI100026B (fi) | 1997-08-29 |
ATE112805T1 (de) | 1994-10-15 |
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