CS225664B1 - Method of the saccharose inversion - Google Patents
Method of the saccharose inversion Download PDFInfo
- Publication number
- CS225664B1 CS225664B1 CS277780A CS277780A CS225664B1 CS 225664 B1 CS225664 B1 CS 225664B1 CS 277780 A CS277780 A CS 277780A CS 277780 A CS277780 A CS 277780A CS 225664 B1 CS225664 B1 CS 225664B1
- Authority
- CS
- Czechoslovakia
- Prior art keywords
- pollen
- inversion
- sucrose
- invertase
- water
- Prior art date
Links
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 title claims description 12
- 229930006000 Sucrose Natural products 0.000 title claims description 12
- 238000000034 method Methods 0.000 title claims description 4
- 235000013681 dietary sucrose Nutrition 0.000 title 1
- 229960004793 sucrose Drugs 0.000 title 1
- 239000005720 sucrose Substances 0.000 claims description 11
- 108010051210 beta-Fructofuranosidase Proteins 0.000 claims description 10
- 239000001573 invertase Substances 0.000 claims description 10
- 235000011073 invertase Nutrition 0.000 claims description 10
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 8
- 239000000725 suspension Substances 0.000 claims description 5
- 238000003756 stirring Methods 0.000 claims description 4
- 238000001914 filtration Methods 0.000 claims description 2
- 238000000926 separation method Methods 0.000 claims description 2
- 238000005119 centrifugation Methods 0.000 claims 1
- 238000005188 flotation Methods 0.000 claims 1
- 230000000694 effects Effects 0.000 description 7
- 102000004190 Enzymes Human genes 0.000 description 6
- 108090000790 Enzymes Proteins 0.000 description 6
- 229940088598 enzyme Drugs 0.000 description 6
- 239000000203 mixture Substances 0.000 description 4
- 241000257303 Hymenoptera Species 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 102000035195 Peptidases Human genes 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 235000012907 honey Nutrition 0.000 description 2
- 235000000346 sugar Nutrition 0.000 description 2
- 102000016938 Catalase Human genes 0.000 description 1
- 108010053835 Catalase Proteins 0.000 description 1
- 102000030523 Catechol oxidase Human genes 0.000 description 1
- 108010031396 Catechol oxidase Proteins 0.000 description 1
- 102000005575 Cellulases Human genes 0.000 description 1
- 108010084185 Cellulases Proteins 0.000 description 1
- 240000001980 Cucurbita pepo Species 0.000 description 1
- 235000009852 Cucurbita pepo Nutrition 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 102000005548 Hexokinase Human genes 0.000 description 1
- 108700040460 Hexokinases Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 102000009097 Phosphorylases Human genes 0.000 description 1
- 108010073135 Phosphorylases Proteins 0.000 description 1
- 235000000405 Pinus densiflora Nutrition 0.000 description 1
- 240000008670 Pinus densiflora Species 0.000 description 1
- MYEJFUXQJGHEQK-ALRJYLEOSA-N Proscillaridin Chemical compound O[C@@H]1[C@H](O)[C@@H](O)[C@H](C)O[C@H]1O[C@@H]1C=C2CC[C@H]3[C@@]4(O)CC[C@H](C5=COC(=O)C=C5)[C@@]4(C)CC[C@@H]3[C@@]2(C)CC1 MYEJFUXQJGHEQK-ALRJYLEOSA-N 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000007244 Zea mays Nutrition 0.000 description 1
- 108010019077 beta-Amylase Proteins 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 229960004903 invert sugar Drugs 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 239000011265 semifinished product Substances 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
Landscapes
- Jellies, Jams, And Syrups (AREA)
Description
Problematika inverze aacharózy je diskutována v PV 8043-75 (Jarý, Bacílek, Marková, Mark). Pro enzymatický způsob inverze je velmi důležitá otázka zdroje invertázy. Zpravidla se se získává z vhodných kmenů mikroorganismu. Schicketanz (1962) popisuje využití invertázy, obsažené v medu k přípravě invertních cukrů vhodných ke krmení včel. Podle Rinauda a dalších (1973) je medová invertáza živočišného původu, protože prokázal, že je identická s invertázou z hltanových žláz včel.The issue of inversion of aaccharosis is discussed in PV 8043-75 (Jarý, Bacílek, Marková, Mark). The question of the source of invertase is very important for the enzymatic method of inversion. It is generally obtained from suitable strains of the microorganism. Schicketanz (1962) describes the use of invertase contained in honey to prepare invert sugars suitable for bee feeding. According to Rinaud et al (1973), honey invertase is of animal origin because it has been shown to be identical to bee pharyngeal invertase.
V pylu byla zjištěna aktivita celé řady enzymů, např. alfa-, beta- amylázy, fosforylázy (Iwanami, 1960), hexokinázy (Teizo Katsumata, Yoshihisa Togasawa, 1968), katalázy, peroxidázy, polyfenoloxidázy, proteolytických enzymů a invertázy (Nevryanskaja, Dorochov, 1970), proteáz a celulázy (Simeonova, Spirova, Dimitrov, 1974).The activity of a number of enzymes has been found in pollen, eg alpha-, beta- amylase, phosphorylase (Iwanami, 1960), hexokinase (Teizo Katsumata, Yoshihisa Togasawa, 1968), catalase, peroxidase, polyphenol oxidase, proteolytic enzymes and invertase (Nevryanskaya, Dorochov) (1970), proteases and cellulases (Simeon, Spir, Dimitrov, 1974).
V další práci se Teizo Katsumata a Yoshihisa Togasawa (1968 b) zabýval podrobněji aktivitou invertázy v pylu Pinus densiflora, Zea mays a Cucurbita maxima, které však nejsou pro včely příliš přitažlivé. Zjistil, že v těchto pylech je invertáza, ale má jen nepatrnou aktivitu.In another work, Teizo Katsumata and Yoshihisa Togasawa (1968 b) dealt in more detail with invertase activity in the pollen of Pinus densiflora, Zea mays and Cucurbita maxima, which are not very attractive to bees. He found that there was invertase in these pollen, but had little activity.
Způsobem podle vynálezu se připravuje koncentrovaný mikrobiálně stálý roztok invertního cukru pomocí invertázy obsažené v pylu rostlin tak, aby se dosáhlo požadovaného stupně inverze aacharózy a požadované sušiny hotového produktu. S výhodou se invertují roztoky aacharózy suspendovaným pylem ve stanoveném tepelném režimu za neustálého míchání. Jako zdroje enzymu se s výhodou používá pylu získaného od včel pomocí pylochytů. K inverzi lzeAccording to the process of the present invention, a concentrated microbially stable invert sugar solution is prepared by invertase contained in the plant pollen so as to achieve the desired degree of inversion of aacharose and the desired dry matter of the finished product. Preferably, the aacharose solutions are inverted by the suspended pollen under a specified thermal regime with constant stirring. As an enzyme source, pollen obtained from bees by pylochytes is preferably used. Inversion is possible
225 664225 664
225 664 používat i pyly, které nesbírají včely, jestliže mají dostatečnou aktivitu invertázy. Zdroj enzymu, který je v roztoku sacharózy suspendován, lze z hotového výrobku odstanit filtrací či jinými vhodnými separačními metodami, avšak s ohledem na naprostou zdravotní nezávadnost ho lze s ohledem na využití hotového produktu v nšm ponechat.225 664 also use pollen that does not collect bees if they have sufficient invertase activity. The source of the enzyme that is suspended in the sucrose solution can be removed from the finished product by filtration or other suitable separation methods, but with respect to complete health safety it can be left in the finished product for use.
Příklad 1. 10 kg sacharózy se rozpustí v 4,45 kg vody a do směsi se přidá suspenze 10 g pylu v 50 ml vody, pH upraveno u vody na hodnotu 5. Směs se udržuje při teplotě optimální pro aktivitu enzymu, zpravidla 40 °C za neustálého míchání až je 70 % sacharózy zinvertováno a obsah vody klesne pod 25 %·Example 1. 10 kg of sucrose is dissolved in 4.45 kg of water and a suspension of 10 g of pollen in 50 ml of water is added to the mixture, pH adjusted to 5 with water. The mixture is maintained at an optimal temperature for enzyme activity, typically 40 ° C. with continuous stirring up to 70% sucrose is inverted and the water content drops below 25% ·
Příklad 2. Na 1 tunu 60# roztoku sacharózy (polotovar výroby sacharózy z cukrovaru) se přidá suspenze 0,6 kg pylu v 3 1 vody, pH se upraví na optimální pro aktivitu enzymu a suspenze ae udržuje za stálého míchání při 40 °G až je 70 % přítomné sacharózy zinvertováno a obsah sušiny vzroste na požadovanou mez.Example 2. A suspension of 0.6 kg of pollen in 3 L of water is added to 1 ton of a 60 # sucrose solution (sucrose semi-finished product from a sugar refinery), the pH is adjusted to optimal for enzyme and suspension activity and maintained under stirring at 40 ° C to 70% of the sucrose present is inverted and the dry matter content increases to the desired limit.
Příklad 3. Na 10 kg 40# roztoku sacharózy se přidá suspenze 6 g pylu v 30 ml vody o pH upravené na optimální pro aktivitu enzymu, a směs se udržuje při 40 °C až se dosáhne požadovaný stupeň inverze(lze dosáhnout až 95 % inverze). Suspendovaný pyl se odfiltruje v tlakových filtrech, nebo se separuje na odstředivkách. Směs se zahustí při teplotě 60 °C na požadovaný stupeň sušiny sacharózou. Obsah vody lze snížit i na vakuové odparce.Example 3. A suspension of 6 g pollen in 30 ml water adjusted to optimal for enzyme activity is added to 10 kg of 40 # sucrose solution, and the mixture is maintained at 40 ° C until the desired degree of inversion is achieved (up to 95% inversion can be achieved ). The suspended pollen is filtered off in pressure filters or separated on centrifuges. The mixture is concentrated at 60 ° C to the desired degree of sucrose. The water content can also be reduced on a vacuum evaporator.
Claims (2)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CS277780A CS225664B1 (en) | 1980-04-21 | 1980-04-21 | Method of the saccharose inversion |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CS277780A CS225664B1 (en) | 1980-04-21 | 1980-04-21 | Method of the saccharose inversion |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CS225664B1 true CS225664B1 (en) | 1984-02-13 |
Family
ID=5365831
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CS277780A CS225664B1 (en) | 1980-04-21 | 1980-04-21 | Method of the saccharose inversion |
Country Status (1)
| Country | Link |
|---|---|
| CS (1) | CS225664B1 (en) |
-
1980
- 1980-04-21 CS CS277780A patent/CS225664B1/en unknown
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