NO164421B - PROCEDURE FOR STABILIZING ALFA AMYLASES AND / OR BETA GLUCANASES. - Google Patents
PROCEDURE FOR STABILIZING ALFA AMYLASES AND / OR BETA GLUCANASES. Download PDFInfo
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- NO164421B NO164421B NO834679A NO834679A NO164421B NO 164421 B NO164421 B NO 164421B NO 834679 A NO834679 A NO 834679A NO 834679 A NO834679 A NO 834679A NO 164421 B NO164421 B NO 164421B
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- Prior art keywords
- enzymes
- amylases
- solid carrier
- glucanases
- stated
- Prior art date
Links
- 238000000034 method Methods 0.000 title claims description 16
- 230000000087 stabilizing effect Effects 0.000 title claims description 4
- 108700038091 Beta-glucanases Proteins 0.000 title abstract description 5
- 102000013142 Amylases Human genes 0.000 title 1
- 108010065511 Amylases Proteins 0.000 title 1
- 229940025131 amylases Drugs 0.000 title 1
- 102000004190 Enzymes Human genes 0.000 claims abstract description 36
- 108090000790 Enzymes Proteins 0.000 claims abstract description 36
- 229940088598 enzyme Drugs 0.000 claims abstract description 36
- 239000007787 solid Substances 0.000 claims abstract description 19
- 230000000694 effects Effects 0.000 claims abstract description 11
- 108090000637 alpha-Amylases Proteins 0.000 claims abstract description 10
- 102000004139 alpha-Amylases Human genes 0.000 claims abstract description 10
- 238000000855 fermentation Methods 0.000 claims abstract description 6
- 230000004151 fermentation Effects 0.000 claims abstract description 6
- 230000001476 alcoholic effect Effects 0.000 claims abstract description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 5
- 240000008042 Zea mays Species 0.000 claims description 14
- 235000002017 Zea mays subsp mays Nutrition 0.000 claims description 14
- 235000013339 cereals Nutrition 0.000 claims description 8
- 241001465754 Metazoa Species 0.000 claims description 5
- 235000016383 Zea mays subsp huehuetenangensis Nutrition 0.000 claims description 4
- 229940024171 alpha-amylase Drugs 0.000 claims description 4
- 235000009973 maize Nutrition 0.000 claims description 4
- 239000000463 material Substances 0.000 claims description 2
- 239000007788 liquid Substances 0.000 abstract description 16
- 238000004519 manufacturing process Methods 0.000 abstract description 9
- 239000006227 byproduct Substances 0.000 abstract description 3
- 238000004821 distillation Methods 0.000 abstract description 2
- 238000003860 storage Methods 0.000 abstract description 2
- 238000005507 spraying Methods 0.000 abstract 1
- 235000013311 vegetables Nutrition 0.000 abstract 1
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 10
- 235000005822 corn Nutrition 0.000 description 10
- 239000000203 mixture Substances 0.000 description 5
- 244000144977 poultry Species 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 4
- 238000009826 distribution Methods 0.000 description 4
- 101710130006 Beta-glucanase Proteins 0.000 description 3
- 241000209219 Hordeum Species 0.000 description 3
- 235000007340 Hordeum vulgare Nutrition 0.000 description 3
- 239000000969 carrier Substances 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 108010068370 Glutens Proteins 0.000 description 2
- 108700040099 Xylose isomerases Proteins 0.000 description 2
- 238000001035 drying Methods 0.000 description 2
- 230000002255 enzymatic effect Effects 0.000 description 2
- 235000021312 gluten Nutrition 0.000 description 2
- 238000000265 homogenisation Methods 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 239000002243 precursor Substances 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 1
- 108010059892 Cellulase Proteins 0.000 description 1
- 101001094831 Homo sapiens Phosphomannomutase 2 Proteins 0.000 description 1
- 108010093096 Immobilized Enzymes Proteins 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102100035362 Phosphomannomutase 2 Human genes 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 238000011138 biotechnological process Methods 0.000 description 1
- 239000002775 capsule Substances 0.000 description 1
- 229940106157 cellulase Drugs 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 239000000446 fuel Substances 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- 235000005985 organic acids Nutrition 0.000 description 1
- 238000005502 peroxidation Methods 0.000 description 1
- 235000018102 proteins Nutrition 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
- C12N9/2411—Amylases
- C12N9/2414—Alpha-amylase (3.2.1.1.)
- C12N9/2422—Alpha-amylase (3.2.1.1.) from plant source
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K20/00—Accessory food factors for animal feeding-stuffs
- A23K20/10—Organic substances
- A23K20/189—Enzymes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/02—Enzymes or microbial cells immobilised on or in an organic carrier
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
- C12N9/2411—Amylases
- C12N9/2414—Alpha-amylase (3.2.1.1.)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/96—Stabilising an enzyme by forming an adduct or a composition; Forming enzyme conjugates
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01001—Alpha-amylase (3.2.1.1)
Abstract
Description
Foreliggende oppfinnelse vedrører en fremgangsmåte -for stabilisering av a-amylaser og/eller (5-glukanaser, og det særegne ved fremgangsmåten i henhold til oppfinnelsen er at de nevnte enzymer fordeles på en fast bærer som omrøres kontinuerlig, og som har en vannaktivitet på høyst 0,55 og et høyt proteininnhold. The present invention relates to a method - for stabilizing α-amylases and/or β-glucanases, and the peculiarity of the method according to the invention is that the mentioned enzymes are distributed on a solid carrier which is stirred continuously, and which has a water activity of at most 0.55 and a high protein content.
Oppfinnelsen vedrører også a-amylaser og/eller fj-glukanaser som er stabilisert ved hjelp av nevnte fremgangsmåte, samt fSrstoff, omfattende minst en av nevnte a-amylaser eller p-glukanaser. The invention also relates to α-amylases and/or β-glucanases which are stabilized by means of the aforementioned method, as well as starting material, comprising at least one of the aforementioned α-amylases or β-glucanases.
Disse og andre trekk ved oppfinnelsen fremgår av patentkravene. These and other features of the invention appear in the patent claims.
Oppfinnelsen har særlig betydning på området med stabilisering av slike enzymer for fSring av spesielt enmavedyr. The invention is of particular importance in the area of stabilization of such enzymes for the production of monogastric animals in particular.
Enzymer anvendes stadig hyppigere industrielt, spesielt ved slike bioteknologiske prosesser som benevnes fermenteringer. Enzymes are increasingly used industrially, especially in biotechnological processes called fermentations.
Av denne grunn er det blitt aktuelt med stadig mer og mer aktive enzymer og følgelig nedsettes den mengde som anvendes ved en og samme prosess, noe som medfører en reduksjon av omkostningene ved prosessen. For this reason, it has become relevant to use more and more active enzymes and consequently the amount used in one and the same process is reduced, which entails a reduction in the costs of the process.
Generelt markedsføres enzymene i form av væske eller pulver, tørket eller samtørket med forskjellige sukkermoleky.ler for å øke deres termiske stabilitet i det siste tilfellet. Oftest medfører tørkingen tap av enzymaktivitet med derav følgende ulemper. In general, the enzymes are marketed in liquid or powder form, dried or co-dried with different sugar molecules to increase their thermal stability in the latter case. Most often, the drying results in a loss of enzyme activity, with consequent disadvantages.
På det teknologiske plan anvendes enzymene i prinsippet i form av følgende to former: frie eller immobilisert ved hjelp av forskjellige teknikker. I tilfellet av immobiliserte enzymer skiller man vanligvis mellom enzymer som er tilknyttet ved adsorpsjon, d.v.s. kovalente bindinger som f.eks. glukoseisomeraseproduktet som selges av det amerikanske selskap CPC International Inc., og enzymer innesluttet i en kapsel eller en grunnmasse som f.eks. glukoseisomeraseproduktet som markeds-føres, av det italienske selskap Snamprogetti. Et enzym kan således immobiliseres på en av de to nevnte måter. On the technological level, the enzymes are used in principle in the form of the following two forms: free or immobilized using different techniques. In the case of immobilized enzymes, a distinction is usually made between enzymes which are associated by adsorption, i.e. covalent bonds such as the glucose isomerase product sold by the American company CPC International Inc., and enzymes contained in a capsule or a matrix such as e.g. the glucose isomerase product marketed by the Italian company Snamprogetti. An enzyme can thus be immobilized in one of the two ways mentioned.
Generelt gjennomføres fikseringen av enzymene når substratet er oppløselig eller dispergerbart. På denne måte kommer substratet i direkte kontakt med enzymet slik at mekaniske bar-riereproblemer ikke forekommer. På matområdet, både for mennesker og dyr, omhandler mange publikasjoner anvendelse av forskjellige enzymer for å avhjelpe en fysiologisk mangel. Således suppleres et byggholdig for for fjærkre med ct-amylase eller p-glukanase, eller et silof6r av korn for storfe med særlig proteaser, a-amylase eller cellulase. Resultatene er imidlertid ikke alltid overbevisende, d.v.s. at enzymene ikke fører til noen gunstig effekt og har endog en negativ virkning. In general, the fixation of the enzymes is carried out when the substrate is soluble or dispersible. In this way, the substrate comes into direct contact with the enzyme so that mechanical barrier problems do not occur. In the area of food, both for humans and animals, many publications deal with the use of different enzymes to remedy a physiological deficiency. Thus, a barley-containing feed for poultry is supplemented with α-amylase or β-glucanase, or a grain silo for cattle with particular proteases, α-amylase or cellulase. However, the results are not always convincing, i.e. that the enzymes do not lead to any beneficial effect and even have a negative effect.
Den mengde flytende enzymer som er biologisk effektiv viser seg ofte å være meget liten, vanligvis under 150 ml for 100 kg ferdig for. Dette utgjør en teknologisk hindring ved anvendelse av de flytende enzymer ved selve fremstillingen av fåret. Betingelsene for å konservere de flytende enzymer er blant annet forholdsvis snevre, spesielt ved at enzymene bør lagres ved en temperatur på +4°C. The amount of liquid enzymes that is biologically effective often turns out to be very small, usually below 150 ml per 100 kg finished for. This constitutes a technological obstacle when using the liquid enzymes in the actual production of the sheep. The conditions for preserving the liquid enzymes are, among other things, relatively strict, especially in that the enzymes should be stored at a temperature of +4°C.
Et formål for den foreliggende oppfinnelse er å tilveiebringe en fremgangsmåte for stabilisering av flytende enzymer som tillater konservering av disse ved vanlig temperatur, videre å oppnå et enzym som bibeholder sin aktivitet under lagring og hvor det flytende stabiliserte enzym ikke fremviser noe aktivitetstap under de forskjellige faser for fremstilling av f6ret, uansett typen av dette (pulver, korn eller biter). An aim of the present invention is to provide a method for stabilizing liquid enzymes which allows their conservation at normal temperature, further to obtain an enzyme which retains its activity during storage and where the liquid stabilized enzyme does not show any loss of activity during the different phases for the production of the feed, regardless of its type (powder, grain or pieces).
Oppfinnelsen muliggjør således fremstilling av et f6r inneholdende enzymer som er effektivt stabilisert og som er spesielt egnet for fQring av enmavedyr. The invention thus enables the production of a feed containing enzymes which is effectively stabilized and which is particularly suitable for feeding monogastric animals.
Mengden enzymer er fordelaktig mellom 0,5 og 100 ml pr. kg fast bærer. The amount of enzymes is advantageously between 0.5 and 100 ml per kg solid carrier.
Den faste bærer skriver seg fordelaktig fra alkoholgjæring av maiskorn eller fremstilling av etanol og betegnes vanligvis som et "brenneriprodukt". The solid carrier is advantageously obtained from the alcoholic fermentation of corn kernels or the production of ethanol and is usually referred to as a "distillery product".
Foretrukket underkastes den faste bærer på forhånd en behand-ling med organiske syrer for å unngå enhver forurensning. The solid carrier is preferably subjected to a treatment with organic acids in advance to avoid any contamination.
Fordelaktig frembyr den faste bærer en kornstørrelse under Advantageously, the solid support provides a grain size below
1 mm. 1 mm.
Ved fordeling av et flytende enzym på en fast bærer fra alkoholgjæring av maiskorn blir det flytende enzym absorbert på den faste bærer slik at dette kan frigis i vandig miljø for hydrolysering av et substrat. When distributing a liquid enzyme on a solid carrier from alcoholic fermentation of maize grain, the liquid enzyme is absorbed on the solid carrier so that it can be released in an aqueous environment for the hydrolysis of a substrate.
Som det er antydet i det foregående utgjøres de faste bærere As indicated above, they constitute fixed carriers
i første rekke av biprodukter fra fremstillingen av etanol som drank som tømmes ut fra brenneriene (brenneridrank eller DSG) eller fra alkoholgjæring av mais som de fraksjoner rike på proteiner som oppnås etter destillasjon. Disse fraksjoner omfatter brenneridrank og en oppløselig fraksjon. I dette tilfellet er de vesentlige biprodukter brenneriavfall fra mais inneholdende oppløselige bestanddeler (tørkede korn fra maisbrennerier med oppløselige bestanddeler eller DCGS), tørket brenneridrank fra mais (tørkede korn fra maisbrennerier eller CDG) og tørkede oppløselige bestanddeler fra maisbrenneri (tørkede oppløselige bestanddeler fra maisbrennerier eller CDS). Som en annen type av faste bærere kan nevnes produkter på basis av maisgluten (masiglutenf6r eller CGF). Den midlere verdi av de viktigste fysikalsk-kjemiske egenskaper og den midlere sammensetning av disse forskjellige produkter er angitt i den etterfølgende tabell. in the first place of by-products from the production of ethanol that was drunk that is discharged from the distilleries (distillers or DSG) or from the alcoholic fermentation of corn as the fractions rich in proteins obtained after distillation. These fractions comprise burner grade and a soluble fraction. In this case, the main by-products are corn roaster waste containing solubles (dried grains from corn distillers with solubles or DCGS), dried corn roasters (dried grains from corn roasters or CDG) and dried solubles from corn roasters (dried solubles from corn roasters or CDS). As another type of solid carrier, products based on maize gluten (maize gluten f6r or CGF) can be mentioned. The average value of the most important physico-chemical properties and the average composition of these different products are indicated in the following table.
De vesentlige egenskaper av de faste bærere slik som angitt The essential properties of the solid carriers as indicated
i den nevnte tabell er: in the aforementioned table are:
- en forholdsvis lav pH på omtrent 5, - a relatively low pH of approximately 5,
en lav vannaktivitet (Aw) fordelaktig under 0,55, a low water activity (Aw) advantageously below 0.55,
et lavt innhold av fettmaterial for å unngå enhver per-oksydering av enzymatisk type som kan føre til frie radikaler som kan denaturere de flytende enzymer som skal stabiliseres. a low content of fatty material to avoid any peroxidation of an enzymatic type which may lead to free radicals which may denature the liquid enzymes to be stabilized.
De faste bærere skal blant annet ikke fremby noen egenenzyma-tisk aktivitet som kan forstyrre enzymaktiviteten av de stabiliserte enzymer. Among other things, the solid carriers must not present any intrinsic enzymatic activity that could interfere with the enzyme activity of the stabilized enzymes.
Den mengde flytende enzymer som er fordelt på den faste bærer som omrøres kontinuerlig er mellom 0,5 og 100 ml pr. kg fast bærer. Den maksimale fordelingsgrad er på den ene side begrenset av den maksimale vannaktivitet (Aw) som tillater veksten av mikroorganismer - som skal unngås - og på den annen side av stivningen og tilsvarende tap av fluiditet. The amount of liquid enzymes that is distributed on the solid carrier that is stirred continuously is between 0.5 and 100 ml per kg solid carrier. The maximum degree of distribution is limited on the one hand by the maximum water activity (Aw) which allows the growth of microorganisms - which must be avoided - and on the other hand by the stiffening and corresponding loss of fluidity.
De etterfølgende eksempler illustrerer oppfinnelsen. The following examples illustrate the invention.
EKSEMPEL 1 EXAMPLE 1
I et apparat av type"24 ACCELA-COTA DE MANESTY" anvendt for overtrekking av presskaker og hvori åpningene som vanlig tjener til injeksjon av varm luft for tørking munner ut, innføres 6 kg tørr drank fra maisbrenneri (CDG). Under rotasjon av apparatet med en hastighet på omtrent 12 omdreininger pr. minutt fordeles i løpet av seks minutter en flytende p-glukanase ved hjelp av en pistoldyse med diameter 0,8 mm. Fordelingstakten er 5 0 ml/min. med et lufttrykk på In an apparatus of the type "24 ACCELA-COTA DE MANESTY" used for coating pressed cakes and in which the openings which normally serve for the injection of hot air for drying open out, 6 kg of dry liquor from corn distillery (CDG) are introduced. During rotation of the apparatus at a speed of approximately 12 revolutions per minute, a liquid p-glucanase is distributed over the course of six minutes using a gun nozzle with a diameter of 0.8 mm. The distribution rate is 50 ml/min. with an air pressure on
3,5-10^ paskal. Etter en homogeniseringstid på omtrent tre minutter stanses omdreiningen av beholderen og man oppnår den stabiliserte flytende p-glukanase. 3.5-10^ pascals. After a homogenization time of approximately three minutes, the rotation of the container is stopped and the stabilized liquid β-glucanase is obtained.
Enzymet stabilisert på denne måte tilsettes f.eks. til et The enzyme stabilized in this way is added, e.g. to a
f6r for fjærkre hvor sammensetningen kan omfatte et innhold av bygg på mellom 5 og 7 0 vekt%. Den etterfølgende tabell gir en sammensetning av et fjærkrefår omfattende et flytende enzym stabilisert i samsvar med fremgangsmåten for den foreliggende oppfinnelse. f6r for poultry where the composition may include a barley content of between 5 and 70% by weight. The following table gives a composition of a poultry feed comprising a liquid enzyme stabilized in accordance with the method of the present invention.
EKSEMPEL 2 EXAMPLE 2
I en horisontal blander med romfang 5000 liter inneholdende ti dyser for fordeling innføres 2200 kg brenneridrank av mais inneholdende oppløselige bestanddeler (CDGS), idet omdreinings hastigheten for blanderen holdes ved 20 omdreininger pr. minutt. Fordelingen av en blanding av [J-glukanase og a-amylase gjennomføres i løpet av 6,5 minutter med en takt på 140 l/time under et lufttrykk på 4,1-IO<5> paskal. In a horizontal mixer with a volume of 5,000 liters containing ten nozzles for distribution, 2,200 kg of burner fuel of corn containing soluble components (CDGS) is introduced, the speed of rotation of the mixer being kept at 20 revolutions per minute. minute. The distribution of a mixture of β-glucanase and α-amylase is carried out within 6.5 minutes at a rate of 140 l/hour under an air pressure of 4.1-10<5> pascal.
Etter tre minutters homogenisering gjenvinnes den stabiliserte flytende enzymblanding som kan innføres i en mengde på 0,5 eller 1 vekt% i et forstoff for fjærkre som kan inneholde fra til 70 vekt% bygg. After three minutes of homogenization, the stabilized liquid enzyme mixture is recovered, which can be introduced in an amount of 0.5 or 1% by weight in a precursor for poultry which can contain from to 70% by weight of barley.
Ved fremgangsmåten i henhold til oppfinnelsen muliggjøres fremstilling av flytende enzymer som er stabilisert på en fast bærer og som kan utgjøre et konsentrat som kan anvendes for fremstilling av et forstoff for enmavedyr, spesielt fjærkre. The method according to the invention enables the production of liquid enzymes which are stabilized on a solid carrier and which can constitute a concentrate which can be used for the production of a precursor for monogastric animals, especially poultry.
Claims (6)
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
FR8221302A FR2537991A1 (en) | 1982-12-20 | 1982-12-20 | PROCESS FOR STABILIZING LIQUID ENZYMES, LIQUID ENZYMES SO STABILIZED AND FOOD COMPRISING SUCH ENZYMES, IN PARTICULAR FOR MONOGASTRIC ANIMALS |
Publications (3)
Publication Number | Publication Date |
---|---|
NO834679L NO834679L (en) | 1984-06-21 |
NO164421B true NO164421B (en) | 1990-06-25 |
NO164421C NO164421C (en) | 1990-10-03 |
Family
ID=9280267
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO834679A NO164421C (en) | 1982-12-20 | 1983-12-19 | PROCEDURE FOR STABILIZING ALFA AMYLASES AND / OR BETA GLUCANASES. |
Country Status (10)
Country | Link |
---|---|
EP (1) | EP0113626B1 (en) |
AT (1) | ATE38249T1 (en) |
AU (1) | AU567322B2 (en) |
DE (1) | DE3378323D1 (en) |
DK (1) | DK161717C (en) |
ES (1) | ES528164A0 (en) |
FI (1) | FI78317C (en) |
FR (1) | FR2537991A1 (en) |
IE (1) | IE56328B1 (en) |
NO (1) | NO164421C (en) |
Families Citing this family (10)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
IL74177A (en) * | 1984-02-03 | 1989-09-10 | Abbott Lab | Stabilized enzyme conjugate composition containing a calcium salt and a polyethylene glycol |
US4707287A (en) * | 1985-06-28 | 1987-11-17 | The Procter & Gamble Company | Dry bleach stable enzyme composition |
FI77359C (en) * | 1986-08-22 | 1989-03-10 | Suomen Sokeri Oy | Feed fix and process for making the same. |
US5314692A (en) * | 1987-08-24 | 1994-05-24 | Cultor Ltd. | Enzyme premix for feed and method |
US5256788A (en) * | 1989-02-13 | 1993-10-26 | Nippon Shinyaku Co. Ltd. | Moranoline derivatives and their production and the use of moranoline and its derivatives as a stabilizing agent for enzymes |
DK13491D0 (en) * | 1991-01-25 | 1991-01-25 | Novo Nordisk As | APPLICATION OF AN ENZYMOUS GRANULATE AND PROCEDURE FOR PREPARING A TABLET FORM |
LT3208B (en) * | 1992-04-10 | 1995-03-27 | Ssv Dev Oy | Enzyme products for use in the improvement of feed value and conservation of fibrous crops |
DE10157069A1 (en) * | 2001-11-12 | 2003-05-28 | Ipc Process Ct Gmbh | Nutritional supplements for animal feeds are obtained by infiltrating enzymes into de-husked grain by a simple low-energy solution spraying process |
JP2018519794A (en) | 2015-04-28 | 2018-07-26 | マース インコーポレーテッドMars Incorporated | Method of preparing a sterilized wet type pet food product |
CN107937435A (en) * | 2018-01-08 | 2018-04-20 | 安徽省农业科学院水稻研究所 | A kind of method for strengthening crop resistant storage properties |
Family Cites Families (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
GB191229996A (en) * | 1912-12-30 | 1913-10-09 | Max Hamburg | A Process of Raising the Nutritive Value of Brewery Grains and Obtaining a New or Improved Food for Cattle. |
US2594356A (en) * | 1949-06-24 | 1952-04-29 | Us Agriculture | Isolation of alpha-amylase from malt extract |
GB869615A (en) * | 1957-04-12 | 1961-05-31 | James Mcginnis | Animal feedstuffs |
US3617300A (en) * | 1967-12-28 | 1971-11-02 | Gen Mills Inc | In situ conversion of starch |
FR2000884A1 (en) * | 1968-01-29 | 1969-09-19 | Inst Cercetari Alime | |
NL7103490A (en) * | 1970-03-18 | 1971-09-21 | ||
DE2602260A1 (en) * | 1976-01-22 | 1977-08-04 | Henkel & Cie Gmbh | PROCESS FOR THE PRODUCTION OF ENZYME-CONTAINING ANIMAL FEED |
-
1982
- 1982-12-20 FR FR8221302A patent/FR2537991A1/en active Granted
-
1983
- 1983-12-08 IE IE2887/83A patent/IE56328B1/en not_active IP Right Cessation
- 1983-12-14 FI FI834595A patent/FI78317C/en not_active IP Right Cessation
- 1983-12-19 EP EP83402461A patent/EP0113626B1/en not_active Expired
- 1983-12-19 NO NO834679A patent/NO164421C/en unknown
- 1983-12-19 DE DE8383402461T patent/DE3378323D1/en not_active Expired
- 1983-12-19 ES ES528164A patent/ES528164A0/en active Granted
- 1983-12-19 AT AT83402461T patent/ATE38249T1/en not_active IP Right Cessation
- 1983-12-20 DK DK585783A patent/DK161717C/en not_active IP Right Cessation
-
1984
- 1984-02-13 AU AU24547/84A patent/AU567322B2/en not_active Ceased
Also Published As
Publication number | Publication date |
---|---|
DK161717B (en) | 1991-08-05 |
EP0113626B1 (en) | 1988-10-26 |
NO164421C (en) | 1990-10-03 |
EP0113626A1 (en) | 1984-07-18 |
AU2454784A (en) | 1985-08-22 |
FI834595A (en) | 1984-06-21 |
DK585783D0 (en) | 1983-12-20 |
FI78317C (en) | 1989-07-10 |
DK161717C (en) | 1992-01-20 |
FR2537991A1 (en) | 1984-06-22 |
FI78317B (en) | 1989-03-31 |
IE56328B1 (en) | 1991-06-19 |
FR2537991B1 (en) | 1985-03-15 |
ES8502474A1 (en) | 1985-01-01 |
AU567322B2 (en) | 1987-11-19 |
NO834679L (en) | 1984-06-21 |
ATE38249T1 (en) | 1988-11-15 |
IE832887L (en) | 1984-06-20 |
FI834595A0 (en) | 1983-12-14 |
DE3378323D1 (en) | 1988-12-01 |
ES528164A0 (en) | 1985-01-01 |
DK585783A (en) | 1984-06-21 |
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