Preparation method of strong gelatin fibrillin

The technology of myofibrillar protein and strong gel is applied in the field of preparation of strong gel myofibrillar protein, which can solve the problems of decreased water holding capacity, poor gelation ability of fish meat protein, and reduction of the number of sulfhydryl groups.

Inactive Publication Date: 2018-10-09
XIAMEN UNIV
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  • Abstract
  • Description
  • Claims
  • Application Information

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Problems solved by technology

[0003] Studies have shown that horse mackerel meat is easily oxidized during rinsing and storage, which significantly increases the carbonyl content in fish meat (Sylvie, Carolinep et al. 2015); protein oxidation in rainbow trout meat changes chemical forces, such as hydrophobic force, Disulfide bonds, non-covalent bonds, etc., promote the change of protein molecular conformation and aggregation mode (Herrera and Mackie 2004). Protein oxidation in fish meat is also caused by free radical chain reaction. Free radicals first attack the protein with active side chains. The peptide chain backbone (Sante-Lhoutellier, Aubry et al.2007), such as cysteine, tryptophan, lysine, will produce carbonyl derivatives, reduce the number of sulfhydryl groups, etc., resulting in oxidized fish protein gel Decreased capacity, reduced elasticity, decreased water holding capacity

Method used

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  • Preparation method of strong gelatin fibrillin
  • Preparation method of strong gelatin fibrillin

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Experimental program
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Effect test

Embodiment 1

[0024] Such as figure 1 Shown, a kind of preparation method of strongly gelatinous myofibrillar protein comprises the steps:

[0025] (1) Add the first separation buffer to the minced surimi, and then homogenize and centrifuge to remove the soluble protein to obtain the first precipitate, then add the second separation buffer to the first precipitate, and then Homogenize, filter the liquid with three layers of gauze and centrifuge to get the second precipitate; the pH of the above first separation buffer is 7.0, including 0.1M KCl, 2mM MgCl 2 , 1mM EGTA, 0.5mM DTT and 10mM K 2 HPO 4 ; The pH of the above second buffer is 6.0, including 0.1M NaCl and 1mM NaN 3 ; In this step, the homogenization condition is 8000rpm, 5min, and the centrifugation condition is 8000rpm, 15min, 4°C;

[0026] (2) Add cold dissolving buffer solution to the above-mentioned second precipitation, place it at 0°C for 30 minutes after homogenization, then centrifuge to take the supernatant, and then co...

Embodiment 2

[0031] (1) Add the first separation buffer to the minced surimi, and then homogenize and centrifuge successively to remove the soluble protein to obtain the first precipitate, then add the second separation buffer to the first precipitate, and then Homogenize, filter the liquid with three layers of gauze and centrifuge to get the second precipitate; the pH of the above first separation buffer is 7.0, including 0.1M KCl, 2mM MgCl 2 , 1mM EGTA, 0.5mM DTT and 10mM K 2 HPO 4 ; The pH of the above second buffer is 6.0, including 0.1M NaCl and 1mM NaN 3 ; In this step, the homogenization condition is 8000rpm, 5min, and the centrifugation condition is 8000rpm, 15min, 4°C;

[0032] (2) Add cold dissolving buffer solution to the above-mentioned second precipitation, place it at 0°C for 30 minutes after homogenization, then centrifuge to take the supernatant, and then concentrate it with an ultrafiltration tube to obtain a concentrated solution with a concentration of 20mg / mL; the abo...

Embodiment 3

[0036] (1) Add the first separation buffer to the minced surimi, and then homogenize and centrifuge successively to remove the soluble protein to obtain the first precipitate, then add the second separation buffer to the first precipitate, and then Homogenize, filter the liquid with three layers of gauze and centrifuge to get the second precipitate; the pH of the above first separation buffer is 7.0, including 0.1M KCl, 2mM MgCl 2 , 1mM EGTA, 0.5mM DTT and 10mM K 2 HPO 4 ; The pH of the above second buffer is 6.0, including 0.1M NaCl and 1mM NaN 3 ; In this step, the homogenization condition is 8000rpm, 5min, and the centrifugation condition is 8000rpm, 15min, 4°C;

[0037] (2) Add cold dissolving buffer solution to the above-mentioned second precipitation, place it at 0°C for 30 minutes after homogenization, then centrifuge to take the supernatant, and then concentrate it with an ultrafiltration tube to obtain a concentrated solution with a concentration of 20mg / mL; the above...

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Abstract

The invention discloses a preparation method of strong gelatin fibrillin. The method comprises the following steps of (1) preparing fibrillin; (2) dissolving the fibrillin; performing concentration toobtain concentration liquid; (3) adding the concentration liquid into pyrogallic acid; performing uniform mixing; thus obtaining a mixed protein solution after the placement at the normal temperature; (4) performing vacuum packaging on the mixed protein solution; performing treatment at ultrahigh pressure; (5) performing program temperature rise on materials obtained in the step (4); performing sharp cooling to obtain the strong gelatin fibrillin. The system oxidization degree of the fibrillin is weakened by using the oxidization resistance of pyrogallic acid; ultrahigh pressure treatment iscombined, so that the inside structure of the fibrillin is changed; the uniform three-dimensional network gel structure is formed. The method is applicable to the field of food processing auxiliary materials; the quality of fish meat products is regulated.

Description

technical field [0001] The invention belongs to the technical field of food processing auxiliary materials, and in particular relates to a preparation method of strong gelling myofibrillar protein. Background technique [0002] Myofibrillar protein is a kind of salt-soluble protein with important biological functional properties, and it is also the main protein that constitutes muscle fibers, accounting for 50-55% of the total protein content, mainly including myosin, actin, tropomyosin , troponin, etc. Myofibrillar proteins are involved in the contraction of muscles, affecting the tenderness of meat and the functional properties of meat products, such as gelation, rheological properties, water retention, elasticity, texture, etc. Among them, the gel properties of myofibrillar proteins are the most important functional properties in the processing of surimi products. Gel is an elastic semi-solid intermediate between solid and liquid, uniform in appearance and maintaining a...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): A23J1/04
CPCA23J1/04A23V2002/00A23V2250/543A23V2300/46A23V2300/38A23V2300/14A23V2250/02A23J3/22A23L17/70
Inventor 凌雪萍马荣荣卢英华何宁吴雪娥车黎明李正龙
Owner XIAMEN UNIV
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