CN116473157A - Goose muscle fibrillin modification method and application of goose muscle fibrillin modification method in preparation of fat mimics - Google Patents
Goose muscle fibrillin modification method and application of goose muscle fibrillin modification method in preparation of fat mimics Download PDFInfo
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Classifications
-
- 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
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/04—Animal proteins
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23B—PRESERVING, e.g. BY CANNING, MEAT, FISH, EGGS, FRUIT, VEGETABLES, EDIBLE SEEDS; CHEMICAL RIPENING OF FRUIT OR VEGETABLES; THE PRESERVED, RIPENED, OR CANNED PRODUCTS
- A23B4/00—General methods for preserving meat, sausages, fish or fish products
- A23B4/14—Preserving with chemicals not covered by groups A23B4/02 or A23B4/12
- A23B4/18—Preserving with chemicals not covered by groups A23B4/02 or A23B4/12 in the form of liquids or solids
- A23B4/20—Organic compounds; Microorganisms; Enzymes
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23D—EDIBLE OILS OR FATS, e.g. MARGARINES, SHORTENINGS, COOKING OILS
- A23D7/00—Edible oil or fat compositions containing an aqueous phase, e.g. margarines
- A23D7/005—Edible oil or fat compositions containing an aqueous phase, e.g. margarines characterised by ingredients other than fatty acid triglycerides
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23D—EDIBLE OILS OR FATS, e.g. MARGARINES, SHORTENINGS, COOKING OILS
- A23D7/00—Edible oil or fat compositions containing an aqueous phase, e.g. margarines
- A23D7/015—Reducing calorie content; Reducing fat content, e.g. "halvarines"
-
- 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
- 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
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
- A23L13/40—Meat products; Meat meal; Preparation or treatment thereof containing additives
- A23L13/42—Additives other than enzymes or microorganisms in meat products or meat meals
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
- A23L13/40—Meat products; Meat meal; Preparation or treatment thereof containing additives
- A23L13/42—Additives other than enzymes or microorganisms in meat products or meat meals
- A23L13/43—Addition of vegetable fats or oils; Addition of non-meat animal fats or oils; Addition of fatty acids
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
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- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Polymers & Plastics (AREA)
- Food Science & Technology (AREA)
- Nutrition Science (AREA)
- Health & Medical Sciences (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Biochemistry (AREA)
- Zoology (AREA)
- Microbiology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
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- Meat, Egg Or Seafood Products (AREA)
Abstract
The invention discloses a goose fibril protein modification method and application of preparing a fat simulator, which is characterized in that the modification method comprises the steps of adding sodium tripolyphosphate into a goose fibril protein dispersion solution with the concentration of 10mg/mL while stirring to enable the final concentration to be 1%, stirring for 30min, then carrying out ultrasonic treatment at 200-600W for 12min at 20kHz, keeping the constant temperature of water bath at 45 ℃ for 48min, and then placing the solution into an ice bath for 30min; adding the solution into the dialyzate, magnetically stirring and dialyzing for 12 hours, and centrifuging to remove supernatant; finally, carrying out vacuum freeze drying to obtain modified goose muscle fibril protein; after the modified goose muscle fibrillin powder is dissolved in water to adjust the concentration to 10mg/mL, sunflower oil with equal mass is added, and the high-speed homogenizer is homogenized for 2min at 10000rpm to obtain the fat mimics.
Description
Technical Field
The invention relates to a protein modification method, in particular to a goose muscle fibrilcellulose modification method and application of preparing a fat mimetic.
Background
The goose is an ideal high-protein, low-fat and low-cholesterol nutritional health food, and the goose has rich and balanced essential amino acid content and contains multiple vitamins and minerals such as calcium, phosphorus, selenium, iron, zinc and the like. But the surface of the goose is mostly covered with connective tissues, the muscle fiber is thicker, the meat quality is thicker and older, the functional characteristics are poor, and the development and the utilization of the goose are less in the domestic market at present. Therefore, the structure of the goose is improved, and the function of the goose is improved, so that the application field of the goose is further expanded, and the overall economic benefit is improved. The main methods of protein modification are physical techniques (e.g. microwave, high pressure, ultrasound, radiation), chemical techniques (e.g. glycosylation, phosphorylation, acylation) and biological techniques (e.g. enzymatic hydrolysis, enzymatic cross-linking). The physical modification has the advantages of good safety, short acting time, small influence on the nutritional performance of the product and the like, but the modification effect is not obvious. The enzymatic reaction has obvious effect, mild condition and strong specificity, but has higher cost. Among the protein modification methods, chemical modification has the advantages of good repeatability, convenient operation, easy control and the like, and is most widely applied. The phosphorylation has the advantages of low improvement cost, obvious effect, easy realization, industrialization and the like, does not generate toxic products in the phosphorylation process, and has greater utilization potential than glycosylation or acylation. However, the traditional phosphorylation modification method has the characteristics of relatively long modification time, high raw material pretreatment energy consumption and low reaction efficiency. Therefore, it is necessary to accelerate the reaction between the protein and the phosphorylating agent and to improve the reaction efficiency.
The emulsion sausage is a typical emulsion meat product, generally containing 30% animal fat. However, due to the high fat content, the product is easy to oxidize fat, so that the quality of the product is reduced, the good texture characteristics and the good color are lost, the storage life is shortened, and some potential safety hazards are brought, so that the acceptance of consumers is affected. At the same time, high fat content products also pose a serious threat to the health of the consumer. The fat mimics have the function similar to fat, and the heat quantity is far lower than that of fat, so that the fat mimics not only can be applied to high-fat foods, but also can obviously reduce the total energy of the foods. Therefore, development of a substance capable of replacing animal fat containing a large amount of saturated fatty acids in meat products while maintaining the original texture, flavor and sensory quality of the fat has been a hot problem in meat product processing research. At present, related research reports about phosphorylation and ultrasonic synergistic modification of goose muscle fibril protein and application of the goose muscle fibril protein in preparation of fat mimics are not disclosed at home and abroad.
Disclosure of Invention
The invention aims to provide a goose muscle fibrillin modification method with improved myofibrillin solubility, and improved emulsifying property, foamability, water holding and oil holding properties, gel property and other functional properties, and an application of the method for preparing a fat mimetic.
The technical scheme adopted for solving the technical problems is as follows: a method for modifying goose myofibrillar protein, which comprises the following steps:
(1) Preparing a protein solution: dissolving goose muscle fibrillin in 0.02mol/L PBS solution to prepare a protein dispersion solution with the concentration of 10 mg/mL;
(2) Ultrasonic assisted phosphorylation modification: adding sodium tripolyphosphate into the protein dispersion solution prepared in the step (1) while stirring to make the final mass concentration of the solution be 1%, stirring for 30min, then performing ultrasonic treatment at 200-600W for 12min at 20kHz, keeping the water bath at a constant temperature of 45 ℃ for 48min, and then placing the solution into an ice bath for 30min;
(3) And (3) dialysis: adding the solution obtained in the step (2) into the dialysate, magnetically stirring, changing the dialysate every 2 hours, dialyzing for 12 hours, centrifuging for 15 minutes at 4 ℃ and 5100g, and removing supernatant;
(4) And (3) drying: and (3) performing a vacuum freeze drying method on the precipitate obtained in the step (3) to obtain the modified goose muscle fibril protein.
Further, the preparation method of the goose myofibrillar protein in the step (1) comprises the following steps:
(1) Thawing the split-packed goose meat at 4 ℃ for 12 hours, mincing with a meat mincer, adding 4 times of extracting solution by mass, homogenizing for 60s with a high-speed disperser for 10 s/time in ice bath, centrifuging the sample at 12600g at 4 ℃ for 20min after homogenizing, and removing the supernatant, wherein the formula of the extracting solution is 0.1mol/L Tris, 10mmol/L EDTA, and the pH=8.3;
(2) Dispersing the precipitate obtained in step (1) in 4 times volume of standard salt solution, centrifuging at 12600g at 4deg.C for 10min to remove supernatant, and repeating the steps twice, wherein the standard salt solution has a formula of 0.1mol/LKCl and 0.02mol/L K 2 HPO 4 /KH 2 PO 4 、2mmol/L MgCl 2 、1mmol/L EGTA，pH7.0；
(3) Placing the precipitate obtained in the step (2) into 4 times of standard salt solution containing 1% TritonX-100, centrifuging 12600g for 10min to collect the precipitate, and repeating the step twice;
(4) Then uniformly dispersing the precipitate obtained in the step (3) in a standard salt solution with the volume of 4 times, centrifuging 12600g for 10min, collecting the precipitate, and repeating the step twice;
(5) Dissolving the precipitate obtained in the step (4) in 0.1mmol/L KCl solution with the volume of 4 times, centrifuging 12600g for 10min to collect the precipitate, and repeating the step twice;
(6) Filtering the precipitate obtained in the step (5) through three layers of gauze, adding 0.1mmol/LNaCl solution with the volume of 4 times, and centrifuging 12600g for 10min to obtain the precipitate, namely the purified goose muscle fibril protein.
Further, the formulation of the PBS solution in step (1) is as follows: 0.02mol/L K 2 HPO 4 ，0.02mol/LKH 2 PO 4 ，0.6mol/L NaCl，pH＝7。
Further, the ultrasonic power in the step (2) is 400W.
Further, the dialysate in the step (3) is deionized water.
The application of the goose muscle fibrillin obtained by modification by the method in the preparation of fat mimics.
Further, the preparation method of the fat mimetic comprises the following steps: after the modified goose muscle fibrillin powder is dissolved in water to adjust the concentration to 10mg/mL, adding sunflower oil with equal mass, homogenizing for 2min by a high-speed homogenizer at 10000rpm to obtain the fat mimics. The vegetable oil and the protein solution are dispersed in advance by adopting the pre-emulsification technology and then added into the ground meat matrix, and the mixed multiphase system is mutually dispersed and connected under the mechanical and chemical actions, so that a stable and uniform form is finally formed. During the formation of the emulsion phase, the soluble protein can migrate, position, associate and stretch around the fat particles to form a dense film material, and the oil can be stabilized or immobilized in the protein matrix. At the same time, hydrophilic groups in protein molecules are combined with water molecules, so that the original mutually-insoluble phase state systems are tightly connected to form a unified whole. In the heating process, the soluble protein is gelled to form a protein matrix, so that fat and water are firmly restrained, and a good emulsifying effect is achieved.
Further, the fat mimics replace 25-75% of the pig backfat by mass in the goose meat emulsion sausage, wherein the mass ratio of the goose meat to the pig backfat in the goose meat emulsion sausage before replacement is 4:1.
Further, the fat mimics replace 50% of the pig backfat by mass in the goose meat emulsion sausage, wherein the mass ratio of the goose meat to the pig backfat in the goose meat emulsion sausage before replacement is 4:1.
Compared with the prior art, the invention has the advantages that: the invention discloses a goose muscle fibrillin modification method and application of preparing a fat simulator, wherein ultrasonic waves and phosphorylation are applied to the modification of poultry muscle fibrillin, and high-intensity ultrasonic is utilized to assist in the phosphorylation modification, on one hand, ultrasonic cavitation can generate strong physical forces, including shearing force, shock wave and turbulence, so that the functional characteristics of protein can be possibly changed; on the other hand, the cavitation bubble explosion can break the covalent bond, expose more reaction sites and promote the protein phosphorylation modification. The ultrasonic and phosphorylation effects are synergistic, so that the solubility of the obtained poultry myofibrillar protein is improved, and the emulsifying property, foamability, water and oil holding property, gel property and other functional properties of the poultry myofibrillar protein are improved.
The 400W ultrasonic-assisted phosphorylation modified protein is pre-emulsified and then used as a fat simulator to replace pig backfat with different proportions in the emulsified sausage, and the fat simulator is found to replace fat so as not to cause negative influence on the texture characteristics of the low-fat emulsified sausage, and the emulsified sausage has more juiciness when the replacement proportion is 50%, the gel strength, hardness and cohesiveness of the emulsified sausage can be obviously improved, the tissue structure is more continuous and compact, and a uniform and ordered network structure is formed. By studying the pH, color difference, fat oxidation number and volatile basic nitrogen change of the emulsion sausage in different storage periods (10, 20, 30 and 40 d), the use of the fat simulant can improve the stability of the pH value in the storage process of the emulsion sausage, inhibit fat oxidation and protein degradation, and prolong the storage time of the emulsion sausage.
Drawings
FIG. 1 is a graph showing the solubility of goose myofibrillar proteins;
FIG. 2 shows the water and oil retention of goose myofibrillar proteins;
FIG. 3 shows the Emulsion Stability (ESI) and the EAI of goose myofibrillar proteins;
FIG. 4 is a laser confocal of a goose muscle fibril protein emulsion;
FIG. 5 shows the foaming property (FC) and Foaming Stability (FS) of goose myofibrillar proteins;
FIG. 6 is the texture characteristics of the low fat emulsified sausage;
FIG. 7 is a dynamic rheological profile of a low fat emulsion sausage; wherein (a) is the storage modulus of the emulsion temperature sweep, (b) is the loss modulus of the emulsion temperature sweep, (c) is the tan delta of the emulsion temperature sweep, and (d) is the storage modulus and loss modulus of the emulsion frequency sweep;
FIG. 8 is an SEM observation of a low fat emulsion sausage;
FIG. 9 is a sensory evaluation of low fat emulsified sausage; in the figure, (a) is the total sensory evaluation score of the emulsified sausage with different pig backfat substitution ratios, and (b) is a sensory evaluation radar chart;
FIG. 10 shows pH change during storage of low fat emulsion sausage;
FIG. 11 shows color difference change during storage of low fat emulsion sausage; wherein (a) is L, (b) is a, (c) is b, (d) is chromaticity, and (e) is whiteness;
FIG. 12 shows the change in TBARS values during storage in low fat emulsion intestines;
FIG. 13 shows the change in TVB-N values during storage in low fat emulsion intestines.
Detailed Description
The invention is described in further detail below with reference to the embodiments of the drawings.
1. Detailed description of the preferred embodiments
Blank comparison 1
The preparation method of the goose muscle fibrillin comprises the following specific steps:
1. thawing the split-packed goose meat at 4 ℃ for 12 hours, mincing with a meat mincer, adding 4 times of extracting solution (containing 0.1mol/L Tris, 10mmol/L EDTA and pH=8.3), carrying out ice bath, homogenizing for 60s,10 s/time by using a high-speed disperser, and centrifuging the sample at 12600g and 4 ℃ for 20min after the homogenization is finished;
2. after removing the supernatant, the precipitate was re-uniformly dispersed in a standard salt solution (containing 0.1mol/L KCl, 0.02 mol/LK) at 4 times the volume 2 HPO 4 /KH 2 PO 4 、2mmol/L MgCl 2 1mmol/L EGTA, pH 7.0), centrifuging at 12600g at 4deg.C for 10min to remove supernatant, and repeating the steps twice;
3. placing the precipitate obtained after centrifugation in 4 times of standard salt solution containing 1% TritonX-100, centrifuging 12600g for 10min to collect precipitate, and repeating the steps twice;
4. then re-uniformly dispersing the precipitate in a standard salt solution with the volume of 4 times, centrifuging 12600g for 10min, collecting the precipitate, and repeating the steps twice;
5. dissolving the obtained precipitate in 4 times of 0.1mmol/L KCl solution, centrifuging 12600g for 10min to collect precipitate, and repeating the steps twice;
6. finally, the obtained precipitate is filtered through three layers of gauze, 4 times of volume of 0.1mmol/L NaCl solution is added into the obtained solution, 12600g is centrifuged for 10min, and the obtained precipitate is purified goose muscle fibril protein and is marked as GMP. Protein concentration was determined using BCA kit.
Example 1
The method for modifying the goose muscle fibrillin by utilizing the ultrasonic mainly comprises the following steps:
1. dissolving goose muscle fibrillin in 0.02mol/L PBS (0.02 mol/L K) 2 HPO 4 ，0.02mol/L KH 2 PO 4 0.6mol/L NaCl, ph=7) to form a protein dispersion solution with a concentration of 10 mg/mL;
2. after magnetic stirring for 30min, carrying out ultrasonic treatment at 400W for 12min at 20 kHz;
3. the water bath is kept at a constant temperature of 45 ℃ for 48min, and the solution is put into an ice bath for 30min;
4. adding magnetic stirring dialysate (deionized water) into the dialysate, changing dialysate every 2 hours, dialyzing for 12 hours, centrifuging for 15min at 4deg.C and 5100g, and removing supernatant;
5. and (3) drying: vacuum freeze drying method is adopted to obtain modified protein powder, and the modified protein powder is marked as UGGMP.
Example 2
The phospho-modification of goose fibril protein was carried out as in example 1, with the following differences: in step 2, the protein dispersion solution in step 1 was stirred while adding sodium tripolyphosphate to a final mass concentration of Sodium Tripolyphosphate (STP) of 1%, and the protein dispersion solution containing STP was stirred for 30min. The modified protein powder finally obtained was labeled GMP-STP.
Example 3
Ultrasonic-assisted phosphorylation modification of goose fibril protein was carried out as in example 1, except that: in step 2, the protein dispersion solution in step 1 was added with Sodium Tripolyphosphate (STP) to a final mass concentration of 1% while stirring, and the protein dispersion solution containing STP was stirred for 30min before ultrasonic treatment. The modified protein powder finally obtained was labeled UP-400.
Example 4
The difference from example 3 is that: the ultrasonic power was 200W. The modified protein powder finally obtained was labeled UP-200.
Example 5
The difference from example 3 is that: the ultrasonic power was 300W. The modified protein powder finally obtained was labeled UP-300.
Example 6
The difference from example 3 is that: the ultrasonic power was 500W. The modified protein powder finally obtained was labeled UP-500.
Example 7
The difference from example 3 is that: the ultrasonic power was 600W. The modified protein powder finally obtained was labeled UP-600.
2. Application examples
The modified protein powder obtained in the above example 3 was sufficiently dissolved in water to adjust the concentration to 10mg/mL, and the weight ratio was 1:1, adding sunflower oil in proportion, homogenizing for 2min at 10000rpm in a high-speed homogenizer, and storing the prepared pre-emulsion at 4deg.C to serve as fat simulator for replacing 25%, 50% and 75% of pig backfat in goose meat emulsion sausage.
The preparation method of the emulsified sausage comprises the following steps:
(1) Formulation of
Goose meat: fat pig weight 4:1 (w/w), the additive mass percentages of the seasonings and the food additives are as follows: 1.2% of edible salt, 0.04% of pricklyash peel powder, 1% of cooking wine, 0.4% of composite phosphate, 0.1% of beta-cyclodextrin, 0.3% of TG enzyme, 15% of ice water and 0.1% of red yeast rice (all ingredients are added according to the total weight percentage of goose meat and pig fat).
TABLE 1 Main raw material proportions
| Formula (%) | CK | FM-25％ | FM-50％ | FM-75％ |
| Goose meat | 80 | 80 | 80 | 80 |
| Pig backfat | 20 | 15 | 10 | 5 |
| Fat mimics | 0 | 5 | 10 | 15 |
(2) Process flow
Finishing fresh raw meat, cutting into blocks, curing, chopping, sausage filling, knotting, airing, steaming, spraying and cooling, and packaging a finished product.
(3) Key points of operation
Trimming and curing: selecting fresh Jiang Shanda goose, removing connective tissue such as fascia, cut into meat pieces (2X 2 cm), adding salt and Chinese liquor, mixing, and pickling at 4deg.C for 5 hr. The pig backfat is peeled and cut into meat pieces with the same size.
Chopping: the pickled raw meat, the composite phosphate, the TG enzyme and other food additives are added into a chopper in proportion, after being chopped for 30s at a low speed, the pig backfat and the fat mimics are added into the chopped raw meat, and then the chopping is continued for 90s at a high speed. In the chopping process, 15% (w/w) of ice water is added in batches, and the low temperature of the system is maintained. The minced meat after being chopped is uniform and has viscosity.
Clysis, knotting and drying: the chopped meat emulsion is poured into a sheep casing with the diameter of about 15mm, and the meat emulsion is kept uniform, consistent in density and proper in tightness as much as possible in the sausage filling process. Knotting at about 8cm length, using a clean toothpick bundle Kong Fangqi to avoid intestinal rupture during cooking. And after the clysis is finished, uniformly placing the clysis in a ventilated and dried place for airing until no obvious oil-water exudation exists on the surface.
And (3) cooking: placing the dried emulsified sausage in a water bath kettle at 25 ℃, continuously carrying out water bath for 30min after the temperature is increased to 75 ℃, immediately spraying and cooling after the steaming is finished, wiping oil water on the surface of the sausage, packaging to obtain a product, and storing at-20 ℃.
3. Analysis of modified results of goose myofibrillar proteins
1. Solubility of goose muscle fibrillin
As shown in fig. 1, the solubility of goose myofibrillar proteins after the ultrasonic treatment, the phosphorylation treatment and the ultrasonic auxiliary treatment were all significantly higher than those of the blank Group (GMP). The solubility of the phosphorylated modified histone is higher than that of an ultrasonic group, and the solubility of the phosphorylated modified by using ultrasonic assistance is obviously higher than that of the phosphorylated group, which indicates that the effect of ultrasonic assistance is better than that of single phosphorylation and single ultrasound.
2. Water retention and (WHC) oil retention (OBC) of goose myofibrillar proteins
As shown in fig. 2, the water and oil retention properties of the phospho-modified goose myofibrillar proteins were significantly higher than those of the blank combination sonication group. Compared with the phosphorylation modified group, the ultrasonic-assisted phosphorylation has no obvious influence on the water retention of the protein, but the water retention of the protein is obviously increased when the ultrasonic power is 400W for the assisted phosphorylation.
3. Emulsion Activity (EAI) and Emulsion Stability (ESI) of goose myofibrillar proteins
As shown in fig. 3, the EAI of protein after ultrasonication and phosphorylation was increased by 33.56% and 174.27% respectively, compared to GMP; after 200W ultrasonic assisted phosphorylation, the emulsification activity effect is better than that of single phosphorylation or ultrasonic treatment, the EAI is increased by 208.50 percent, and the EAI is highest when the ultrasonic power is 400W, and the increase is 298.90 percent. For emulsion stability, there is no significant difference from the blank group after ultrasonic treatment or phosphorylation treatment, but the emulsion stability of the protein after ultrasonic-assisted phosphorylation treatment is significantly improved, and the emulsion stability of the protein is highest when ultrasonic power is 400W for assisted phosphorylation.
4. Laser confocal of goose muscle fibril protein emulsion
As shown in fig. 4, the emulsion particles of the ultrasonic treatment group and the blank group are larger and unevenly dispersed, the protein emulsion particles after the phosphorylation treatment are obviously reduced but are still uneven, and the protein emulsion particles after the ultrasonic-assisted phosphorylation treatment are smaller and more evenly distributed, which indicates that the stability of the protein emulsion is improved by the ultrasonic-assisted phosphorylation.
5. Foaming property (FC) and Foaming Stability (FS) of goose myofibrillar protein
As shown in fig. 5, protein FC increased by 13.55% and 31.31% respectively after the ultrasonic treatment and the phosphorylation treatment compared with GMP; after 200W ultrasonic assisted phosphorylation, the foaming activity effect is better than that of single phosphorylation or ultrasonic treatment, the FC is increased by 51.42%, the FC is highest when the ultrasonic power is 400W, and the FC is increased by 104.21%. The effects of sonication, phosphorylation and ultrasound-assisted phosphorylation were small for foam stability, but protein foam stability was highest when the ultrasound power was 400W-assisted phosphorylation.
6. Gel character (texture, water retention, loss on cooking) of goose muscle fibril protein
TABLE 2 gel character of goose muscle fibrillin (texture, water retention, loss on cooking)
| WHC(％) | Loss of cooking (%) | Gel strength | |
| GMP | 43.43±4.06 g | 35.24：0.95 a | 62.27±3.57 g |
| UGMP | 55.12±0.72 f | 35.01±0.37 a | 82.98±3.51 f |
| GMP-STP | 73.23±2.58 e | 10.97±0.67 b | 123.47±1.63 e |
| UP-200 | 78.55±0.86 d | 6.51±0.34 c | 134.61±1.71 d |
| UP-300 | 82.11±0.43 c | 6.39±0.57 c | 143.85±4.18 c |
| UP-400 | 87.7±1.16 a | 4.27±0.55 de | 173.18±2.8 a |
| UP-500 | 82.96±0.04 b | 3.82±0.69 e | 155.21±0.93 b |
| UP-600 | 81.13±1.3 cd | 4.98±0.23 d | 143.88±3.32 c |
As shown in table 2, the protein gel water retention was increased by 26.92% and 68.62% after the ultrasonic treatment and the phosphorylation treatment, respectively, compared to GMP, and the protein gel water retention was higher for the ultrasonic assisted phosphorylation treatment, and was the highest when the ultrasonic power was 400W assisted phosphorylation, increased by 101.93%. For gel cooking loss, there was no significant difference between the sonicated and blank groups, while protein gel cooking loss after phosphorylation was significantly reduced (68.87% reduction), with further reduction in cooking loss after ultrasound-assisted phosphorylation, and protein gel cooking loss was minimal (87.88% reduction) when ultrasound power was 400W-assisted phosphorylation. Compared with GMP, the gel strength of the protein after ultrasonic treatment and phosphorylation is respectively increased by 33.26 percent and 98.28 percent; the gel strength after the ultrasonic assisted phosphorylation is better than that of the single phosphorylation or ultrasonic treatment, and the gel strength is highest when the ultrasonic power is 400W, and the increase is 178.11 percent.
In conclusion, after the ultrasonic-assisted phosphorylation modification, the functional property and the gel property of the protein are obviously higher than those of a blank group, an ultrasonic group and a phosphorylation group, which indicates that the ultrasonic and the phosphorylation play a synergistic role, and when the ultrasonic power is 400W for assisting the phosphorylation, the functional property and the gel property of the protein are the best.
4. Analysis of results for low fat emulsified sausage
1. Moisture content and cooking loss of low fat emulsified sausage
TABLE 3 moisture content and cooking loss of low fat emulsion sausage
| Moisture content (%) cooking loss (%) | |
| CK | 52.19±3.09 b 4.46±0.58 ab |
| FM-25％ | 51.52±2.15 b 4.23±0.43 b |
| FM-50％ | 58.36±0.98 a 4.92±0.42 ab |
| FM-75％ | 62.95±1.6 a 5.52±0.74 a |
As shown in table 3, when the addition amount of the fat mimetic was 25%, the emulsified intestinal water content was not significantly different from that of the control group (P > 0.05), and when the addition amount was increased to 50% and 75%, the water content was significantly increased (P < 0.05); the cooking loss rate of the emulsified sausage tends to decrease and then increase with the increase of the proportion of the substituted fat, but has no obvious difference from the CK group. This is probably due to the fact that when the proportion of alternative fat is low, the fat mimetic and the protein particles in the meat are thoroughly mixed during the chopping process, and during the subsequent heating process, interactions between the proteins occur, forming a compact and stable three-dimensional network structure, thereby improving the thermostability of the emulsified sausage. With further increases in the proportion of alternative fat, a large amount of moisture is introduced, resulting in a decrease in the binding capacity between protein and water molecules as well as fat molecules, and thus an increase in the rate of loss of cooking. Overall, the addition of fat mimetics had no significant effect on the low fat emulsified intestinal cooking loss, indicating that they were similar in water retention.
2. Texture characteristics of low-fat emulsified sausage
As shown in fig. 6, after 25% and 75% of pig backfat was replaced with fat mimetics, the hardness of the low fat emulsified sausage was not significantly different from the CK group (p > 0.05), while the hardness was significantly increased when 50% of pig backfat was replaced. The use of the modified protein fat mimetic was demonstrated to be effective in controlling the addition of fat in the product, preventing a substantial reduction in hardness while significantly improving the juiciness of the product (Table 3). The gel strength and hardness of the emulsified sausage also show the same change trend. This may be due to the fact that the simulant plays a role in filling the interstices of the emulsified intestinal gel network. In addition, the chewiness was not significantly different from CK in the FM-25%, FM-50% group (p > 0.05), but only significantly reduced when the fat substitution rate was 75%. The replacement of fat by the simulant has no obvious influence on the elasticity and the recovery of the emulsified sausage and can obviously improve the cohesiveness of the emulsified sausage. Because the added modified protein matrix simulant can interact with protein and fat in the meat emulsion to form a denser gel structure, and the meat emulsion is more viscous due to the high water content of experimental groups and the existence of sunflower oil, so that the effect of fat on product cohesiveness is compensated. In summary, it was found that the replacement of fat with fat mimetics does not negatively affect the texture properties of the low fat emulsified sausage, but rather that a suitable replacement rate can improve the gel strength, hardness and cohesiveness of the emulsified sausage. The use of the modified protein matrix fat mimetic is described as being effective in controlling the addition of fat in the product and improving the quality of the product.
3. Dynamic rheological properties of low-fat emulsified sausage
As shown in fig. 7 (a-c), all samples showed similar trends over the 15-90 ℃ range, indicating that the different proportions of the simulant replacement fat had substantially no effect on the temperature of meat emulsion protein denaturation, but both G' and G "were significantly higher in the FM-50% group than in the other groups, consistent with their texture property changes. G' (FIG. 7 (a)) drops sharply at 15-50℃, mainly because of the large amount of GMP that dissolves and swells during the mincing of the goose emulsion and folds in this temperature range. All samples exhibited a first thermal denaturation peak around 55 ℃, which indicates that most of the myosin molecules had developed at this time and cross-linked together to form a weak three-dimensional gel network. Subsequently, G' bottoms out at 60℃because the temperature can cause myosin tail expansion and denaturation, changes in the interior of the protein molecule, disrupting the initially formed protein network. After further heating (60-90 ℃), G' rises sharply, probably because the protein continues to aggregate, resulting in gradual conversion of the semi-sol to an elastic solid gel in this temperature range, at which time the gel network structure of the meat emulsion is fully formed. However, the G' of the FM-50% group was higher than the CK group indicating that the use of fat mimetics can significantly improve the gel properties of low fat goose-emulsion. In the heating process, sunflower oil and modified protein in the pre-emulsion can interact with meat emulsion protein to form an irregular network gel structure, so that the elasticity of the meat emulsion gel is enhanced.
As can be seen from FIG. 7 (b), the G 'of the four group meat emulsion was similar to the G' results, with the G 'of the FM-50% group meat emulsion being the highest, with the G' each exhibiting a first peak at about 55℃ and a second peak at about 75℃, followed by a decrease. G' is always greater than G "throughout the heating process, indicating that the elasticity of the matrix gel dominates during this process.
Tan delta is a ratio of G "to G' in value that can laterally reflect changes in the rheological properties of the emulsion. As shown in fig. 7 (c), tan δ decreases with increasing temperature in the range of 15-35 ℃; the subsequent rise in Tan delta and peak at 40 ℃, probably because disulfide cross-linking promotes myosin heavy chain binding, leading to elastic network formation. At 55 ℃, tan delta continued to decrease after another peak, indicating a further change in GMP molecular conformation and formation of an irreversible solid gel. Furthermore, the general trend of Tan δ with temperature was consistent among the groups, indicating that the three-dimensional network formed was similar in rheology.
As shown in fig. 7 (d), the frequency sweep of meat emulsion shows the same trend of change in the viscoelastic modulus between the four groups and can form a stable gel system, but the G' values of the FM-25% and FM-50% groups are significantly higher than those of the CK group, probably because the fat mimetics are uniformly filled between the other raw and auxiliary materials, and act as an adhesive effect, helping to form a tight gel structure, which is consistent with the coacervation results in fig. 6.
4. SEM observation of low-fat emulsified sausage
As shown in fig. 8, the emulsified sausages with different proportions of fat mimetics instead of fat have a certain difference in microstructure. The CK group has uneven surface, rough structure and no regularity. In contrast, the tissue structures of the FM-25%, FM-50% and FM-75% groups are more continuous and compact, and a more uniform and ordered network structure is formed. This is because animal fat particles are larger and unevenly distributed during processing, while homogenized fat mimetics are smaller in particle size and evenly distributed and can be effectively and evenly distributed in the meat emulsion. In addition, the interaction of the modified proteins in the fat mimics and the proteins in the meat emulsion can also enhance the compactness and the emulsion stability of the tissue structure of the emulsion. It is possible that the regular network structure reduces the cooking loss of the emulsified sausage, and the gel strength is improved, and the results in the study indicate that the addition of the fat simulant can not only reduce the fat content in the meat product, but also further improve the quality of the meat product, and has expected application value.
5. Sensory evaluation of low-fat emulsified sausage
As shown in fig. 9 (a), the total scores of the sensory scores of the FM-25% and FM-50% groups were not significantly different from the control group, indicating that a proper amount of fat simulant could replace the contribution of fat to the sensory quality of the product. As shown in fig. 9 (b), the FM-75% group showed a significant decrease in total score, especially in taste, texture and viscoelasticity, compared to the CK group, and the tissue structure of the product was significantly loose due to the significant decrease in backfat addition, and it was difficult to compensate for the effect of fat loss on the overall acceptability of the product even with fat mimetic substitution. In conclusion, the FM-50% group of emulsified sausage in this study not only has higher sensory scores, high viscoelasticity, mouthfeel, color, taste and flavor acceptance, but also has less fat content.
6. pH change during storage of low-fat emulsified sausage
As shown in fig. 10, the pH of the four groups of emulsion intestines tended to decrease during storage, but the pH of the three groups of emulsion intestines to which the fat mimetic was added all decreased at a lower rate than the CK group. As the shelf life of meat products continues to increase, the meat products may become rancid, causing the pH to decrease continuously. The addition of fat mimetics can improve the stability of pH during storage of the emulsified sausage compared to CK group.
7. Color difference value change during storage period of low-fat emulsified sausage
Fig. 11 shows the changes in color difference of the emulsified intestines of each group during storage, and the differences in L, a and b values between the experimental group and the control group are significant. Overall, the addition of fat mimetics increased the low fat emulsified sausage a x value, decreased the L x value (p < 0.05), thus also increased the hue and decreased whiteness. Thus, the addition of modified protein pre-emulsification to the low-fat emulsion sausage significantly changes its color difference, but not significantly over time.
8. Changes in TBARS values during storage in low fat emulsified intestines
As shown in fig. 12, the TBARS values of the emulsified intestines with the fat mimetics added were all significantly lower than those of the CK group at the same storage time of the emulsified intestines, probably because the reduction of the fat content resulted in the reduction of the unsaturated fatty acid content in the emulsified intestines, thereby impairing the degree of oxidation. Thus, the addition of fat mimetics can further improve the antioxidant properties of the emulsified bowel.
9. TVB-N value change in storage period of low-fat emulsified sausage
As shown in FIG. 13, the TVB-N values of the four groups of emulsified intestines were in an ascending trend with the storage time. While three groups of emulsified intestines using fat mimetics had lower TVB-N values than the CK group. The reduced TVB-N value may be due to the fact that phosphorylation can alter the structure of goose muscle fibril protein, reducing protein decomposition. The use of fat mimetics in combination with the TBARS results in inhibiting fat oxidation and protein degradation, extending the shelf life of the emulsified sausage and ensuring its quality during storage.
The above description is not intended to limit the invention, nor is the invention limited to the examples described above. Variations, modifications, additions, or substitutions will occur to those skilled in the art and are therefore within the spirit and scope of the invention.
Claims (9)
1. The goose muscle fibrillin modification process includes the following steps:
(1) Preparing a protein solution: dissolving goose muscle fibrillin in 0.02mol/L PBS solution to prepare a protein dispersion solution with the concentration of 10 mg/mL;
(2) Ultrasonic assisted phosphorylation modification: adding sodium tripolyphosphate into the protein dispersion solution prepared in the step (1) while stirring to make the final mass concentration of the solution be 1%, stirring for 30min, then performing ultrasonic treatment at 200-600W for 12min at 20kHz, keeping the water bath at a constant temperature of 45 ℃ for 48min, and then placing the solution into an ice bath for 30min;
(3) And (3) dialysis: adding the solution obtained in the step (2) into the dialysate, magnetically stirring, changing the dialysate every 2 hours, dialyzing for 12 hours, centrifuging for 15 minutes at 4 ℃ and 5100g, and removing supernatant;
(4) And (3) drying: and (3) performing a vacuum freeze drying method on the precipitate obtained in the step (3) to obtain the modified goose muscle fibril protein.
2. The method for modifying goose myofibrillar protein according to claim 1, wherein the step (1) of preparing the goose myofibrillar protein comprises the following steps:
(1) Thawing the split-packed goose meat at 4 ℃ for 12 hours, mincing with a meat mincer, adding 4 times of extracting solution by mass, homogenizing 60s with a high-speed disperser for 10 s/time in ice bath, centrifuging the sample at 12600g at 4 ℃ for 20min after homogenizing, and removing the supernatant, wherein the formula of the extracting solution is 0.1mol/L Tris, 10mmol/LEDTA, and the pH=8.3;
(2) Dispersing the precipitate obtained in step (1) in 4 times volume of standard salt solution, centrifuging at 12600g at 4deg.C for 10min to remove supernatant, and repeating the steps twice, wherein the standard salt solution has a formula of 0.1mol/LKCl and 0.02mol/L K 2 HPO 4 /KH 2 PO 4 、2mmol/L MgCl 2 、1mmol/L EGTA，pH7.0；
(3) Placing the precipitate obtained in the step (2) into 4 times of standard salt solution containing 1% TritonX-100, centrifuging 12600g for 10min to collect the precipitate, and repeating the step twice;
(4) Then uniformly dispersing the precipitate obtained in the step (3) in a standard salt solution with the volume of 4 times, centrifuging 12600g for 10min, collecting the precipitate, and repeating the step twice;
(5) Dissolving the precipitate obtained in the step (4) in 0.1mmol/L KCl solution with the volume of 4 times, centrifuging 12600g for 10min to collect the precipitate, and repeating the step twice;
(6) Filtering the precipitate obtained in the step (5) through three layers of gauze, adding 0.1mmol/LNaCl solution with the volume of 4 times, and centrifuging 12600g for 10min to obtain the precipitate, namely the purified goose muscle fibril protein.
3. The method for modifying goose myofibrillar protein according to claim 1, wherein the PBS solution in step (1) is formulated as follows: 0.02mol/L K 2 HPO 4 ，0.02mol/L KH 2 PO 4 ，0.6mol/L NaCl，pH＝7。
4. The method for modifying goose myofibrillar protein according to claim 1, wherein: the ultrasonic power in the step (2) is 400W.
5. The method for modifying goose myofibrillar protein according to claim 1, wherein: the dialysate in the step (3) is deionized water.
6. Use of a goose muscle fibrillin modified by the method of any one of claims 1-5 in the preparation of a fat mimetic.
7. The use of goose myofibrillar proteins according to claim 6 for the preparation of fat mimetics, characterized in that the preparation method of the fat mimetics comprises the following steps: after the modified goose muscle fibrillin powder is dissolved in water to adjust the concentration to 10mg/mL, adding sunflower oil with equal mass, homogenizing for 2min by a high-speed homogenizer at 10000rpm to obtain the fat mimics.
8. Use of goose myofibrillar proteins according to claim 7 in fat mimics, characterized in that: the fat mimics replace 25-75% of pig backfat by mass in goose meat emulsion sausage, wherein the mass ratio of goose meat to pig backfat in goose meat emulsion sausage before replacement is 4:1.
9. Use of goose myofibrillar proteins according to claim 8 in fat mimics, characterized in that: the fat mimics replace 50% of the pig backfat by mass in the goose meat emulsion sausage, wherein the mass ratio of the goose meat to the pig backfat in the goose meat emulsion sausage before replacement is 4:1.
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| CN202310364889.0A CN116473157A (en) | 2023-04-07 | 2023-04-07 | Goose muscle fibrillin modification method and application of goose muscle fibrillin modification method in preparation of fat mimics |
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| CN202310364889.0A CN116473157A (en) | 2023-04-07 | 2023-04-07 | Goose muscle fibrillin modification method and application of goose muscle fibrillin modification method in preparation of fat mimics |
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