CN107594068A - A kind of be crosslinked using tyrosinase reduces knife volume newly to the method for shrimp allergen tropomyosin allergenicity - Google Patents
A kind of be crosslinked using tyrosinase reduces knife volume newly to the method for shrimp allergen tropomyosin allergenicity Download PDFInfo
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- CN107594068A CN107594068A CN201710873022.2A CN201710873022A CN107594068A CN 107594068 A CN107594068 A CN 107594068A CN 201710873022 A CN201710873022 A CN 201710873022A CN 107594068 A CN107594068 A CN 107594068A
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- tyrosinase
- tropomyosin
- albumen
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- knife volume
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Abstract
The present invention proposes that a kind of be crosslinked using tyrosinase reduces knife volume newly to the method for shrimp allergen tropomyosin allergenicity, comprises the following steps：A, the new prawn tropomyosin of knife volume is diluted to the tropomyosin that concentration is 1 4mg/ml with 50mM PBS；B, tyrosinase is added into the albumen after dilution, the addition of the enzyme is 20 2000nkat/g albumen；Or tyrosinase and 0.1M caffeic acid are added into the albumen after dilution, the wherein addition of tyrosinase is 20 2000nkat/g albumen；The albumen and addition tyrosinase and caffeinic albumen the sustained response 24h in 37 DEG C of environment of tyrosinase will be only added, sustained oscillation is kept in course of reaction.The present invention is tyrosinase and tyrosinase with by way of caffeic acid association response, significantly reducing the activity of the main allergen tropomyosin of the new prawn of knife volume, strong guarantee being provided for the prawn product for preparing low-allergen from now on.
Description
Technical field
Knife volume is reduced newly to shrimp allergen tropomyosin allergenicity using tyrosinase crosslinking the present invention relates to one kind
Method.
Background technology
The new prawn of knife volume, trade name are shrimp, are a kind of aquatic foods being loved by people, however, it is also
Cause one of conventional food of food-borne allergic diseases.Report of the recent domestic about food-borne shrimp allergy is shown in repeatly
It is not fresh, it is especially common in Asia.The clinical manifestation of diet diversity includes respiratory system, gastrointestinal system, central nervous system
Various forms of clinical symptoms such as system, skin, muscle and bone, such as nettle rash, dermatitis herpetiformis, oral cavity Hypersensitivity Syndrome, intestines
Disease syndrome, asthma and allergic rhinitis etc..Serious food hypersenstivity can cause anaphylactic shock, even result in death.
The tropomyosin isolated from sea shrimp is confirmed（Tropomyosin）It is the main allergen of shrimp, tropomyosin is one
Kind 34-38 kDa protein, has coiled coil secondary structure, accounts for the 6% of total shrimp protein, about 2 .9% containing sugar.
It is to prevent the unexpected anaphylactoid preferred plan of generation to avoid edible sensitization food, but excludes anaphylactogen completely
Food can produce certain negative effect to diet.By effectively reducing food sensitizability, to the hair of low-allergen food
Exhibition is furtherd investigate, it has also become the task of top priority.
Tyrosinase is the copper enzyme for belonging to oxidizing ferment group.It is a kind of difunctionality enzyme, can be catalyzed TYR hydroxylating
It is changed into L-3,4 dihydroxyphenylalanine, also oxidable L-3,4 dihydroxyphenylalanine forms DOPA quinone.Because they have high response, therefore they can be further
React.In addition, DOPA and tyrosine（The natural substrate of tyrosinase）With tyrosine residue in oxidized protein side chain
Potentiality, so as to form covalent Trp-Lys, tyrosine-cysteine or Tyr-Tyr crosslinking.
Tyrosinase can also be with the material such as various diphenol and single phenolic compounds such as caffeic acid, tannic acid, catechol, phenol
React, can be used for protein cross to improve the property of food.This is reacted to be proved to can be used for casein, whey
In the modification of albumen and shellfish allergens arginine kinase.
If knife volume can be greatly lowered newly to the sensitization of shrimp allergen tropomyosin allergenicity using above-mentioned reaction
Ability, security, commercial value and the market popularization for the food can all produce active influence.
The content of the invention
In order to solve the problems of the prior art, the present invention proposes that a kind of be crosslinked using tyrosinase reduces the new prawn of knife volume
The method of anaphylactogen tropomyosin allergenicity.It is achieved through the following technical solutions：
A kind of be crosslinked using tyrosinase reduces knife volume newly to the method for shrimp allergen tropomyosin allergenicity, including as follows
Step：
A, the new prawn tropomyosin of knife volume is diluted to the tropomyosin that concentration is 1-4mg/ml with 50mM PBS
In vain；
B, tyrosinase is added into the albumen after dilution, the addition of the enzyme is 20-2000nkat/g albumen；Or to dilution
Tyrosinase and 0.1M caffeic acid are added in albumen afterwards, the wherein addition of tyrosinase is 20-2000nkat/g albumen；
The albumen for only adding tyrosinase and addition tyrosinase and caffeinic albumen are continued instead in 37 DEG C of environment
24h is answered, sustained oscillation is kept in course of reaction.
Further, the step A is specially：Tropomyosin is diluted to concentration as 2 with 50mM PBS
Mg/ml tropomyosin.
Further, in the step B, the albumen and addition tyrosinase and caffeinic of tyrosinase will only be added
Albumen is placed in carrying out oscillation incubation in the water-bath that temperature is 37 DEG C, and clean rotor is added in protein liquid and keeps even
Speed stirring, reaction time 24h.
Further, after the completion of the step B reactions, albumen is boiled 10 minutes with terminating reaction, obtained modified
Low-allergen tropomyosin.
Further, in the step B, tyrosinase is added into the albumen after dilution, the addition of the enzyme is 1000
Nkat/g albumen；Or adding tyrosinase and 0.1M caffeic acid into the albumen after dilution, wherein tyrosinase enzyme adds
Dosage is 1000 nkat/g albumen.
The preparation method of low-allergen tropomyosin,
A, the new prawn tropomyosin of knife volume is diluted to the tropomyosin that concentration is 1-4mg/ml with 50mM PBS
In vain；
B, tyrosinase is added into the albumen after dilution, the addition of the enzyme is 20-2000nkat/g albumen；Or to dilution
Tyrosinase and 0.1M caffeic acid are added in albumen afterwards, the wherein addition of tyrosinase is 20-2000nkat/g albumen；
By the only albumen of addition tyrosinase and addition tyrosinase and 0.1M caffeinic albumen in 37 DEG C of environment
Sustained response 24h, sustained oscillation is kept in course of reaction；
C, reaction are completed albumen boiling 10 minutes with terminating reaction, obtain modified low-allergen tropomyosin.
The present invention also proposes that tyrosinase is reducing the newly application to shrimp allergen tropomyosin allergenicity of knife volume.
The present invention also proposes that tyrosinase and caffeic acid collective effect are reducing knife volume newly to shrimp allergen tropomyosin
The application of allergenicity.
The present invention also proposes that tyrosinase is preparing the application of low-allergen tropomyosin.
The present invention also proposes the application of tyrosinase and caffeic acid collective effect in low-allergen tropomyosin.
It is of the invention to be relative to advantage possessed by prior art：
1. the present invention is tyrosinase and tyrosinase with by way of caffeic acid association response, significantly reducing knife volume
The allergenicity of the main allergen tropomyosin of new prawn, provided effectively to prepare the prawn product of low-allergen from now on
Ensure.
2. the present invention has used tyrosinase, it is catalyzed shrimp internal protein and forms covalent Trp-Lys,
Tyrosine-cysteine or Tyr-Tyr crosslinking, it can effectively strengthen the gelling performance of shrimp albumen, and to improve in the future
The quality structure and mouthfeel of shrimp quality provide support.
3. the present invention is handled using tyrosinase with the anaphylactogen for the method prawn that caffeic acid is combined first, by
Caffeic acid is introduced in processing, certain antibacterial and detoxicating effect can be played.
4. the present invention by way of caffeic acid association response tyrosinase with reacting, the time is shorter and reaction condition temperature
With, the problem of reaction rate is relatively low is avoided, and will not be destroyed the nutritional ingredient in protein and amino sugar, also not
Various complicated or even harmful accessory substances can be produced.This is expected to further be applied in food processing.
Brief description of the drawings
In order to illustrate more clearly about the embodiment of the present invention or technical scheme of the prior art, below will be to embodiment or existing
There is the required accompanying drawing used in technology description to be briefly described, it should be apparent that, drawings in the following description are this hairs
Some bright embodiments, for those of ordinary skill in the art, without having to pay creative labor, can be with
Other accompanying drawings are obtained according to these accompanying drawings.
Fig. 1 is the SDS-PAGE analyses of the lower tropomyosin of different condition processing；
Fig. 2 is the allergen activity that tropomyosin is detected using indirect elisa method；
Fig. 3 is the allergen activity that tropomyosin is detected using Western blot；
In above-mentioned accompanying drawing, wherein, M：Protein labeling；1：Shrimp tropomyosin；2：20 nkat/g tyrosinases；3：100
Nkat/g tyrosinases；4：400nkat/g tyrosinases;5：1000nkat/g tyrosinases；6：2000 nkat/g junket ammonia
Sour enzyme；7：0.1M caffeic acids; 8：20nkat/g tyrosinase+0.1M caffeic acids；9：100nkat/g tyrosinases+
0.1M caffeic acids；10：400 nkat/g tyrosinase+0.1M caffeic acids；11：1000nkat/g tyrosinases+
0.1M caffeic acids；12：2000 nkat/g tyrosinase+0.1M caffeic acids.
Embodiment
In the present invention, unless otherwise stated, Science and Technology noun used herein has art technology
The implication that personnel are generally understood that.
In the present invention, refered in particular to Ru non-, used raw material and equipment etc. are commercially available or commonly used in the art.
Method in following embodiments, it is the conventional method of this area unless otherwise specified.
Embodiment one,
A kind of be crosslinked using tyrosinase reduces knife volume newly to the method for shrimp allergen tropomyosin allergenicity, including following
Step：
1. by the new prawn tropomyosin 50mM of knife volume PBS（pH=8.0）It is diluted to the former flesh that concentration is 2mg/ml
Globulin；
2. the tyrosinase extracted from mushroom is added into the albumen after dilution（Wherein, tyrosinase is extracted from mushroom
Extraction process is prior art, be will not be repeated here, similarly hereinafter）, concentration is 400 nkat/g, the sustained response 24 in 37 DEG C of environment
Hour, keep sustained oscillation in course of reaction.
React and albumen is boiled 10 minutes with terminating reaction after terminating, obtain modified tropomyosin.
Embodiment two,
A kind of be crosslinked using tyrosinase reduces knife volume newly to the method for shrimp allergen tropomyosin allergenicity, including following
Step：
1. by the new prawn tropomyosin 50mM of knife volume PBS（pH=8.0）It is diluted to the former flesh that concentration is 2mg/ml
Globulin；
2. the tyrosinase extracted from mushroom, concentration 1000nkat/g, in 37 DEG C of environment are added into the albumen after dilution
Middle sustained response 24 hours, keeps sustained oscillation in course of reaction.
React and albumen is boiled 10 minutes with terminating reaction after terminating, obtain modified tropomyosin.
Embodiment three,
One kind reduces knife volume newly to shrimp allergen tropomyosin allergenicity, bag using tyrosinase and caffeic acid association response
Include following steps：
1. by the new prawn tropomyosin 50mM of knife volume PBS（pH=8.0）It is diluted to the former flesh that concentration is 2mg/ml
Globulin；
2. tyrosinase and 0.1M caffeic acid that into the albumen after dilution, addition is extracted from mushroom, wherein tyrosinase
Concentration is respectively 400nkat/g, and sustained response 24 hours, keep sustained oscillation in 37 DEG C of environment in course of reaction.Reaction knot
Albumen is boiled 10 minutes with terminating reaction after beam, obtains modified tropomyosin.
Example IV,
One kind reduces knife volume newly to shrimp allergen tropomyosin allergenicity, bag using tyrosinase and caffeic acid association response
Include following steps：
1. by the new prawn tropomyosin 50mM of knife volume PBS（pH=8.0）It is diluted to the former flesh that concentration is 2mg/ml
Globulin；
2. adding the tyrosinase and caffeic acid extracted from mushroom into the albumen after dilution, concentration is respectively 1000nkat/g
And 0.1M, sustained response 24 hours, keep sustained oscillation in 37 DEG C of environment in course of reaction；Reaction boils albumen after terminating
Boiling 10 minutes, with terminating reaction, obtains modified tropomyosin.
Each solution formula is in the present invention：
50mM PBS formulas：14.5gNa2HPO4·12H2O, 1.0 g KH2PO4, 1.0 gKCl, 40.0 gNaCl, add
Ultra-pure water is settled to 1000 mL, and its pH is adjusted into 8.0,4 DEG C of preservations.
Temperature is in tyrosinase optimum temperature section in the present invention.The reaction time of 24 hours can ensure small clear egg
Sufficiently reaction occurs with tyrosinase in vain, improves efficiency of pcr product.
Addition 0.1M caffeic acids are to improve the activity of tyrosinase, ensure that reaction is efficiently carried out.
In 0-400 nkat/g, with the rising of tyrosinase dosage, cross-linking products content also rises therewith, when reaching
After the nkat/g of critical point 400, cross-linking products content no longer rises with the rising of tyrosinase dosage.When tyrosinase concentration
During higher than 1000 nkat/g, tropomyosin band no longer attenuates.Therefore the scope of tyrosinase addition is 400 ~ 2000
It is advisable in the range of nkat/g.
Embodiment five, SDS-PAGE methods analyze the tropomyosin change of component of different disposal
2.1. material to be tested
Control sample：Tropomyosin after purification
Sample 1：The tropomyosin handled through tyrosinase；
Sample 2：Tropomyosin through tyrosinase and coffee acid treatment；
Sample 3：Tropomyosin only through coffee acid treatment；
Sample is made by the steps to obtain：By the new prawn tropomyosin 50mM of knife volume PBS（pH=8.0）
It is diluted to the tropomyosin that concentration is 2mg/ml.The tyrosinase extracted from mushroom is added into the albumen after dilution, it is dense
Degree is respectively 0（Blank）, the nkat/ g albumen of 20,100,400,1000 and 2000, or into the albumen after dilution
Tyrosinase and caffeic acid are added, the addition of wherein enzyme is respectively 0（Blank）, 20, 100, 400, 1000 and
2000 nkat/ g albumen, caffeinic concentration are 0.1M.Sustained response 24 hours, keep in course of reaction in 37 DEG C of environment
Sustained oscillation.React and albumen is boiled 10 minutes with terminating reaction after terminating, obtain modified tropomyosin.
Tropomyosin change of component after the analysis distinct methods processing of 2.2, SDS-PAGE methods
Electrophoretic separation gum concentration is 15% (w/v), and concentration gum concentration is 5% (w/v).By above-mentioned each sample and sample-loading buffer
After mixing thermal denaturation, per the μ g of swimming lane loading 10.Dyeing, it is imaged after decolourizing with gel imager shooting, collects image.
2.3. SDS-PAGE evaluations are carried out to reaction：
It is can be seen that from the protein band in SDS-PAGE such as Fig. 1（A）（B）Shown, non-crosslinked tropomyosin is positioned at about
At 36kDa, pass through modification of the tyrosinase or tyrosinase and caffeic acid of various dose to tropomyosin, tropomyosin
Informal voucher band shoals, and whole swimming lane produces a number of new band there occurs diffusing phenomenon, wherein, 72,108,140kDa
Place is the most obvious, and as the raising of tyrosinase concentration, new caused band deepen therewith.Work of this explanation in tyrosinase
Under, tropomyosin crosslinks, and in certain enzyme concentration with enzyme concentration into positive correlation.
Embodiment six, the detection of product sensitization
The preparation of the new prawn tropomyosin polyclonal antibody of the anti-knife volumes of 3.1,：
Rabbit is immunized by the way of subcutaneous multi-point injection, immunoreagent is tropomyosin after purification.Antigen is exempted from
Dosage needed for epidemic disease is every mg/ml of rabbit 1, and frequency is 2 weeks/time, while detects antibody titer, continues to be immunized 4 times altogether for 8 weeks.
Extracting arterial blood, centrifuged after blood coagulation, take the serum of supernatant, frozen at -20 DEG C standby.
The detection of 3.2, measuring samples Prawn tropomyosin allergen activities：
1. indirect enzyme-linked immunosorbent assay：The tropomyosin after the processing of 100 μ L distinct methods is coated with per hole in 96 hole elisa Plates
Albumin sample, 4 DEG C be incubated overnight after, with PBST board-washings three times, then with 1%BSA close nonspecific binding site, 37 DEG C
It is incubated 1.5 h.Then three times, the rabbit-anti shrimp polyclonal antibody of preparation adds 100 μ L, 37 DEG C of incubations per hole to board-washing as primary antibody
1.5 h.Afterwards by the use of the goat anti-rabbit igg of HRP marks as secondary antibody, 100 μ L, 37 DEG C of 1 h of incubation are added per hole three times for board-washing.Board-washing
100 μ L tropomyosin B nitrite ions are added after three times per hole, lucifuge is incubated 20min in 37 DEG C of incubators, and incubation terminates
Afterwards, with 2M sulfuric acid terminating reaction.The light absorption value under 450 nm is read with ELIASA.
2. Western blot：After different protein samples are carried out into SDS-PAGE electrophoresis according to the method in 2.2, use
IBlot2 is transferred, and the protein band on gel is all transferred on the pvdf membrane of activation.Then with 3.1 rabbit-antis prepared
For shrimp polyclonal antibody as primary antibody, secondary antibody is the goat anti-rabbit antibody of HRP marks, and two kinds of antibody and the pvdf membrane after transfer are added
In iBand, it is incubated at least 3 hours.Then developed the color using ECL nitrite ions, be incubated 2 min, 30s is exposed, in gel imaging
Taken pictures under instrument, collect the picture rich in detail under optimum exposure.
3.3, carry out indirect ELISA evaluation to allergen activity：
By indirect elisa method come the binding ability of quantitative analysis tropomyosin immunocompetence and rabbit-anti shrimp polyclonal antibody,
So as to evaluate using tyrosinase or using tyrosinase and coffee acid treatment to the new prawn tropomyosin anaphylactogen of knife volume
Influence.As a result as shown in Fig. 2 processing of the tyrosinase to tropomyosin can make tropomyosin and IgG（Fig. 2A, B）
And IgE（Fig. 2 C, D）With reference to ability be remarkably decreased（P ＜ 0.05）, slight decline is only also resulted in using only caffeic acid.Knot
Conjunction ability fall is more notable with the rising of tyrosinase concentration, meets the Crosslinking regulation in SDS-PAGE results.
Fig. 2A, B represent anaphylactogen and the change of IgG binding abilities, it can be seen that when the junket of addition same concentrations
During propylhomoserin enzyme, while the allergen activity for adding caffeinic experimental group is lived than not adding the anaphylactogen of caffeinic experimental group
Property fall is bigger.When adding 1000nkat/g tyrosinases, activity decrease amplitude is about 20.75%, works as addition
During 1000nkat/g tyrosinase+0.1M caffeic acids, activity decrease amplitude is 33.82%.When coffee acid concentration is identical,
Tyrosinase concentration is bigger, and the amplitude that allergen activity declines is also bigger.Relative to addition 1000nkat/g tyrosinases+
Allergen activity declines 33.82% during 0.1M caffeic acids, allergy when adding 2000nkat/g tyrosinase+0.1M caffeic acids
Former activity decrease 37.22%.For IgE binding ability, phenomenon is also similar, and allergen activity declines respectively
43.90%（Add 2000nkat/g tyrosinases）And 49.41%（Add 2000nkat/g tyrosinase+0.1M coffees
Acid）.As can be seen that when adding 2000nkat/g tyrosinase+0.1M caffeic acids, there is best abatement effect.
3.4. Western blot evaluations are carried out to allergen activity：
Tyrosinase and caffeic acid can modify its amino acid, so as to cause the change of tropomyosin structure.For its knot
The modification of structure may mask some combination epitopes of the exposure in its inherent structure, however, tyrosinase modification can not be complete
The antibody identification of shrimp tropomyosin is eliminated, shows some linear epitopes be present, it can not possibly be wholly absent by ferment treatment.
Pass through immunoblot experiment（Western blot）Determine tyrosinase and caffeic acid combined modification tropomyosin
The change of binding ability is immunized afterwards, its result figure is similar to SDS-PAGE result figure results.Use rabbit-anti shrimp Anti-TNF-α physical examination
Survey IgG binding abilities（Fig. 3 A, B）, when using tyrosinase and coffee acid treatment tropomyosin, tropomyosin band
Shoal, and the bigger new band of molecular weight occur, this demonstrates the formation of crosslinking, and the albumen after crosslinking from another angle
It can be combined with IgG.Utilize the Virus monitory of the patient of prawn allergy and IgE binding ability（Fig. 3 C, D）, occur similar
As a result, increasing with tyrosinase concentration, newly-generated band significantly deepen therewith, and positive band almost disappears.Produced after crosslinking
Raw new band is primarily generated at 72,108,140kDa, and with increasing for tyrosinase concentration, newly-generated band significantly becomes
It is deep.Although although aggregation can be identified by IgE, weaker binding ability is shown.
Tyrosinase processing may cause the denaturation of tropomyosin, then the multiple epitopes of exposure on protein surface,
And these epitopes are further combined with IgE or IgG.However, although crosslinking after albumen can be combined with IgG and IgE, but due to lead to
Ferment treatment is crossed to change IgE combination epitopes, thus crosslinking after caused albumen can not possibly as native allergens sensitization.
In summary, the scope of tyrosinase addition is advisable in the range of 400-2000 nkat/g.
Tyrosinase can effectively reduce its sensitizability with caffeic acid combined modification tropomyosin, it is contemplated that it is to work(
The influence of energy property, thus have more application prospect.
The above embodiments are merely illustrative of the technical solutions of the present invention, rather than is limited；Although with reference to foregoing reality
Example is applied the present invention is described in detail, for the person of ordinary skill of the art, still can be to foregoing implementation
Technical scheme described in example is modified, or carries out equivalent substitution to which part technical characteristic；And these are changed or replaced
Change, the essence of appropriate technical solution is departed from the spirit and scope of claimed technical solution of the invention.
Claims (9)
1. a kind of be crosslinked using tyrosinase reduces knife volume newly to the method for shrimp allergen tropomyosin allergenicity, its feature
It is, comprises the following steps：
A, the new prawn tropomyosin of knife volume is diluted to the tropomyosin that concentration is 1-4mg/ml with 50mM PBS
In vain；
B, tyrosinase is added into the albumen after dilution, the addition of the enzyme is 20-2000nkat/g albumen；Or to dilution
Tyrosinase and 0.1M caffeic acid are added in albumen afterwards, the wherein addition of tyrosinase is 20-2000nkat/g albumen；
The albumen for only adding tyrosinase and addition tyrosinase and caffeinic albumen are continued instead in 37 DEG C of environment
24h is answered, sustained oscillation is kept in course of reaction.
2. a kind of be crosslinked using tyrosinase according to claim 1 reduces knife volume newly to shrimp allergen tropomyosin mistake
The method of quick originality, it is characterised in that the step A is specially：Tropomyosin is diluted to 50mM PBS dense
Spend the tropomyosin for 2mg/ml.
3. a kind of be crosslinked using tyrosinase according to claim 2 reduces knife volume newly to shrimp allergen tropomyosin mistake
The method of quick originality, it is characterised in that in the step B, by only add tyrosinase albumen and addition tyrosinase and
Caffeinic albumen is placed in carrying out oscillation incubation in the water-bath that temperature is 37 DEG C, and clean rotor is added in protein liquid
And the stirring that remains a constant speed, reaction time 24h.
4. a kind of according to claim 3 reduce knife volume newly to shrimp allergen tropomyosin allergy using tyrosinase crosslinking
The method of originality, it is characterised in that after the completion of the step B reactions, albumen is boiled 10 minutes with terminating reaction, is modified
Low-allergen tropomyosin afterwards.
5. the preparation method of low-allergen tropomyosin, it is characterised in that comprise the following steps：
A, the new prawn tropomyosin of knife volume is diluted to the tropomyosin that concentration is 1-4mg/ml with 50mM PBS
In vain；
B, tyrosinase is added into the albumen after dilution, the addition of the enzyme is 20-2000nkat/g albumen；Or to dilution
Tyrosinase and 0.1M caffeic acid are added in albumen afterwards, the wherein addition of tyrosinase is 20-2000nkat/g albumen；
The albumen for only adding tyrosinase and tyrosinase and 0.1M caffeinic albumen are continued in 37 DEG C of environment
24h is reacted, sustained oscillation is kept in course of reaction；
C, reaction are completed albumen boiling 10 minutes with terminating reaction, obtain modified low-allergen tropomyosin.
6. tyrosinase is reducing the newly application to shrimp allergen tropomyosin allergenicity of knife volume.
7. tyrosinase and caffeic acid collective effect are reducing the newly application to shrimp allergen tropomyosin allergenicity of knife volume.
8. application of the tyrosinase during low-allergen tropomyosin is prepared.
9. the application of tyrosinase and caffeic acid collective effect during low-allergen tropomyosin is prepared.
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| DE10151922A1 (en) * | 2001-10-20 | 2003-11-27 | Bsr Bio Schuh Recycling Gmbh | Oil binder for removing oils from solid or liquid surfaces is obtained by sealing and hydrophobicizing leather granulate by an enzymatic reaction |
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Application publication date: 20180119 |