CN113907175A - Method for reducing heat loss of essential amino acid of myofibrillar protein - Google Patents
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- A—HUMAN NECESSITIES
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
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- A—HUMAN NECESSITIES
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Abstract
The invention discloses a method for reducing heat loss of essential amino acid of myofibrillar protein, which utilizes the interaction of nano cellulose molecules, myofibrillar protein molecules and amino acid residues thereof to reduce the damage degree of the spatial structure of the myofibrillar protein after being heated and reduce the exposure of the amino acid residues buried in the myofibrillar protein, thereby reducing the heat loss of the essential amino acid of the myofibrillar protein in the heating process and improving the quality of heat-treated meat products.
Description
Technical Field
The invention belongs to the field of meat product thermal processing, and particularly relates to a method for reducing heat loss of essential amino acid of myofibrillar protein.
Background
The hot processed meat products are classified into high-temperature meat products, low-temperature meat products and the like which require a heat treatment process. Heat treatment has a great influence on the nutrition, flavor, color and the like of meat, and also can cause protein denaturation, thereby influencing the quality of meat products. Myofibrillar Protein (MP) is the highest protein content in meat, and is closely related to the quality and nutritional value of meat products, and mainly includes tropomyosin, myosin, troponin, actomyosin, and the like. The heating can cause the desulfurization and CO removal of protein amino acid2And the like, and excessive heating causes them to lose essential amino acids and a large amount of vitamins and minerals, thereby reducing the nutritional value of the protein. Energy destruction of amino acids [ J ] in protein feed]Thermal energy destruction of amino acids in protein feed was studied, showing that heat treatment of protein feed ingredients results in destruction of some amino acids to form products that are not utilized by animals.
Therefore, it is important to improve the quality of the meat products after heat treatment, especially to maintain the nutritional value of the meat products. The heat stability of proteins has been studied in a number of related documents and patents, and dianthus superbus et al (CN201710237756.1) have provided a method for improving the heat stability of multimeric proteins by linking the subunits of multimeric proteins to form a ring-closed whole by introducing covalent bonds between the N-terminal and internal subunit contact interfaces of multimeric proteins. Lespanic et al (CN201911107914.7) propose a method for improving bovine serum albumin heat stability, wherein bovine serum albumin is dissolved in a buffer solvent to prepare a protein solution with a certain concentration, and phytic acid is added to improve the bovine serum albumin stability. The invention relates to a method for improving the heat stability of lactoferrin, which is invented in Jinghua et al (CN202011475507.4), and is characterized in that lactoferrin is dialyzed in an acid buffer solution to prepare the iron-free lactoferrin, and then an iron-nitrogen-based triethyl acid solution is added into the iron-free lactoferrin to prepare the lactoferrin with high heat stability and high iron saturation. Wuchao et al (CN202110243415.1) invented a method for improving the thermal stability of soybean protein by combining preheating and ultrasound, and the prepared thermal stability soybean protein can be widely applied to protein-containing beverages, which not only increases the protein content, but also improves the stability of related products in the thermal processing process. The above studies all relate to the improvement of protein heat stability, but no influence on amino acids in the protein is reported, and the effect on the improvement of the nutritional quality of the heat-processed protein is not clear. There is a clear literature on preventing the destruction of amino acids, particularly essential amino acids, in proteins by heat treatment with nanocellulose, and further improving the nutritional value of proteins.
Cellulose is the most widely distributed polysaccharide molecule, consisting of β -1,4 linked pyranose units, with unique physical and chemical properties. The nano-cellulose is a novel high molecular functional material, has a unique structure and excellent performance, and has more and more attention paid to the excellent performances of a three-dimensional nano-net structure, biocompatibility, mechanical stability, antibacterial property and the like. Protein-sugar interactions, such as covalent bonds, hydrogen bonds, van der waals forces, hydrophobic interactions, and molecular cross-linking, have a considerable impact on protein properties. At present, the research and the patent that nano-cellulose is added into myofibrillar protein to improve the heat dispersibility of the myofibrillar protein and reduce the heat loss of amino acid are not reported. The object of the present application is to create a method for reducing the heat loss of myofibrillar amino acids, in particular essential amino acids.
Disclosure of Invention
Aiming at the defects of the prior art, the invention aims to provide a method for reducing heat loss of essential amino acid of myofibrillar protein, which utilizes the interaction of nano cellulose molecules, myofibrillar protein molecules and amino acid residues thereof to reduce the damage degree of the spatial structure of the myofibrillar protein after being heated and reduce the exposure of the amino acid residues buried in the myofibrillar protein, thereby reducing the heat loss of the essential amino acid of the myofibrillar protein in the heating process and improving the quality of heat-treated meat products.
In order to achieve the purpose, the invention adopts the following technical scheme:
a method of reducing heat loss from essential amino acids of myofibrillar proteins comprising the steps of:
s1, dicing fresh meat, grinding, uniformly mixing with a separation buffer solution I with ten times of volume, centrifuging the obtained mixed solution, and collecting a precipitate I;
s2, adding five times of volume of separation buffer II and 0.5% Triton X-100 into the collected precipitate I, homogenizing by using a homogenizer, and then centrifuging to collect the precipitate II;
s3, adding a separation buffer solution III into the precipitate II, and filtering by using gauze to remove the residual connective tissue; centrifuging and collecting a third precipitate, wherein the third precipitate is myofibrillar protein;
s4, adding a NaCl solution into the myofibrillar protein; adding nano-cellulose to prepare a mixed solution; the mixed solution was heated and immediately cooled in an ice bath.
Further, in step S1, the first separation buffer contains 25mM NaCl, 5mM Tris-HCl and 5mM EDTA, and has a pH of 7.5.
Further, in step S2, the second separation buffer contained 100mM NaCl, 5mM Tris-HCl, and 5mM EDTA, at a pH of 7.5.
Further, in step S3, the separation buffer III contains 100mM NaCl, 5mM Tris-HCl and 5mM EDTANA2，pH＝7.5。
Further, the centrifugation conditions in step S1 were 10000 Xg, 4 ℃.
Further, in step S2, homogenizing at 12,000rpm for 3 times, each for 30S, and intermittently for 10S; the centrifugation conditions were 10000 Xg, 4 ℃.
Further, in step S3, the conditions for centrifugation were 10000 Xg, 4 ℃.
Further, in step S4, the concentration of NaCl solution was 600mM, the concentration of myofibrillar protein was adjusted to 1mg/mL, and nanocellulose in an amount of 3% by mass of myofibrillar protein was added.
The invention has the beneficial effects that: the method of the invention utilizes the interaction of the nano-cellulose molecules, the myofibrillar protein molecules and the amino acid residues thereof to reduce the damage degree of the spatial structure of the myofibrillar protein after being heated and reduce the exposure of the amino acid residues buried in the myofibrillar protein, thereby reducing the heat loss of the essential amino acid of the myofibrillar protein in the heating process and improving the quality of the heat-treated meat product.
Drawings
FIG. 1 is a graph showing the particle size distribution of myofibrillar proteins experimentally measured in examples of the present invention.
Detailed Description
The present invention will be further described with reference to the accompanying drawings, and it should be noted that the present embodiment is based on the technical solution, and the detailed implementation and the specific operation process are provided, but the protection scope of the present invention is not limited to the present embodiment.
The method for reducing the heat loss of essential amino acids of myofibrillar proteins, provided by the embodiment, comprises the following steps of:
s1, dicing fresh meat, grinding for 10S with a stirrer, mixing with ten-fold volume of separation buffer one (25mM NaCl, 5mM Tris-HCl, 5mM EDTA, pH 7.5), centrifuging the mixed solution at 10000 × g and 4 ℃ to collect precipitate one;
s2, adding five times volume of separation buffer two (100mM NaCl, 5mM Tris-HCl, 5mM EDTA, pH 7.5) and 0.5% Triton X-100 to the first precipitate, and homogenizing 3 times at 12,000rpm for 30 seconds each for 10 seconds using a homogenizer, and then centrifuging at 10000 × g and 4 ℃ to collect the second precipitate;
s3, adding separation buffer III (100mM NaCl, 5mM Tris-HCl, 5mM EDTANa) into the second precipitate2pH 7.5), filtered through three layers of gauze to remove the remaining connective tissue. Centrifuging at 10000 Xg and 4 deg.C to collect precipitate III; the precipitate, trimyofibrillarin (MP), was kept at 4 ℃ for future use.
S4, adding 600mM NaCl solution into MP, and adjusting the concentration of the MP to be 1 mg/mL; adding nanocellulose (CNFs) with the mass of 3% of myofibrillar protein to prepare a mixed solution, wherein the mixed solution without the CNFs is a control group; the mixed solution was heated at 25, 80, 100 and 121 ℃ for 30 minutes, respectively, and immediately cooled to 4 ℃ in an ice bath. The relative content of essential amino acids and the particle size distribution of myofibrillar proteins were determined.
In this example, the steps S4 at 25 deg.C, 80 deg.C and 100 deg.C were carried out by heating in a water bath, and at 121 deg.C by heating in an oil bath in a pressure-resistant vessel.
TABLE 1
Note: the lower case letters (a-c) of the same column of data shoulder marks were different and indicated significant differences (P < 0.05); MP: myofibrillar proteins; CNFs: and (3) nano cellulose.
The relative amounts of essential amino acids of myofibrillar proteins determined are shown in table 1. In this example, the amino acid was detected by acid hydrolysis, and tryptophan was destroyed and could not be detected. The relative amounts of threonine, isoleucine, valine and phenylalanine do not change with increasing temperature. The relative content of leucine and lysine in the control group is obviously reduced along with the increase of temperature (80 ℃ -121 ℃) (P < 0.05). Leucine is reduced from 8.21% to 7.08%, lysine is reduced from 9.17% to 7.46%, and methionine is reduced from 2.19% to 1.53%. However, as the temperature (100 ℃ to 121 ℃) increases, the loss of three essential amino acids, leucine, lysine and methionine after adding CNFs is reduced compared with the control group.
The particle size distribution of myofibrillar proteins measured in the above examples is shown in FIG. 1. The MP particle size is divided into two peaks at 25 ℃ and is distributed in the ranges of 10-100nm and 100-1000 nm; with the addition of CNFs, the particle size of CNFs-MP is obviously increased. The particle size distribution of CNFs-MP is not changed much compared with that of MP with the temperature rise (25-100 ℃) (FIG. 1). The particle size distribution of MP and CNFs-MP is unimodal at 121 ℃, but the intensity of the latter is small and the distribution is wide, which shows that CNFs have a certain stabilizing effect on the MP structure.
In conclusion, the degree of space structure damage of the myofibrillar protein after being heated is reduced and the exposure of the amino acid residues buried in the myofibrillar protein is reduced through the interaction of the nano cellulose molecules, the myofibrillar protein molecules and the amino acid residues, so that the heat loss of the essential amino acid of the myofibrillar protein in the heating process is reduced, and the quality of the heat-treated meat product is improved.
Various corresponding changes and modifications can be made by those skilled in the art based on the above technical solutions and concepts, and all such changes and modifications should be included in the protection scope of the present invention.
Claims (8)
1. A method for reducing heat loss from essential amino acids in myofibrillar proteins comprising the steps of:
s1, dicing fresh meat, grinding, uniformly mixing with a separation buffer solution I with ten times of volume, centrifuging the obtained mixed solution, and collecting a precipitate I;
s2, adding five times of volume of separation buffer II and 0.5% Triton X-100 into the collected precipitate I, homogenizing by using a homogenizer, and then centrifuging to collect the precipitate II;
s3, adding a separation buffer solution III into the precipitate II, and filtering by using gauze to remove the residual connective tissue; centrifuging and collecting a third precipitate, wherein the third precipitate is myofibrillar protein;
s4, adding a NaCl solution into the myofibrillar protein; adding nano-cellulose to prepare a mixed solution; the mixed solution was heated and immediately cooled in an ice bath.
2. The method of claim 1, wherein in step S1, the first separation buffer comprises 25mM NaCl, 5mM Tris-HCl and 5mM EDTA, and has a pH of 7.5.
3. The method of claim 1, wherein in step S2, separation buffer two contains 100mM NaCl, 5mM Tris-HCl and 5mM EDTA, and has a pH of 7.5.
4. The method of claim 1, wherein in step S3, the separation buffer III contains 100mM NaCl, 5mM Tris-HCl and 5mM EDTANA2，pH＝7.5。
5. The method according to claim 1, wherein the centrifugation conditions of step S1 are 10000 × g, 4 ℃.
6. The method according to claim 1, wherein in step S2, the homogenizing conditions are 12,000rpm for 3 times of 30S each with 10S intervals; the centrifugation conditions were 10000 Xg, 4 ℃.
7. The method according to claim 1, wherein in step S3, the centrifugation is performed at 10000 Xg and 4 ℃.
8. The method according to claim 1, wherein in step S4, the concentration of NaCl solution is 600mM, the concentration of myofibrillar protein is adjusted to 1mg/mL, and nanocellulose with a mass of 3% of myofibrillar protein is added.
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| CN202111303417.1A CN113907175A (en) | 2021-11-05 | 2021-11-05 | Method for reducing heat loss of essential amino acid of myofibrillar protein |
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| CN202111303417.1A CN113907175A (en) | 2021-11-05 | 2021-11-05 | Method for reducing heat loss of essential amino acid of myofibrillar protein |
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Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN108771076A (en) * | 2018-05-17 | 2018-11-09 | 南京农业大学 | A kind of compound curcumin fribrillin solid beverage prepares and redissolves method |
| CN110353083A (en) * | 2019-08-30 | 2019-10-22 | 长江大学 | A method of heating improves pork myofibrillar protein gel retention ability |
| BE1027237B1 (en) * | 2019-10-30 | 2020-11-23 | Univ Xiamen | Process for the production of a reinforced gel-like myofibrillar protein |
| CN112574292A (en) * | 2020-12-15 | 2021-03-30 | 中国计量大学 | Method for preparing myofibrillar protein solution |
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN108771076A (en) * | 2018-05-17 | 2018-11-09 | 南京农业大学 | A kind of compound curcumin fribrillin solid beverage prepares and redissolves method |
| CN110353083A (en) * | 2019-08-30 | 2019-10-22 | 长江大学 | A method of heating improves pork myofibrillar protein gel retention ability |
| BE1027237B1 (en) * | 2019-10-30 | 2020-11-23 | Univ Xiamen | Process for the production of a reinforced gel-like myofibrillar protein |
| CN112574292A (en) * | 2020-12-15 | 2021-03-30 | 中国计量大学 | Method for preparing myofibrillar protein solution |
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| 仇超颖等: "糖基化鸢乌贼肌原纤维蛋白体外消化产物抗氧化性研究" * |
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