CN109527192B - Method for enhancing gel property of fish myofibrillar protein product by inducing riboflavin oxidation based on UVA irradiation - Google Patents
Method for enhancing gel property of fish myofibrillar protein product by inducing riboflavin oxidation based on UVA irradiation Download PDFInfo
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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
- A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
- A23J1/04—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from fish or other sea animals
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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
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/04—Animal proteins
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- 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
- A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
- A23L29/03—Organic compounds
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- 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
- A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
- A23L29/20—Foods or foodstuffs containing additives; Preparation or treatment thereof containing gelling or thickening agents
- A23L29/275—Foods or foodstuffs containing additives; Preparation or treatment thereof containing gelling or thickening agents of animal origin, e.g. chitin
- A23L29/281—Proteins, e.g. gelatin or collagen
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- 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
- A23L5/00—Preparation or treatment of foods or foodstuffs, in general; Food or foodstuffs obtained thereby; Materials therefor
- A23L5/30—Physical treatment, e.g. electrical or magnetic means, wave energy or irradiation
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- 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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Abstract
The invention discloses a method for enhancing the gel property of a fish myofibrillar protein product by inducing riboflavin oxidation based on UVA irradiation. The method comprises the following steps: extracting myofibrillar protein from fish to prepare myofibrillar protein solution with the concentration of 35-100 mg/ml; adding riboflavin into the myofibrillar protein solution, and adding 0.5-300 nmol of riboflavin into each gram of myofibrillar protein to obtain a mixed solution; the obtained mixed solution is 0.8-2.0W/m below 4 DEG C 2 UVA irradiation for 0.1-3 h; heating for 5-30 min at 50-100 ℃; cooling for 1-6 h at 0-10 ℃; obtaining the fish myofibrillar protein product. The method provided by the invention is suitable for industrial production, and can effectively improve the characteristics of the fish myofibrillar protein product, thereby improving the quality of the fish myofibrillar protein product.
Description
Technical Field
The invention belongs to the technical field of deep processing of aquatic products, and particularly relates to a method for enhancing the gel property of a fish myofibrillar protein product based on UVA irradiation induced riboflavin oxidation.
Background
Fish sausage products (Fish food products) are used as one of main products for high-value processing of aquatic products, and have the problems of low price and insufficient freshness of production raw materials, poor meat quality and insufficient elasticity of the Fish sausage products caused by inherent protein characteristics of the raw materials and the like. This results in a large number of low value fishery resources that are not fully utilized and the commercial value of the fish sausage product is not high. Therefore, how to effectively improve the gelling property of myofibrillar proteins in fish meat is a focus problem in processing fish meat and fish intestine products.
At present, various food auxiliary materials and additives such as potato starch, soybean protein isolate, egg white protein, plasma protein and the like are added to improve the gel property of the fish sausage product, but the addition amount of the food auxiliary materials and the additives in fish meat is large, and the flavor of the product can be influenced.
The UVA band is a part of ultraviolet wavelength division, and the wavelength is 320-420 nm. It has strong penetrating power. The irradiation technique called "cold sterilization" is a new food processing technique developed in recent years. Riboflavin is a water-soluble B-group vitamin, a component of the human body's metabolic enzyme system, and is one of the essential vitamins in biological life activities, and has close relationship with the metabolism of carbohydrates, fats and amino acids in human body, and biologically, riboflavin has important functions, such as: phototropism, phototaxis and phototherapy, which is an important photosensitizer, rapidly generates free radicals when being irradiated by strong light, and generates about 80% of O when being irradiated by riboflavin for 30min 2～· And 20% of ～ O 2 . Riboflavin can damage biological macromolecules in the photosensitive degradation process of the riboflavin, and the damage process is considered to be that the light induces the riboflavin to release free radicals, and further causes the oxidative damage of the biological macromolecules such as protein, lipid, DNA and the like.
Disclosure of Invention
The invention aims to solve the problems of insufficient elasticity and the like in the processing process of fish intestine products, and provides a method for inducing riboflavin oxidation based on UVA irradiation so as to improve the gel property of myofibrillar protein products, further improve the gel strength of the fish intestine products and improve the quality of the fish intestine products.
In order to achieve the purpose, the invention adopts the following technical scheme:
a method for enhancing the gel properties of a fish myofibrillar protein preparation based on UVA irradiation induced riboflavin oxidation comprising the steps of:
s1, extracting myofibrillar protein: extracting myofibrillar protein from fish to prepare a myofibrillar protein solution;
s2, adding riboflavin: adding riboflavin (namely vitamin B2) into the myofibrillar protein solution obtained in the step S1 to obtain a mixed solution;
s3, UVA irradiation: carrying out UVA irradiation on the mixed solution obtained in the step S2, and refrigerating and standing;
s4, preparing a gel product: and (4) heating and cooling the product obtained in the step (S3) to obtain the fish myofibrillar protein product.
In a preferred aspect, the method for enhancing the gel properties of a fish myofibrillar protein product based on UVA irradiation induced riboflavin oxidation comprises the steps of:
s1, extracting myofibrillar protein: extracting myofibrillar protein from fish to prepare myofibrillar protein solution with the concentration of 35-100 mg/ml;
s2, adding riboflavin: adding riboflavin (namely vitamin B2) into the myofibrillar protein solution obtained in the step S1 to obtain a mixed solution; adding 0.5-300 nmol of riboflavin into each gram of myofibrillar protein based on the total amount of the myofibrillar protein in the myofibrillar protein solution;
s3, UVA irradiation: carrying out UVA irradiation on the mixed solution obtained in the step S2 at the temperature of below 4 ℃; standing at 4 ℃ for 12-20 h; wherein the UVA irradiation intensity is 0.8-2.0W/m 2 The irradiation time is 0.1 to 3 hours;
s4, preparing a gel product: heating the product obtained in the step S3 at 50-100 ℃ for 5-30 min; cooling for 1-6 h at 0-10 ℃; obtaining the fish myofibrillar protein product.
In a preferable mode, the fish meat in the step S1 is Spanish mackerel meat, tilapia meat or grass carp meat.
Preferably, the height of the mixed solution is 1mm to 15mm during the UVA irradiation in step S3.
In a most preferred form, the method for enhancing the gel properties of a fish myofibrillar protein product based on UVA irradiation induced riboflavin oxidation comprises the steps of:
s1, extracting myofibrillar protein: thawing frozen Spanish mackerel, removing head, tail and viscera, collecting meat in ice bath, extracting myofibrillar protein from fish meat, and preparing into myofibrillar protein solution with concentration of 50 mg/ml;
s2, adding riboflavin: adding riboflavin (namely vitamin B2) into the myofibrillar protein solution obtained in the step S1 to obtain a mixed solution; adding 80nmol riboflavin per gram of myofibrillar protein based on the total amount of myofibrillar protein in the myofibrillar protein solution;
s3, UVA irradiation: placing the mixed solution obtained in the step S2 in a culture dish for UVA irradiation, and placing for 16h at 4 ℃; wherein the intensity of UVA irradiation is 1.4W/m 2 The irradiation time is 0.3h, and the liquid level height of the mixed solution is 8mm;
s4, preparing a gel product: and (4) heating the product obtained in the step (S3) at 85 ℃ for 10min to gelatinize the product, immediately placing the gelatinized product at 4 ℃ for 1h to obtain the fish myofibrillar protein product.
Wherein, the myofibrillar protein extraction of the step S1 comprises the following steps:
s11: adding 50mM phosphate buffer solution with pH6.0 into fish meat according to the ratio of 1:3 (weight: volume, g/ml), homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain precipitate;
s12: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S11 according to the ratio of 1 (weight: volume, g/ml) of material to liquid, homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain the precipitate;
s13: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S12 according to the ratio of 1 to 3 (weight: volume, g/ml), homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain the precipitate;
s14: adding the precipitate obtained in the step S13 into 0.1M NaCl according to the ratio of 1 to 3 (weight: volume, g/ml), homogenizing at 8000rpm for 1min, and centrifuging at 8000g for 15min to obtain a precipitate;
s15: adding the precipitate obtained in the step S14 into 0.1M NaCl at 8000rpm according to the ratio of 1; diluting myofibrillar protein to 35-100 mg/mL by 25mM phosphate buffer (containing 0.6mol NaCl); wherein the protein concentration (i.e., myofibrillar protein concentration) is determined by the biuret method.
The invention has the beneficial effects that:
the method for enhancing the gel property of the fish myofibrillar protein product by inducing the oxidation of riboflavin based on UVA irradiation can effectively improve the gel property of the myofibrillar protein product and further effectively improve the gel strength of the fish myofibrillar protein product. Meanwhile, the physical UVA irradiation method is adopted, so that the product quality reduction caused by the addition of an exogenous preservative and a high-temperature sterilization method can be avoided, and the color, the original flavor and the nutrient content of the product can be better maintained. The gel strength of the fish myofibrillar protein product obtained by the method can be improved by 20-60 percent, the elasticity and the taste of the fish sausage product are obviously improved, the process is simple and easy to implement, and the industrial production is convenient.
The method for enhancing the gel property of the fish myofibrillar protein product based on UVA-induced riboflavin is obtained on the basis of repeated tests. Wherein, the irradiation intensity of UVA, the addition amount of riboflavin and the combination sequence of all the steps can directly influence the gel property of the myofibrillar protein product.
Drawings
FIG. 1 is a process flow diagram for enhancing the gel properties of a fish myofibrillar protein product based on UVA irradiation induced oxidation of riboflavin.
Detailed Description
The following detailed description of the present invention, taken in conjunction with the accompanying drawings and examples, is provided to enable the invention and its various aspects and advantages to be better understood. However, the specific embodiments and examples described below are for illustrative purposes only and are not limiting of the invention.
The invention provides a method for enhancing the gel property of a fish myofibrillar protein product based on UVA irradiation induced riboflavin oxidation. Wherein the preparation method comprises thawing frozen Spanish mackerel, collecting meat, and pulping. Then subpackaging and extracting myofibrillar protein, the extracted myofibrillar proteinDiluting to 35-100 mg/ml, adding 0.5-300 nmol/g protein, and mixing. Placing the myofibrillar protein solution in a culture dish, and carrying out UVA irradiation for 0.1 to 3 hours with the irradiation intensity of 0.8 to 2.0W/m 2 . Refrigerating and standing to obtain fish myofibrillar protein product with diameter of 15mm; and (3) heating by adopting a one-stage water bath, and controlling the heating time and temperature. Cooling and balancing to obtain the myofibrillar protein gel product with satisfactory gel characteristics.
In one embodiment, the riboflavin solution has a concentration of 0.5 to 300nmol/g protein.
In one embodiment, the method comprises pre-treating raw materials, thawing frozen Spanish mackerel, removing head and tail, removing viscera, collecting meat, and packaging.
In one embodiment, the aliquot of fish homogenate is centrifuged to extract myofibrillar proteins to a concentration of 35 to 100mg/ml.
In one embodiment, the fish flesh is subjected to UVA irradiation for 0.1 to 3 hours, and the irradiation process is carried out at the temperature of less than 4 ℃.
In one embodiment, the fish meat is allowed to stand at 4 ℃ for 12 to 20 hours.
In one embodiment, the prepared fish myofibril gel product has a diameter of 15mm.
In one embodiment, the fish myofibril protein product is prepared and then heated in a water bath at 50-100 ℃ for 5-30 min.
In one embodiment, the heat-treated sample is cooled for 1 to 6 hours at 0 to 10 ℃ and subjected to gel strength detection.
In one embodiment, the gel strength measurement is performed by directly measuring the breaking force and breaking distance of the equilibrated fish myofibrillar protein product using a ta.xt. The measurement conditions were as follows: a P5s spherical probe with the diameter of 5mm, the test speed of 1mm/s and the displacement of 10mm. Gel strength (g · cm) = breaking force (g) × breaking distance (cm).
Example 1
A method for enhancing the gel properties of a fish myofibrillar protein product based on UVA irradiation induced riboflavin oxidation comprising the steps of:
s1, extracting myofibrillar protein: thawing frozen fresh Spanish mackerel, removing head, tail and viscera, collecting meat in ice bath, extracting myofibrillar protein from fish meat, and preparing into myofibrillar protein solution with concentration of 35 mg/ml;
s2, adding riboflavin: adding riboflavin (namely vitamin B2) into the myofibrillar protein solution obtained in the step S1 to obtain a mixed solution; adding 300nmol riboflavin per gram of myofibrillar protein based on the total amount of myofibrillar protein in the myofibrillar protein solution;
s3, UVA irradiation: carrying out UVA irradiation on the mixed solution obtained in the step S2, wherein the liquid level height of the mixed solution is 1mm; standing at 4 ℃ for 20h; wherein the intensity of UVA irradiation is 2.0W/m 2 And the irradiation time is 3h;
s4, preparing a gel product: heating the product obtained in the step S3 at 100 ℃ for 30min to gelatinize the product, immediately placing the gelatinized product in a 0 ℃ for storage for 6h to obtain a fish myofibrillar protein product;
wherein the extracting of myofibrillar proteins in the step S1 comprises the steps of:
s11: adding 50mM phosphate buffer solution with pH6.0 into fish meat according to the ratio of 1:3 (weight: volume, g/ml), homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain precipitate;
s12: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S11 according to the ratio of 1 (weight: volume, g/ml) of material to liquid, homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain the precipitate;
s13: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S12 according to the ratio of 1 (weight: volume, g/ml) of material to liquid, homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain precipitate;
s14: adding the precipitate obtained in the step S13 into 0.1M NaCl according to the ratio of 1 to 1 (weight: volume, g/ml), homogenizing at 8000rpm for 1min, and centrifuging at 8000g for 15min to obtain a precipitate;
s15: and (3) adding the precipitate obtained in the step (S14) into 0.1M NaCl according to the ratio of the material to the liquid of 1:3 (weight: volume, g/mL), homogenizing for 1min at 8000rpm, sieving by two layers of 80-mesh gauze, centrifuging to obtain a precipitate, namely myofibrillar protein, and diluting the myofibrillar protein to 35mg/mL by using 25mM phosphate buffer (containing 0.6mol of NaCl).
The fish myofibrillar protein product obtained in the example was tested for gel strength, and the breaking distance of the fish myofibrillar protein product was 4.231g, and the gel strength was 18.735g cm. Compared with the comparative example 1, the gel strength of the myofibrillar protein product obtained by adding the riboflavin and irradiating by the UVA can be improved by 41.31 percent.
Example 2
A method for enhancing the gel properties of a fish myofibrillar protein preparation based on UVA irradiation induced riboflavin oxidation comprising the steps of:
s1, extracting myofibrillar protein: thawing iced grass carp, removing head, tail and viscera, and collecting meat in ice bath; extracting myofibrillar protein from fish meat to prepare a myofibrillar protein solution with the concentration of 40 mg/ml;
s2, adding riboflavin: adding riboflavin (namely vitamin B2) into the myofibrillar protein solution obtained in the step S1 to obtain a mixed solution; adding 20nmol riboflavin per gram of myofibrillar protein based on the total amount of myofibrillar protein in the myofibrillar protein solution;
s3, UVA irradiation: placing the mixed solution obtained in the step S2 in a culture dish for UVA irradiation, wherein the liquid level height of the mixed solution is 2mm, and placing for 16h at 4 ℃; wherein the intensity of UVA irradiation is 1.0W/m 2 And the irradiation time is 2h;
s4, preparing a gel product: and (4) heating the product obtained in the step (S3) at 95 ℃ for 15min to gelatinize the product, immediately placing the gelatinized product into a place at 2 ℃ for storage for 4h, and obtaining the fish myofibrillar protein product.
Wherein the extracting of myofibrillar proteins in the step S1 comprises the steps of:
s11: adding 50mM phosphate buffer solution with pH6.0 into fish meat according to the ratio of 1:3 (weight: volume, g/ml), homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain precipitate;
s12: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S11 according to the ratio of 1 (weight: volume, g/ml) of material to liquid, homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain the precipitate;
s13: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S12 according to the ratio of 1 to 3 (weight: volume, g/ml), homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain the precipitate;
s14: adding the precipitate obtained in the step S13 into 0.1M NaCl according to the ratio of 1 to 3 (weight: volume, g/ml), homogenizing at 8000rpm for 1min, and centrifuging at 8000g for 15min to obtain a precipitate;
s15: and (3) adding the precipitate obtained in the step (S14) into 0.1M NaCl according to the ratio of the material to the liquid of 1:3 (weight: volume, g/mL), homogenizing for 1min at 8000rpm, sieving by two layers of 80-mesh gauze, centrifuging to obtain a precipitate, namely myofibrillar protein, and diluting the myofibrillar protein to 40mg/mL by using 25mM phosphate buffer (containing 0.6mol of NaCl).
The fish myofibrillar protein product obtained in the example was tested for gel strength, and the breaking distance of the fish myofibrillar protein product was 4.053g, and the gel strength was 20.357 g-cm. Compared with the comparative example 2, the gel strength of the myofibrillar protein product added with the riboflavin and irradiated by the UVA can be improved by 23.89%. Compared with the comparative example 6, the gel strength of the protein product obtained in the embodiment can be improved by 33.46%.
Example 3
A method for enhancing the gel properties of a fish myofibrillar protein product based on UVA irradiation induced riboflavin oxidation comprising the steps of:
s1, extracting myofibrillar protein: thawing frozen fresh tilapia, removing heads, tails and viscera, collecting meat in ice bath, extracting myofibrillar protein from fish meat, and preparing into a myofibrillar protein solution with the concentration of 45 mg/ml;
s2, adding riboflavin: adding riboflavin (namely vitamin B2) into the myofibrillar protein solution obtained in the step S1 to obtain a mixed solution; adding 25nmol riboflavin per gram myofibrillar protein based on the total amount of myofibrillar protein in the myofibrillar protein solution;
s3, UVA irradiation: carrying out UVA irradiation on the mixed solution obtained in the step S2, wherein the liquid level height of the mixed solution is 4mm, and standing for 18h at 4 ℃; wherein the intensity of UVA irradiation is 1.2W/m 2 The irradiation time is 1.5h;
s4, preparing a gel product: and (4) heating the product obtained in the step (S3) at 90 ℃ for 5min to gelatinize the product, and immediately placing the gelatinized product in a temperature range of 10 ℃ for 3h to obtain the fish myofibrillar protein product.
Wherein the extracting of myofibrillar proteins in the step S1 comprises the steps of:
s11: adding 50mM phosphate buffer solution with pH6.0 into fish meat according to the ratio of 1:3 (weight: volume, g/ml), homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain precipitate;
s12: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S11 according to the ratio of 1 (weight: volume, g/ml) of material to liquid, homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain the precipitate;
s13: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S12 according to the ratio of 1 (weight: volume, g/ml) of material to liquid, homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain precipitate;
s14: adding the precipitate obtained in the step S13 into 0.1M NaCl according to the ratio of 1 to 1 (weight: volume, g/ml), homogenizing at 8000rpm for 1min, and centrifuging at 8000g for 15min to obtain a precipitate;
s15: and (3) adding the precipitate obtained in the step (S14) into 0.1M NaCl according to the ratio of the material to the liquid of 1:3 (weight: volume, g/mL), homogenizing for 1min at 8000rpm, sieving by two layers of 80-mesh gauze, centrifuging to obtain a precipitate, namely myofibrillar protein, and diluting the myofibrillar protein to 45mg/mL by using 25mM phosphate buffer (containing 0.6mol of NaCl).
The fish myofibrillar protein product obtained in the example was tested for gel strength, and the breaking distance of the fish myofibrillar protein product was 7.243g, and the gel strength was 35.892g cm. Compared with the comparative example 3, the gel strength of the myofibrillar protein product obtained by the embodiment can be improved by 36.36 percent.
Example 4
A method for enhancing the gel properties of a fish myofibrillar protein preparation based on UVA irradiation induced riboflavin oxidation comprising the steps of:
s1, extracting myofibrillar protein: thawing frozen Spanish mackerel, removing head, tail and viscera, collecting meat in ice bath, extracting myofibrillar protein from fish meat, and preparing into myofibrillar protein solution with concentration of 50 mg/ml;
s2, adding riboflavin: adding riboflavin (namely vitamin B2) into the myofibrillar protein solution obtained in the step S1 to obtain a mixed solution; adding 80nmol riboflavin per gram of myofibrillar protein based on the total amount of myofibrillar protein in the myofibrillar protein solution;
s3, UVA irradiation: placing the mixed solution obtained in the step S2 in a culture dish for UVA irradiation, wherein the liquid level height of the mixed solution is 8mm, and placing for 16h at 4 ℃; wherein the intensity of UVA irradiation is 1.4W/m 2 The irradiation time is 0.3h;
s4, preparing a gel product: heating the product obtained in the step S3 at 85 ℃ for 10min to gelatinize the product, immediately placing the product at 4 ℃ for 1h to obtain the fish myofibrillar protein product.
Wherein the extraction of myofibrillar proteins in the step S1 comprises the following steps:
s11: adding 50mM phosphate buffer solution with the pH value of 6.0 into fish meat according to the ratio of 1 to 3 (weight: volume, g/ml), homogenizing at 8000rpm for 2min, centrifuging at 8000g for 15min, and taking a precipitate;
s12: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S11 according to the ratio of 1 (weight: volume, g/ml) of material to liquid, homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain the precipitate;
s13: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S12 according to the ratio of 1 to 3 (weight: volume, g/ml), homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain the precipitate;
s14: adding the precipitate obtained in the step S13 into 0.1M NaCl according to the ratio of 1 to 1 (weight: volume, g/ml), homogenizing at 8000rpm for 1min, and centrifuging at 8000g for 15min to obtain a precipitate;
s15: and (3) adding the precipitate obtained in the step (S14) into 0.1M NaCl according to the ratio of the material to the liquid of 1:3 (weight: volume, g/mL), homogenizing for 1min at 8000rpm, sieving by two layers of 80-mesh gauze, centrifuging to obtain a precipitate, namely myofibrillar protein, and diluting the myofibrillar protein to 50mg/mL by using 25mM phosphate buffer (containing 0.6mol of NaCl).
The fish myofibrillar protein product obtained in the example was tested for gel strength, and the breaking distance of the fish myofibrillar protein product was 10.369g, and the gel strength was 50.263 g-cm. Compared with the comparative example 4, the gel strength of the myofibrillar protein product obtained in the embodiment can be improved by 53.94%.
Example 5
A method for enhancing the gel properties of a fish myofibrillar protein product based on UVA irradiation induced riboflavin oxidation comprising the steps of:
s1, extracting myofibrillar protein: thawing frozen fresh Spanish mackerel, removing head, tail and viscera, collecting meat in ice bath, extracting myofibrillar protein from fish meat, and preparing into myofibrillar protein solution with concentration of 100mg/ml;
s2, adding riboflavin: adding riboflavin (namely vitamin B2) into the myofibrillar protein solution obtained in the step S1 to obtain a mixed solution; adding 0.5nmol riboflavin per gram of myofibrillar protein based on the total amount of myofibrillar protein in the myofibrillar protein solution;
s3, UVA irradiation: carrying out UVA irradiation on the mixed solution obtained in the step S2, wherein the liquid level height of the mixed solution is 15mm, and standing at 4 ℃ for 12h; wherein the intensity of UVA irradiation is 0.8W/m 2 The irradiation time is 0.1h;
s4, preparing a gel product: and (4) heating the product obtained in the step (S3) at 50 ℃ for 20min to gelatinize the product, immediately putting the gelatinized product into ice at 5 ℃ and storing the gelatinized product for 2h to obtain the fish myofibrillar protein product.
Wherein the extraction of myofibrillar proteins in the step S1 comprises the following steps:
s11: adding 50mM phosphate buffer solution with pH6.0 into fish meat according to the ratio of 1:3 (weight: volume, g/ml), homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain precipitate;
s12: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S11 according to the ratio of 1 (weight: volume, g/ml) of material to liquid, homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain the precipitate;
s13: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S12 according to the ratio of 1 to 3 (weight: volume, g/ml), homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain the precipitate;
s14: adding the precipitate obtained in the step S13 into 0.1M NaCl according to the ratio of 1 to 3 (weight: volume, g/ml), homogenizing at 8000rpm for 1min, and centrifuging at 8000g for 15min to obtain a precipitate;
s15: and (3) adding 0.1M NaCl in the precipitate obtained in the step (S14) according to the ratio of 1 to 3 (weight: volume, g/mL) into the precipitate, homogenizing the mixture for 1min at 8000rpm, passing the mixture through two 80-mesh gauzes, centrifuging the mixture to obtain a precipitate, namely myofibrillar protein, and diluting the myofibrillar protein to 100mg/mL by using 25mM phosphate buffer solution (containing 0.6mol of NaCl).
The fish myofibrillar protein product obtained in the example was subjected to gel strength test, and the breaking distance of the fish myofibrillar protein product was 9.871g, and the gel strength was 46.735g cm. Compared with the comparative example 5, the gel strength of the myofibrillar protein product obtained by the embodiment can be improved by 36.45 percent.
Comparative example 1:
a method for enhancing the gel properties of a fish myofibrillar protein preparation based on UVA irradiation induced riboflavin oxidation comprising the steps of:
s1, extracting myofibrillar protein: thawing frozen Spanish mackerel, removing head, tail and viscera, collecting meat in ice bath, extracting myofibrillar protein from fish meat, and preparing into myofibrillar protein solution with concentration of 35 mg/ml;
s2, UVA irradiation: carrying out UVA irradiation on the myofibrillar protein solution obtained in the step S1, wherein the liquid level height of the mixed solution is 1mm, and standing for 20h at 4 ℃; wherein the intensity of UVA irradiation is 2.0W/m 2 And the irradiation time is 3h;
s3, preparing a gel product: heating the product obtained in the step S2 at 100 ℃ for 30min to gelatinize the product, immediately placing the product in a temperature of 0 ℃ for storage for 6h to obtain the fish myofibrillar protein product.
Wherein the extracting of myofibrillar proteins in the step S1 comprises the steps of:
s11: adding 50mM phosphate buffer solution with pH6.0 into fish meat according to the ratio of 1:3 (weight: volume, g/ml), homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain precipitate;
s12: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S11 according to the ratio of 1 (weight: volume, g/ml) of material to liquid, homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain the precipitate;
s13: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S12 according to the ratio of 1 (weight: volume, g/ml) of material to liquid, homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain precipitate;
s14: adding the precipitate obtained in the step S13 into 0.1M NaCl according to the ratio of 1 to 1 (weight: volume, g/ml), homogenizing at 8000rpm for 1min, and centrifuging at 8000g for 15min to obtain a precipitate;
s15: and (3) adding the precipitate obtained in the step (S14) into 0.1M NaCl according to the ratio of the material to the liquid of 1:3 (weight: volume, g/mL), homogenizing for 1min at 8000rpm, sieving by two layers of 80-mesh gauze, centrifuging to obtain a precipitate, namely myofibrillar protein, and diluting the myofibrillar protein to 35mg/mL by using 25mM phosphate buffer (containing 0.6mol of NaCl).
The fish myofibrillar protein product obtained in this example was tested for gel strength, and the breaking distance of the fish myofibrillar protein product was 3.013g, and the gel strength was 13.258 g/cm.
Comparative example 2:
a method for enhancing the gel properties of a fish myofibrillar protein product based on UVA irradiation induced riboflavin oxidation comprising the steps of:
s1, extracting myofibrillar protein: thawing iced grass carp, removing head, tail and viscera, collecting meat in ice bath, extracting myofibrillar protein from fish meat, and preparing into 40mg/ml myofibrillar protein solution;
s2, UVA irradiation: placing the myofibrillar protein solution obtained in the step S1 in a culture dish for UVA irradiationThe liquid level of the mixed solution is 2mm, and the mixed solution is placed for 16h at 4 ℃; wherein the intensity of UVA irradiation is 1.0W/m 2 And the irradiation time is 2h;
s3, preparing a gel product: and (3) heating the product obtained in the step (S2) at 95 ℃ for 15min to gelatinize the product, immediately placing the gelatinized product in a place at 2 ℃ for storage for 4h to obtain the fish myofibrillar protein product.
Wherein the extracting of myofibrillar proteins in the step S1 comprises the steps of:
s11: adding 50mM phosphate buffer solution with the pH value of 6.0 into fish meat according to the ratio of 1 to 3 (weight: volume, g/ml), homogenizing at 8000rpm for 2min, centrifuging at 8000g for 15min, and taking a precipitate;
s12: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S11 according to the ratio of 1 (weight: volume, g/ml) of material to liquid, homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain the precipitate;
s13: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S12 according to the ratio of 1 to 3 (weight: volume, g/ml), homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain the precipitate;
s14: adding the precipitate obtained in the step S13 into 0.1M NaCl according to the ratio of 1 to 3 (weight: volume, g/ml), homogenizing at 8000rpm for 1min, and centrifuging at 8000g for 15min to obtain a precipitate;
s15: and (3) adding the precipitate obtained in the step (S14) into 0.1M NaCl according to the ratio of the material to the liquid of 1:3 (weight: volume, g/mL), homogenizing for 1min at 8000rpm, sieving by two layers of 80-mesh gauze, centrifuging to obtain a precipitate, namely myofibrillar protein, and diluting the myofibrillar protein to 40mg/mL by using 25mM phosphate buffer (containing 0.6mol of NaCl).
The fish myofibrillar protein product obtained in the example was tested for gel strength, and the breaking distance of the fish myofibrillar protein product was 3.758g, and the gel strength was 16.432g cm.
Comparative example 3
A method for enhancing the gel properties of a fish myofibrillar protein product based on UVA irradiation induced riboflavin oxidation comprising the steps of:
s1, extracting myofibrillar protein: thawing frozen fresh tilapia, removing heads, tails and viscera, collecting meat in ice bath, extracting myofibrillar protein from fish meat, and preparing into a myofibrillar protein solution with the concentration of 45 mg/ml;
s2, adding riboflavin: adding riboflavin (namely vitamin B2) into the myofibrillar protein solution obtained in the step S1 to obtain a mixed solution, and standing at 4 ℃ for 18h; adding 25nmol riboflavin per gram myofibrillar protein based on the total amount of myofibrillar protein in the myofibrillar protein solution;
s3, preparing a gel product: heating the product obtained in the step S2 at 90 ℃ for 5min to gelatinize the product, and immediately placing the gelatinized product in 10 ℃ for 3h to obtain the fish myofibrillar protein product.
Wherein the extraction of myofibrillar proteins in the step S1 comprises the following steps:
s11: adding 50mM phosphate buffer solution with the pH value of 6.0 into fish meat according to the ratio of 1 to 3 (weight: volume, g/ml), homogenizing at 8000rpm for 2min, centrifuging at 8000g for 15min, and taking a precipitate;
s12: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S11 according to the ratio of 1 (weight: volume, g/ml) of material to liquid, homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain the precipitate;
s13: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S12 according to the ratio of 1 to 3 (weight: volume, g/ml), homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain the precipitate;
s14: adding the precipitate obtained in the step S13 into 0.1M NaCl according to the ratio of 1 to 1 (weight: volume, g/ml), homogenizing at 8000rpm for 1min, and centrifuging at 8000g for 15min to obtain a precipitate;
s15: and (3) adding the precipitate obtained in the step (S14) into 0.1M NaCl according to the ratio of the material to the liquid of 1:3 (weight: volume, g/mL), homogenizing for 1min at 8000rpm, sieving by two layers of 80-mesh gauze, centrifuging to obtain a precipitate, namely myofibrillar protein, and diluting the myofibrillar protein to 45mg/mL by using 25mM phosphate buffer (containing 0.6mol of NaCl).
The fish myofibrillar protein product obtained in the example was tested for gel strength, and the breaking distance of the fish myofibrillar protein product was 5.693g, and the gel strength was 26.321g cm.
Comparative example 4:
a method for enhancing the gel properties of a fish myofibrillar protein preparation based on UVA irradiation induced riboflavin oxidation comprising the steps of:
s1, extracting myofibrillar protein: thawing frozen fresh Spanish mackerel, removing head, tail and viscera, collecting meat in ice bath, extracting myofibrillar protein from fish meat, and preparing into myofibrillar protein solution with concentration of 50 mg/ml;
s2, adding riboflavin: adding riboflavin (namely vitamin B2) into the myofibrillar protein solution obtained in the step S1 to obtain a mixed solution, and standing at 4 ℃ for 16h; adding 80nmol riboflavin per gram of myofibrillar protein based on the total amount of myofibrillar protein in the myofibrillar protein solution;
s3, preparing a gel product: heating the product obtained in the step S2 at 85 ℃ for 10min to gelatinize the product, immediately placing the product at 4 ℃ for 1h to obtain the fish myofibrillar protein product.
Wherein the extracting of myofibrillar proteins in the step S1 comprises the steps of:
s11: adding 50mM phosphate buffer solution with pH6.0 into fish meat according to the ratio of 1:3 (weight: volume, g/ml), homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain precipitate;
s12: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S11 according to the ratio of 1 (weight: volume, g/ml) of material to liquid, homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain the precipitate;
s13: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S12 according to the ratio of 1 (weight: volume, g/ml) of material to liquid, homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain precipitate;
s14: adding the precipitate obtained in the step S13 into 0.1M NaCl according to the ratio of 1 to 1 (weight: volume, g/ml), homogenizing at 8000rpm for 1min, and centrifuging at 8000g for 15min to obtain a precipitate;
s15: and (3) adding the precipitate obtained in the step (S14) into 0.1M NaCl according to the ratio of the material to the liquid of 1:3 (weight: volume, g/mL), homogenizing for 1min at 8000rpm, sieving by two layers of 80-mesh gauze, centrifuging to obtain a precipitate, namely myofibrillar protein, and diluting the myofibrillar protein to 50mg/mL by using 25mM phosphate buffer (containing 0.6mol of NaCl).
The fish myofibrillar protein product obtained in the example was subjected to gel strength test, and the breaking distance of the fish myofibrillar protein product was 6.272g, and the gel strength was 32.652g cm.
Comparative example 5:
a method for enhancing the gel properties of a fish myofibrillar protein preparation based on UVA irradiation induced riboflavin oxidation comprising the steps of:
s1, extracting myofibrillar protein: thawing frozen fresh Spanish mackerel, removing head, tail and viscera, collecting meat in ice bath, extracting myofibrillar protein from fish meat, and preparing into myofibrillar protein solution with concentration of 100mg/ml;
s2, adding riboflavin: adding riboflavin (namely vitamin B2) into the myofibrillar protein solution obtained in the step S1 to obtain a mixed solution, and standing at 4 ℃ for 12 hours; adding 0.5nmol riboflavin per gram of myofibrillar protein based on the total amount of myofibrillar protein in the myofibrillar protein solution;
s3, preparing a gel product: and (3) heating the product obtained in the step (S2) at 50 ℃ for 20min to gelatinize the product, immediately putting the gelatinized product into ice at 5 ℃ for storage for 2h, and obtaining the fish myofibrillar protein product.
Wherein the extraction of myofibrillar proteins in the step S1 comprises the following steps:
s11: adding 50mM phosphate buffer solution with pH6.0 into fish meat according to the ratio of 1:3 (weight: volume, g/ml), homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain precipitate;
s12: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S11 according to the ratio of 1 (weight: volume, g/ml) of material to liquid, homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain the precipitate;
s13: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S12 according to the ratio of 1 (weight: volume, g/ml) of material to liquid, homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain precipitate;
s14: adding the precipitate obtained in the step S13 into 0.1M NaCl according to the ratio of 1 to 1 (weight: volume, g/ml), homogenizing at 8000rpm for 1min, and centrifuging at 8000g for 15min to obtain a precipitate;
s15: and (3) adding the precipitate obtained in the step (S14) into 0.1M NaCl according to the ratio of the material to the liquid of 1:3 (weight: volume, g/mL), homogenizing for 1min at 8000rpm, sieving by two layers of 80-mesh gauze, centrifuging to obtain a precipitate, namely myofibrillar protein, and diluting the myofibrillar protein to 100mg/mL by using 25mM phosphate buffer (containing 0.6mol of NaCl).
The fish myofibrillar protein product obtained in the example was tested for gel strength, and the breaking distance of the fish myofibrillar protein product was 6.578g, and the gel strength was 34.251 g-cm.
Comparative example 6:
a method for enhancing the gel properties of a fish myofibrillar protein preparation based on UVA irradiation induced riboflavin oxidation comprising the steps of:
s1, extracting myofibrillar protein: thawing iced grass carp, removing head, tail and viscera, collecting meat in ice bath, extracting myofibrillar protein from fish meat, and preparing into 40mg/ml myofibrillar protein solution;
s2, preparing a gel product: and (2) standing the product obtained in the step (S1) at 4 ℃ for 16h, heating at 95 ℃ for 15min to gelatinize the product, immediately placing the gelatinized product in a storage tank at 2 ℃ for 4h, and obtaining the fish myofibrillar protein product.
Wherein the extraction of myofibrillar proteins in the step S1 comprises the following steps:
s11: adding 50mM phosphate buffer solution with pH6.0 into fish meat according to the ratio of 1:3 (weight: volume, g/ml), homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain precipitate;
s12: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S11 according to the ratio of 1 (weight: volume, g/ml) of material to liquid, homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain the precipitate;
s13: adding 50mM phosphate buffer solution with pH6.0 into the precipitate obtained in the step S12 according to the ratio of 1 (weight: volume, g/ml) of material to liquid, homogenizing at 8000rpm for 2min, and centrifuging at 8000g for 15min to obtain precipitate;
s14: adding the precipitate obtained in the step S13 into 0.1M NaCl according to the ratio of 1 to 1 (weight: volume, g/ml), homogenizing at 8000rpm for 1min, and centrifuging at 8000g for 15min to obtain a precipitate;
s15: and (3) adding the precipitate obtained in the step (S14) into 0.1M NaCl according to the ratio of the material to the liquid of 1:3 (weight: volume, g/mL), homogenizing for 1min at 8000rpm, sieving by two layers of 80-mesh gauze, centrifuging to obtain a precipitate, namely myofibrillar protein, and diluting the myofibrillar protein to 40mg/mL by using 25mM phosphate buffer (containing 0.6mol of NaCl).
The fish myofibrillar protein product obtained in the example was tested for gel strength, and the breaking distance of the fish myofibrillar protein product was 3.435g, and the gel strength was 15.253g cm.
Comparing the examples with the comparative examples, the results are given in the following table:
TABLE 1 gel Properties of myofibrillar protein preparations
Finally, it should be noted that: it should be understood that the above examples are only for clearly illustrating the present invention and are not intended to limit the embodiments. Other variations and modifications will be apparent to persons skilled in the art in light of the above description. This need not be, nor should it be exhaustive of all embodiments. And obvious variations or modifications of the invention may be made without departing from the scope of the invention.
The above description is only for the preferred embodiment of the present invention, but the scope of the present invention is not limited thereto, and any person skilled in the art should be able to cover the technical solutions and the inventive concepts of the present invention within the technical scope of the present invention.
Claims (3)
1. A method for enhancing the gel properties of a fish myofibrillar protein product based on UVA irradiation induced riboflavin oxidation comprising the steps of:
s1, extracting myofibrillar protein: extracting myofibrillar protein from fish meat to prepare a myofibrillar protein solution with the concentration of 35 to 100mg/ml;
s2, adding riboflavin: adding riboflavin into the myofibrillar protein solution obtained in the step S1 to obtain a mixed solution; adding 0.5 to 300nmol of riboflavin into each gram of myofibrillar protein based on the total amount of the myofibrillar protein in the myofibrillar protein solution;
s3, UVA irradiation: carrying out UVA irradiation on the mixed solution obtained in the step S2 at the temperature of below 4 ℃, wherein the height of the mixed solution is 1mm to 15mm; refrigerating at 4 ℃ for 12 to 20h; wherein the UVA irradiation intensity is 0.8 to 2.0W/m 2 And the irradiation time is 0.1 to 3h;
s4, preparing a gel product: heating the product obtained in the step S3 at 50-100 ℃ for 5-30min; cooling for 1 to 6 hours at 0 to 10 ℃; obtaining the fish myofibrillar protein product.
2. The method for enhancing the gel property of the fish myofibrillar protein product based on the induction of the oxidation of riboflavin by the UVA irradiation according to the claim 1, characterized in that the fish meat in the step S1 is Spanish mackerel meat, tilapia mossambica meat or grass carp meat.
3. The method for enhancing the gel properties of a fish myofibrillar protein product based on UVA irradiation induced riboflavin oxidation according to claim 2 comprising the steps of:
s1, extracting myofibrillar protein: extracting myofibrillar protein from mackerel meat to prepare a myofibrillar protein solution with the concentration of 50 mg/ml;
s2, adding riboflavin: adding riboflavin into the myofibrillar protein solution obtained in the step S1 to obtain a mixed solution; adding 80nmol riboflavin per gram myofibrillar protein based on the total amount of myofibrillar protein in the myofibrillar protein solution;
s3, UVA irradiation: placing the mixed solution obtained in the step S2 in a culture dish for UVA irradiation, and placing for 16h at 4 ℃; wherein the intensity of UVA irradiation is highThe degree is 1.4W/m 2 The irradiation time is 0.3h, and the liquid level height of the mixed solution is 8mm;
s4, preparing a gel product: heating the product obtained in the step S3 at 85 ℃ for 10min; standing at 4 deg.C for 1h to obtain fish myofibrillar protein product.
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