CN108850420A - A method of improving chicken myofibril protein antioxidant and functional characteristic - Google Patents
A method of improving chicken myofibril protein antioxidant and functional characteristic Download PDFInfo
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- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
- A23J1/02—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from meat
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
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Abstract
The invention discloses a kind of methods of improvement chicken myofibril protein antioxidant and functional characteristic, to improve protein quality.Fribrillin is carried out under magnetic stirring to react to obtain phosphorylation fribrillin with sodium tripolyphosphate solution；Polyphenol is made an addition in gained phosphorylation fribrillin solution, is stirred, low speed reacts under magnetic stirring, obtains modified fribrillin solution.Modified fribrillin solution is put into water-bath, gradient is warming up to 75 DEG C from 20 DEG C, continues to heat 30min after reaching 75 DEG C；It is immediately placed in cooling in mixture of ice and water later and obtains protein gel.Fribrillin its antioxidant activity, emulsifying activity after improving by means of the present invention, emulsion stability, gel elastomer are significantly increased, this plays an important role to the improvement of meat products quality and the extension of shelf life.
Description
Technical field
The present invention relates to field of biotechnology, are changed more specifically, it relates to a kind of using polyphenol collaboration phosphorylation modification
The method of kind chicken myofibril protein antioxidant and functional characteristic.
Background technique
Meat product is the main source of needed by human body good protein, indispensable food even more in people's daily life
Product.In meat product, chicken with high protein, low fat, low cholesterol, high nutrition and it is famous, become meat packing enterprise and be used for
Substitution pork produces the preferred object of all kinds of meat products.The protein being rich in chicken is except the distinctive flavor of imparting meat products, mouth
Outside sense and nutrition, its some functional characteristics are such as emulsified and gel elastomer plays an important role to the final quality of product.Myogen
Fibrin is the highest albumen of content in Fresh Grade Breast, and gelling performance and organoleptic quality to pigeon breast meat products play decisive work
With.Therefore, the quality of chicken products can further be improved by improving its functional characteristic as object using fribrillin.
In most cases, the absolute magnitude of protein is significant changes will not to occur, and can change it by various modifications
Functional characteristic.Common method of modifying includes phosphorylation, glycosylation etc..In recent years, researchers at home and abroad have studied various
Modified method (such as chemical modification, physical modification) utilizes phosphorylation to improve protein function characteristic the improvement of albumen
It is one of the hot spot studied at present.It is modified due to introducing a large amount of phosphate radical, thus change the isoelectric point of protein, dissolution
Degree, emulsification property etc., and the crosslinking feature of protein molecule is changed, affect gel strength, elasticity and water-retaining property.《Chicken
Compared with fribrillin phosphorylation characteristic in mantis shrimp》(Wang Shimeng, Zhang Kunsheng appoint rosy clouds,《Food and fermentation industries》,
2015,41(09):A kind of method by fribrillin in the modified Fresh Grade Breast of phosphorylation 24-28) is disclosed, so that by chicken
The water-retaining property and intensity of brisket myofibrillar protein gel are improved.
Existing research mostly uses monotechnics to be modified protein greatly, and modification efficiency is relatively low.Phosphate is certain
The functional characteristics such as fribrillin emulsification, gel can be improved in degree, but improvement is limited；And protein oxidation is to lead to meat
The major reason of product quality decline during processing and storage, and phosphate can only chelated metal ions, do not have removing
It is limited that antioxidant effect is used alone in the ability of free radical.
Summary of the invention
Phosphoric acid is cooperateed with using polyphenol in view of the technical drawbacks of the prior art, it is an object of the present invention to provide a kind of
The method that change technology improves Fresh Grade Breast fribrillin antioxidant activity and functional characteristic, to improve protein quality.
The technical solution adopted to achieve the purpose of the present invention is：
A method of improving chicken myofibril protein antioxidant and functional characteristic, includes the following steps：
(1) will reject visible fat connective tissue chicken paste be added protein extract, be homogenized with homogenizer, freeze from
The heart abandons supernatant and stays precipitating, repeats aforesaid operations and obtain chicken myofibril crude protein；By gained crude protein and 0.1mol/L
NaCl solution mixing, homogeneous, refrigerated centrifuge abandon supernatant and stay precipitating, repeat aforesaid operations, and gained paste precipitating is chicken flesh
Fibrillin；
(2) phosphorylation is modified：The resulting chicken myofibril albumen of step (1) and sodium tripolyphosphate solution are stirred in magnetic force
It is reacted under mixing, phosphorylation fribrillin solution of dialysing in the PBS of pH=7.4 in 4 DEG C after reaction to obtain；
(3) addition polyphenol modification：Polyphenol is made an addition in phosphorylation fribrillin solution obtained by step (2), sufficiently
It stirs evenly, low speed reacts under magnetic stirring, obtains modified fribrillin solution；The polyphenol is chlorogenic acid or does not eat
Sub- acid.
Modified fribrillin solution obtained by step (3) is put into water-bath, with the velocity gradient of 1 DEG C/min from 20
75 DEG C DEG C are warming up to, continues to heat 30min after reaching 75 DEG C；After heating, sample is put into immediately cold in mixture of ice and water
But 30min obtains protein gel.
The group of protein extract described in step (1) becomes：0.1mol/L NaCl,0.002mol/L MgCl,
The 0.1mol/L NaH of 0.001mol/L EDTA.2Na and pH=72PO4/Na2HPO4Mixed solution.
Sodium tripolyphosphate solution described in step (2) is that sodium tripolyphosphate is dissolved in 0.75mol/L NaCl solution, three
The final concentration of 3.35-3.45% of polyphosphate sodium (w/v), pH value 7.47-7.53.
Gained protein concentration is 14.80-15.20mg/mL after fribrillin is added in step (2), and the reaction time is
1.9-2.1h。
With the NaCl solution dissolution chlorogenic acid or gallic acid of 0.75mol/L in step (3).
Processing condition in step (1) is：In 22000rpm homogeneous 30s, refrigerated centrifuge condition is：Under the conditions of 4 DEG C
5000r/min is centrifuged 15min.
Compared with prior art, the beneficial effects of the invention are as follows：
1, method of the invention improves fribrillin inoxidizability using natural polyphenol collaboration phosphorylation and function is special
Property, the functional characteristic of albumen was both improved, while improving its physiological activity, and had improved modification efficiency.On the one hand, pass through phosphoric acid
Change and introduce a large amount of phosphate groups, change the electronegativity of protein molecule, improves electrostatic repulsion between protein molecule, be allowed to eating
It is easier to disperse in product system, it is mutually exclusive, it is thus possible to improve the dissolubility and aggregation stability of albumen, and the electricity such as reduction
Point changes the crosslinking feature of albumen, so as to improve the emulsification property and gel elastomer of albumen.On the other hand, phosphate has gold
Belong to ion chelating capacity, so that the metal ion being chelated can not participate in oxidation reaction, therefore can improve to a certain extent
The oxidation stability of meat products.However there is complicated oxidation systems in practical CARCASS QUALITY, as natural
Polyphenol can be interacted with protein with non-covalent or covalent manner, to significantly improve phosphorylation fribrillin
Inoxidizability and Scavenging ability, substantially prolong the shelf life of meat products；Meanwhile albumen has been modified in the combination of polyphenol
The functional group of matter side chain amino acid changes protein structure, surface hydrophilicity/hydrophobicity, solubility, and then influences albumen
The functional characteristic of matter, the emulsification property and gel elastomer of the fribrillin after making phosphorylation significantly improve.
2, fribrillin its antioxidant activity, emulsifying activity, stable emulsifying after improving by means of the present invention
Property, gel elastomer are significantly increased, this plays an important role to the improvement of meat products quality and the extension of shelf life.
3, the present invention has widened field for the improvement of Fresh Grade Breast and meat products, is that polyphenol and phosphate collaboration are used as food additive
Add agent to be applied to meat products and provides convenient reliable method.
Specific embodiment
Below in conjunction with specific embodiment, the present invention is described in detail.
The present invention improves fribrillin inoxidizability and functional characteristic using natural polyphenol collaboration phosphorylation, using also
Proper energy power, DPPH free radical scavenging ability, ultra-oxygen anion free radical Scavenging activity measure and evaluate Fresh Grade Breast fribrillin
Antioxidant activity；Fresh Grade Breast fribrillin functional characteristic, tool are evaluated using emulsifying activity, emulsion stability, gel elastomer
Body method is as follows：
1, the measurement of reducing power：
Using the modification fribrillin solution after phosphorylation and polyphenol modification as protein sample.It uses
Protein sample is diluted 20 times by the NaCl solution of 0.75mol/L.Take dilution after protein solution, be added 2.5mL pH value be 6.6,
Phosphate buffer and 3.0mL concentration that concentration is 0.01mol/L are the potassium ferricyanide solution of 1% (m/v), 50 DEG C of water-baths
20min, is added the solution of trichloroacetic acid that 2.5mL concentration is 10% (m/v), and 3500r/min is centrifuged 10min.Take 3mL supernatant with
The FeCl that 0.5mL concentration is 0.1% (m/v) is added after the mixing of 3mL distilled water3Solution, mixing is stored at room temperature 15min, with equivalent
Deionized water returns to zero instead of sample solution, measures absorbance A under 700nm wavelength.
2, the measurement of DPPH free radical scavenging ability：
Using the modification fribrillin solution after phosphorylation and polyphenol modification as protein sample.Use concentration
Protein sample is diluted 20 times for the NaCl solution of 0.75mol/L.Take 2mL concentration be 0.2mmol/L DPPH ethanol solution with
Protein solution after 2mL dilution, mixes, and is protected from light after 30min the survey absorbance value at 517nm.Blank group selects ethyl alcohol generation
For DPPH ethanol solution；Control group replaces protein sample to react with DPPH ethanol solution by dehydrated alcohol.Using following formula (1)
It calculates.
In formula (1)：A1For the absorbance of experimental group；A2For the absorbance of blank group；A3For the absorbance of control group.
3, the measurement of ultra-oxygen anion free radical Scavenging activity：
Using the modification fribrillin solution after phosphorylation and polyphenol modification as protein sample.Use concentration
Protein sample is diluted 20 times for the NaCl solution of 0.75mol/L.The concentration for taking 4.5mL pH value to be 8 is 0.05mol/L phosphoric acid
Salt buffer heats 20min in 25 DEG C of water-baths, and the protein solution and 0.4mL concentration after 1mL dilution is added are 25mmol/L's
Pyrogallol solution reacts 5min in 25 DEG C of water-baths after mixing, the HCl solution that 1mL concentration is 80mmol/L is added and terminates instead
It answers, and shakes up, react 3min, absorbance is measured at wavelength 420nm.It is free that superoxide anion is calculated using following formula (2)
Base clearance rate.
In formula (2)：
A1：0.05mol/L phosphate buffer+1mL polyphenol treated the phosphorylation muscle fibril that 4.5mL pH value is 8
Protein solution+0.4mL 25mmol/L pyrogallol solution+1mL 80mmol/L HCl；
A2:0.05mol/L phosphate buffer+1mL the polyphenol of 4.5mL pH8 treated phosphorylation fribrillin
Solution+1mL 80mmol/L HCl；
A3:0.05mol/L phosphate buffer+1mL dehydrated alcohol+0.4mL 25mmol/L neighbour the benzene three of 4.5mL pH8
Phenol solution+1mL 80mmol/L HCl
4, the measurement of emulsifying activity and emulsion stability：
Using the modification fribrillin solution after phosphorylation and polyphenol modification as protein sample.Use concentration
Protein sample is diluted to a protein concentration of 2mg/mL for the NaCl solution of 0.75mol/L.Take 16mL diluted protein liquid and 4mL big
Soya-bean oil is mixed in 50mL beaker, high-speed homogenization 2min, is drawn 100 μ L from bottom in 0min and 10min respectively, is added to
In the SDS solution of 10mL 0.1%, oscillation measures absorbance at 500nm after mixing, and 0.1%SDS solution is blank.Emulsification is lived
Property EAI (m2/ g) it is indicated by following formula (3), emulsion stability ESI (%) is indicated by formula (4)：
In formula：A0For emulsion 0min absorbance；A10For emulsion 10min absorbance；N is extension rate；C
For protein quality concentration/(g/mL)；φ is oil phase volume score (v/v) (φ=0.2).
5, the measurement of gel elastomer：Test gels sample is placed on test platform and is fixed, utilizes TA- under room temperature
XT Plus type Texture instrument is measured.Mode determination is set as rate 2mm/s before surveying；Test rate 1mm/s；Rate after survey
1mm/s；Depression distance is 5mm；Cause power 5g；Pop one's head in model P/0.5.Each sample do 3 groups it is parallel, be averaged.
Embodiment 1
(1) Fresh Grade Breast is rejected into visible adipose connective tissue, cuts with a knife and is broken into meat gruel, the albumen that four times of volumes are added mentions
Liquid is taken, is homogenized with homogenizer, refrigerated centrifuge abandons supernatant and stays precipitating, adds protein extract repetition aforesaid operations and obtains twice
Crude protein mixes gained crude protein with the NaCl solution that the concentration of 4 times of volumes is 0.1mol/L, homogeneous, refrigerated centrifuge, in abandoning
Clear liquid stays precipitating, and the NaCl solution that the concentration for adding 4 times of volumes is 0.1mol/L repeats aforesaid operations twice, last gained cream
Shape precipitating is Fresh Grade Breast fribrillin, and the fribrillin of extraction is stored in 4 DEG C, and is finished in interior for 24 hours.
Wherein, the group of the protein extract becomes：0.1mol/L NaCl,0.002mol/L MgCl,0.001mol/L
The 0.1mol/L NaH of EDTA.2Na and pH=72PO4/Na2HPO4Mixed solution, above-mentioned concentration is each in protein extract
The concentration of component.Homogeneous homogenization conditions are 22000rpm, 30s, and refrigerated centrifuge condition is 5000r/min, 15min, 4 DEG C.
(2) sodium tripolyphosphate for participating in reaction is dissolved in the NaCl solution that concentration is 0.75mol/L, sodium tripolyphosphate is dense eventually
Degree is 3.40% (W/V), and adjusts its pH value and obtain sodium tripolyphosphate solution for 7.52.Add in above-mentioned sodium tripolyphosphate solution
Enter step (1) resulting fribrillin, the control of gained protein concentration is 15mg/mL, and magnetic stirring speed is under 1400rpm
Reaction 2 hours is dialysed 12 hours in 4 DEG C, the PBS of pH=7.4 after reaction, and the fribrillin for obtaining phosphorylation is molten
Liquid.
(3) gallic acid is dissolved with the NaCl solution of 0.75mol/L, phosphorus obtained by step (2) is added in gallic acid solution
In fribrillin solution after acidification, make the final concentration of 100 μ g/mL of gallic acid, low speed (400rpm) magnetic agitation is anti-
It answers 4 hours, obtains modified fribrillin solution.
(4) modified fribrillin solution obtained by step (3) is put into water-bath, with the velocity gradient of 1 DEG C/min
It is warming up to 75 DEG C from 20 DEG C, continues to heat 30min after reaching 75 DEG C；After heating, sample is put into mixture of ice and water immediately
Middle cooling 30min obtains protein gel.
It is detected through the above method, when the addition concentration of gallic acid is 100 μ g/mL, cooperates with phosphorylation modification myogen
Fibrinous reducing power absorbance value is 0.226, is improved compared with single phosphorylation fribrillin reducing power
2.09 again；DPPH free radical scavenging activity is 58.232%, improves 5.7 compared with single phosphorylation fribrillin clearance rate
Times；Ultra-oxygen anion free radical clearance rate is 49.972%, improves 7.71% compared with single phosphorylation fribrillin.
In general, the raising of antioxidant activity is extremely significant.Emulsifying activity is 0.234m2/ g, with single phosphorylation muscle fibril egg
White compare improves 50.00%；Emulsion stability is 50.408%, is improved compared with single phosphorylation fribrillin
64.92%.Gel elastomer is 1.223, improves 40.57% compared with single phosphorylation fribrillin.
Embodiment 2
(1) Fresh Grade Breast rejects visible adipose connective tissue, cuts with a knife and is broken into meat gruel, the protein extraction of four times of volumes is added
Liquid is homogenized with homogenizer, refrigerated centrifuge, abandon supernatant stay precipitating, add protein extract repetition aforesaid operations twice slightly
Albumen mixes gained crude protein with the NaCl solution that the concentration of 4 times of volumes is 0.1mol/L, and homogeneous, refrigerated centrifuge abandons supernatant
Liquid stays precipitating, and the NaCl solution that the concentration for adding 4 times of volumes is 0.1mol/L repeats aforesaid operations twice, last gained paste
Precipitating is Fresh Grade Breast fribrillin, and the fribrillin of extraction is stored in 4 DEG C, and is finished in interior for 24 hours.
Wherein, the group of the protein extract becomes：0.1mol/L NaCl,0.002mol/L MgCl,0.001mol/L
The 0.1mol/L NaH of EDTA.2Na and pH=72PO4/Na2HPO4Mixed solution, above-mentioned concentration is each in protein extract
The concentration of component.Homogeneous homogenization conditions are 22000rpm, 30s, and refrigerated centrifuge condition is 5000r/min, 15min, 4 DEG C.
(2) sodium tripolyphosphate for participating in reaction is dissolved in the NaCl solution that concentration is 0.75mol/L, sodium tripolyphosphate is dense eventually
Degree is 3.40% (W/V), and adjusts its pH value and obtain sodium tripolyphosphate solution for 7.52.Add in above-mentioned sodium tripolyphosphate solution
Enter step (1) resulting fribrillin, the control of gained protein concentration is 15mg/mL, and magnetic stirring speed is under 1400rpm
Reaction 2 hours is dialysed 12 hours in 4 DEG C, the PBS of pH=7.4 after reaction, and the fribrillin for obtaining phosphorylation is molten
Liquid.
(3) gallic acid is dissolved with the NaCl solution of 0.75mol/L, phosphorus obtained by step (2) is added in gallic acid solution
In fribrillin solution after acidification, make the final concentration of 200 μ g/mL of gallic acid, low speed (400rpm) magnetic agitation is anti-
Fribrillin solution must be modified by answering 4 hours.
(4) modified fribrillin solution obtained by step (3) is put into water-bath, with the velocity gradient of 1 DEG C/min
It is warming up to 75 DEG C from 20 DEG C, continues to heat 30min after reaching 75 DEG C；After heating, sample is put into mixture of ice and water immediately
Middle cooling 30min obtains protein gel.
It is detected through the above method, when the addition concentration of gallic acid is 200 μ g/mL, cooperates with phosphorylation modification myogen
Fibrinous reducing power absorbance value is 0.31, is improved compared with single phosphorylation fribrillin reducing power
6.8 again；DPPH free radical scavenging activity is 68.933%, improves 2.87 compared with single phosphorylation fribrillin clearance rate
Times；Ultra-oxygen anion free radical clearance rate is 43.58%, improves 23.51% compared with single phosphorylation fribrillin.
In general, the raising of antioxidant activity is extremely significant.Emulsifying activity is 0.267m2/ g, with single phosphorylation muscle fibril egg
White compare improves 71.15%；Emulsion stability is 38.054%, is improved compared with single phosphorylation fribrillin
24.50%；Gel elastomer is 1.076, improves 23.68% compared with single phosphorylation fribrillin.
Embodiment 3
(1) Fresh Grade Breast rejects visible adipose connective tissue, cuts with a knife and is broken into meat gruel, the protein extraction of four times of volumes is added
Liquid is homogenized with homogenizer, refrigerated centrifuge, abandon supernatant stay precipitating, add protein extract repetition aforesaid operations twice slightly
Albumen mixes gained crude protein with the NaCl solution that the concentration of 4 times of volumes is 0.1mol/L, and homogeneous, refrigerated centrifuge abandons supernatant
Liquid stays precipitating, and the NaCl solution that the concentration for adding 4 times of volumes is 0.1mol/L repeats aforesaid operations twice, last gained paste
Precipitating is Fresh Grade Breast fribrillin, and the fribrillin of extraction is stored in 4 DEG C, and is finished in interior for 24 hours.
Wherein, the group of the protein extract becomes：0.1mol/L NaCl,0.002mol/L MgCl,0.001mol/L
The 0.1mol/L NaH of EDTA.2Na and pH=72PO4/Na2HPO4Mixed solution, above-mentioned concentration is each in protein extract
The concentration of component.Homogeneous homogenization conditions are 22000rpm, 30s, and refrigerated centrifuge condition is 5000r/min, 15min, 4 DEG C.
(2) sodium tripolyphosphate for participating in reaction is dissolved in the NaCl solution that concentration is 0.75mol/L, sodium tripolyphosphate is dense eventually
Degree is 3.40% (W/V), and adjusts its pH value and obtain sodium tripolyphosphate solution for 7.5.Add in above-mentioned sodium tripolyphosphate solution
Enter step (1) resulting fribrillin, the control of gained protein concentration is 15mg/mL, and magnetic stirring speed is under 1400rpm
Reaction 2 hours is dialysed 12 hours in 4 DEG C, the PBS of pH=7.4 after reaction, and the fribrillin for obtaining phosphorylation is molten
Liquid.
(3) chlorogenic acid is dissolved with the NaCl solution of 0.75mol/L, phosphorylation obtained by step (2) is added in solution of chlorogenic acid
In fribrillin solution afterwards, make the final concentration of 200 μ g/mL of chlorogenic acid, low speed (400rpm) magnetic agitation is reacted 4 hours
Fribrillin solution must be modified.
(4) modified fribrillin solution obtained by step (3) is put into water-bath, with the velocity gradient of 1 DEG C/min
It is warming up to 75 DEG C from 20 DEG C, continues to heat 30min after reaching 75 DEG C；After heating, sample is put into mixture of ice and water immediately
Middle cooling 30min obtains protein gel.
It is detected through the above method, when the addition concentration of chlorogenic acid is 200 μ g/mL, collaboration phosphorylation modification myogen is fine
The reducing power absorbance value of fibrillarin is 0.171, improves 6.2 compared with single phosphorylation fribrillin reducing power
Times；DPPH free radical scavenging activity is 63.166%, improves 1.58 times compared with single phosphorylation fribrillin clearance rate；
Ultra-oxygen anion free radical clearance rate is 49.118, improves 21.40% compared with single phosphorylation fribrillin.It is overall
For, the raising of antioxidant activity is extremely significant.Emulsifying activity is 0.174m2/ g, with single phosphorylation fribrillin phase
Than improving 11.54%；Emulsion stability is 35.064%, is improved compared with single phosphorylation fribrillin
14.72%；Gel elastomer is 0.952, improves 9.43% compared with single phosphorylation fribrillin.
Method of the invention improves fribrillin inoxidizability and functional characteristic using natural polyphenol collaboration phosphorylation,
Both the functional characteristic of albumen had been improved, while having improved its physiological activity, has improved modification efficiency.It meanwhile being Fresh Grade Breast and meat
Field has been widened in the improvement of product, for polyphenol and phosphate collaboration as food additives be applied to meat products provide it is convenient reliable
Method.
The above is only a preferred embodiment of the present invention, it is noted that for the common skill of the art
For art personnel, various improvements and modifications may be made without departing from the principle of the present invention, these improvements and modifications
Also it should be regarded as protection scope of the present invention.
Claims (7)
1. a kind of method for improving chicken myofibril protein antioxidant and functional characteristic, which is characterized in that include the following steps：
(1) protein extract is added in the chicken paste for rejecting visible fat connective tissue, is homogenized with homogenizer, refrigerated centrifuge, abandoned
Supernatant stays precipitating, repeats aforesaid operations and obtains chicken myofibril crude protein；By the NaCl of gained crude protein and 0.1mol/L
Solution mixing, homogeneous, refrigerated centrifuge abandon supernatant and stay precipitating, repeat aforesaid operations, and gained paste precipitating is that chicken myogen is fine
Fibrillarin；
(2) phosphorylation is modified：Under magnetic stirring by the resulting chicken myofibril albumen of step (1) and sodium tripolyphosphate solution
It is reacted, phosphorylation fribrillin solution of dialysing in the PBS of pH=7.4 in 4 DEG C after reaction to obtain；
(3) addition polyphenol modification：Polyphenol is made an addition in phosphorylation fribrillin solution obtained by step (2), is sufficiently stirred
Uniformly, low speed reacts under magnetic stirring, obtains modified fribrillin solution；The polyphenol is chlorogenic acid or galla turcica
Acid, the polyphenol concentration are 100-200 μ g/mL.
2. the method according to claim 1 for improving chicken myofibril protein antioxidant and functional characteristic, feature exist
In：Modified fribrillin solution obtained by step (3) is put into water-bath, is risen with the velocity gradient of 1 DEG C/min from 20 DEG C
Temperature continues to heat 30min after reaching 75 DEG C to 75 DEG C；After heating, sample is put into mixture of ice and water immediately cooling
30min obtains protein gel.
3. the method according to claim 1 or 2 for improving chicken myofibril protein antioxidant and functional characteristic, feature
It is：The group of protein extract described in step (1) becomes：0.1mol/L NaCl,0.002mol/L MgCl,
The 0.1mol/L NaH of 0.001mol/L EDTA.2Na and pH=72PO4/Na2HPO4Mixed solution.
4. the method according to claim 1 or 2 for improving chicken myofibril protein antioxidant and functional characteristic, feature
It is：Sodium tripolyphosphate solution described in step (2) is that sodium tripolyphosphate is dissolved in 0.75mol/L NaCl solution, trimerization phosphorus
The sour final concentration of 3.35-3.45% of sodium (w/v), pH value 7.47-7.53.
5. the method according to claim 4 for improving chicken myofibril protein antioxidant and functional characteristic, feature exist
In：Gained protein concentration is 14.80-15.20mg/mL, reaction time 1.9- after fribrillin is added in step (2)
2.1h。
6. the method according to claim 1 or 2 for improving chicken myofibril protein antioxidant and functional characteristic, feature
It is：With the NaCl solution dissolution chlorogenic acid or gallic acid of 0.75mol/L in step (3).
7. the method according to claim 1 or 2 for improving chicken myofibril protein antioxidant and functional characteristic, feature
It is：Homogeneous, homogenization conditions in step (1) are：22000rpm, 30s, refrigerated centrifuge condition are：5000r/ under the conditions of 4 DEG C
Min is centrifuged 15min.
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| CN111328994A (en) * | 2020-02-28 | 2020-06-26 | 宁波大学 | Special flavor duck meat and liver protein composite emulsified sausage and preparation method thereof |
| CN113072612A (en) * | 2021-03-16 | 2021-07-06 | 南京农业大学 | Method for improving digestibility and heat stability of chicken protein |
| CN113080244A (en) * | 2021-04-13 | 2021-07-09 | 南京泛成生物科技有限公司 | Use method and application of natural antioxidant |
| CN114431284A (en) * | 2022-02-28 | 2022-05-06 | 陕西科技大学 | Method for improving oxidation stability and gel performance of myofibrillar protein |
| CN115624169A (en) * | 2022-10-28 | 2023-01-20 | 陕西师范大学 | Method for improving stability of myofibrillar protein |
| CN116172115A (en) * | 2022-12-05 | 2023-05-30 | 西北农林科技大学 | Method for improving damage of high-dose EGCG to meat protein gel characteristics by adding L-Lys |
Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101161671A (en) * | 2007-11-15 | 2008-04-16 | 天津商业大学 | Method for extracting fibrillin from chicken |
| CN103564143A (en) * | 2013-10-14 | 2014-02-12 | 中国肉类食品综合研究中心 | Preparation method of fibrillin with high gel property |
| CN104845383A (en) * | 2015-05-21 | 2015-08-19 | 浙江海洋学院 | Myofibrillar protein-chitosan nanometer microsphere composite membrane |
| CN106490512A (en) * | 2016-10-19 | 2017-03-15 | 江苏省农业科学院 | A kind of production method of instant leisure fish |
| CN107821989A (en) * | 2017-12-04 | 2018-03-23 | 南京农业大学 | A kind of glycosylation process for improving class PSE Fresh Grade Breast fribrillin Gelatin Qualities |
| CN108617848A (en) * | 2018-04-12 | 2018-10-09 | 厦门大学 | A kind of preparation method of strong gelation fribrillin |
-
2018
- 2018-06-08 CN CN201810585829.0A patent/CN108850420A/en active Pending
Patent Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101161671A (en) * | 2007-11-15 | 2008-04-16 | 天津商业大学 | Method for extracting fibrillin from chicken |
| CN103564143A (en) * | 2013-10-14 | 2014-02-12 | 中国肉类食品综合研究中心 | Preparation method of fibrillin with high gel property |
| CN104845383A (en) * | 2015-05-21 | 2015-08-19 | 浙江海洋学院 | Myofibrillar protein-chitosan nanometer microsphere composite membrane |
| CN106490512A (en) * | 2016-10-19 | 2017-03-15 | 江苏省农业科学院 | A kind of production method of instant leisure fish |
| CN107821989A (en) * | 2017-12-04 | 2018-03-23 | 南京农业大学 | A kind of glycosylation process for improving class PSE Fresh Grade Breast fribrillin Gelatin Qualities |
| CN108617848A (en) * | 2018-04-12 | 2018-10-09 | 厦门大学 | A kind of preparation method of strong gelation fribrillin |
Non-Patent Citations (4)
| Title |
|---|
| 刘娜等: "鸡肉肌原纤维蛋白酶解产物的抗氧化活性研究 ", 《食品研究与开发》 * |
| 李玲等: "绿原酸抑制猪肉肌原纤维蛋白氧化及NDEA生成的作用研究 ", 《食品工业科技》 * |
| 王诗萌等: "鸡肉与虾蛄中肌原纤维蛋白磷酸化特性的比较", 《食品与发酵工业》 * |
| 贾娜等: "氧化条件下没食子酸对猪肉肌原纤维蛋白结构及凝胶特性的影响", 《食品工业科技》 * |
Cited By (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN110214851A (en) * | 2019-05-08 | 2019-09-10 | 大连工业大学 | A method of improving fish myofibrillar protein gel characteristic |
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| CN113072612A (en) * | 2021-03-16 | 2021-07-06 | 南京农业大学 | Method for improving digestibility and heat stability of chicken protein |
| CN113080244A (en) * | 2021-04-13 | 2021-07-09 | 南京泛成生物科技有限公司 | Use method and application of natural antioxidant |
| CN114431284A (en) * | 2022-02-28 | 2022-05-06 | 陕西科技大学 | Method for improving oxidation stability and gel performance of myofibrillar protein |
| CN114431284B (en) * | 2022-02-28 | 2023-11-14 | 陕西科技大学 | Myofibrillar protein oxidation stability and gel performance improving method |
| CN115624169A (en) * | 2022-10-28 | 2023-01-20 | 陕西师范大学 | Method for improving stability of myofibrillar protein |
| CN116172115A (en) * | 2022-12-05 | 2023-05-30 | 西北农林科技大学 | Method for improving damage of high-dose EGCG to meat protein gel characteristics by adding L-Lys |
| CN116172115B (en) * | 2022-12-05 | 2024-05-14 | 西北农林科技大学 | Method for improving damage of high-dose EGCG to meat protein gel characteristics by adding L-Lys |
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