SU544413A1 - Meat storage method - Google Patents
Meat storage methodInfo
- Publication number
- SU544413A1 SU544413A1 SU2125426A SU2125426A SU544413A1 SU 544413 A1 SU544413 A1 SU 544413A1 SU 2125426 A SU2125426 A SU 2125426A SU 2125426 A SU2125426 A SU 2125426A SU 544413 A1 SU544413 A1 SU 544413A1
- Authority
- SU
- USSR - Soviet Union
- Prior art keywords
- storage method
- meat storage
- attack
- proteins
- protein
- Prior art date
Links
Landscapes
- Coloring Foods And Improving Nutritive Qualities (AREA)
Description
в т контрольные пробы, содержащие все компоненты , кроме раствора фермента.in t control samples containing all components except the enzyme solution.
Как исследуемые, так и контрольные нробы выдерживают в термостате при 37°С 4 час. Останавливают реакцию гидролиза белков ферментом равным объемом 10%-ной трихлоруксусной кислоты. В контрольные пробы раствор фермента ввод т после добавлени трнхлоруксусной кислоты. После осаждени непереваренной части белков пробы центрифугируют 40 мин при скорости 6000 G, и в прозрачных центрифугатах определ ют оптическое поглощение на СФ-4 при 276 ммк. По калибровочной кривой устанавливают накопление тирозина при оптимальных услови х гидролиза белков под действием трипсина и выражают их ферментативную «атакуемость в гаммах тирозина на 1 мг белкового азота (Y тир./мг N).Both the test and control snoobs are kept in a thermostat at 37 ° C for 4 hours. Stop the hydrolysis of proteins by an enzyme equal to a volume of 10% trichloroacetic acid. Enzyme solution was added to the control samples after trichloroacetic acid was added. After sedimentation of the undigested part of the proteins, the samples are centrifuged for 40 min at a speed of 6000 G, and the optical absorption at SF-4 at 276 mmk is determined in transparent centrifugates. The calibration curve establishes the accumulation of tyrosine under optimal conditions of protein hydrolysis under the action of trypsin and expresses their enzymatic attack in gamma tyrosine per 1 mg of protein nitrogen (Y tyr / mg N).
В период окоченени мыщечной ткани «атакуемость белков ферментами снижаетс , в период расслаблени - повыщаетс .During the period of numbness of the muscular tissue, the "attack of proteins by enzymes decreases, and during the period of relaxation it increases.
Данные анализа «атакуемости фибрилл рных белков мышечной ткани под действием трипсина по результатам лабораторных и промыщленных испытаний привод тс в таблицеData on the attack of fibrillary proteins of muscle tissue under the action of trypsin from laboratory and industrial tests are given in the table.
По результатам как лабораторных, так и промыщленных испытаний минимальна «атакуемость белков 34-35 Y тир./мг N характеризует завершение окоченени м са на п тый мес ц.According to the results of both laboratory and industrial tests, the minimal attack of 34-35 Y proteins / mg N protein characterizes the completion of a five-month-long self-accumulation.
После п ти мес цев хранени м са «атакуемость белков возрастает. Оптимум достигаетс на дес тый мес ц но данным лабораторных исследований и на 7-10 мес ц при нромыщленных испытани х. При этом исследуемый показатель возрастает на 47 и 31% соответственно относительно минимального значени на п тый мес ц хранени . К 12-му мес цу ферментативна «атакуемость белков снижаетс , и это служит показателем окончани срока хранеии .After five months of storage, the protein attack rate increases. The optimum is reached for the tenth month according to laboratory tests and at 7-10 months for the unsaturated trials. At the same time, the studied indicator increases by 47 and 31%, respectively, relative to the minimum value for the fifth month of storage. By the 12th month, the enzymatic protein attack rate decreases, and this is an indication of the end of storage.
Claims (1)
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
SU2125426A SU544413A1 (en) | 1975-04-14 | 1975-04-14 | Meat storage method |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
SU2125426A SU544413A1 (en) | 1975-04-14 | 1975-04-14 | Meat storage method |
Publications (1)
Publication Number | Publication Date |
---|---|
SU544413A1 true SU544413A1 (en) | 1977-01-30 |
Family
ID=20616564
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
SU2125426A SU544413A1 (en) | 1975-04-14 | 1975-04-14 | Meat storage method |
Country Status (1)
Country | Link |
---|---|
SU (1) | SU544413A1 (en) |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
RU2685197C1 (en) * | 2018-04-02 | 2019-04-16 | Федеральное государственное бюджетное образовательное учреждение высшего образования "Астраханский государственный технический университет" | Method for long-term storage of frozen meat |
-
1975
- 1975-04-14 SU SU2125426A patent/SU544413A1/en active
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
RU2685197C1 (en) * | 2018-04-02 | 2019-04-16 | Федеральное государственное бюджетное образовательное учреждение высшего образования "Астраханский государственный технический университет" | Method for long-term storage of frozen meat |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Siegelman et al. | Investigation of serum trypsin and related substances: I. The quantitative demonstration of trypsinlike activity in human blood serum by a micromethod | |
Todd | Quantitative studies on the total plasmin and the trypsin inhibitor of human blood serum: I. Methods for the titration of total plasmin and of trypsin inhibitor | |
Akazawa et al. | Structure and function of chloroplast proteins. XIV. Subunit structure of spinach leaf ribulose 1, 5-diphosphate carboxylase | |
Husain et al. | [44] Reversible resolution of flavoproteins into apoproteins and free flavins | |
SU544413A1 (en) | Meat storage method | |
Pauly et al. | Whole blood microculture assay of human lymphocyte function | |
Holland et al. | Chemical reactivity at the catalytic sites of aspartic β-semialdehyde dehydrogenase and glyceraldehyde 3-phosphate dehydrogenase | |
Lum et al. | Comparison of four methods for measuring uric acid: Copper-chelate, phosphotungstate, manual uricase, and automated kinetic uricase | |
Morris | A comparison of methods for the estimation of serum cholesterol and values in random samples of populations in the 55-64 age group | |
Gochman et al. | The amino acid decarboxylase of salivary sediment | |
Matsunaga et al. | Rapid determination of phenylalanine with immobilized leuconostoc mesenteroides and a lactate electrode | |
Fleisher et al. | Leucine aminopeptidase in human serum: An ultramicromethod for the determination of the rates of hydrolysis of L-leucylglycine | |
French et al. | A comparison of methods for measuring acetyl cholinesterase activity in blood samples inhibited by carbamates | |
EP0330358A3 (en) | Method of identifying whole cells having serine esterase activity | |
Humoller et al. | Improved method for the colorimetric determination of glutamic-oxalacetic transaminase activity | |
Corbett | Factors influencing substrate utilization by Tetrahymena pyriformis | |
Darrow et al. | UDP-glucose dehydrogenase from the chick embryo: tissue-specific forms of the enzyme | |
SU1409942A1 (en) | Method of diagnostics of psoriasis | |
SU819635A1 (en) | Method of determination of stainless steel tendency to intercrystalline corrosion | |
SU1596253A1 (en) | Method of diagnosis of kidney tuberculosis | |
US3897363A (en) | Blood control standard | |
DE69431874D1 (en) | METHOD FOR DIAGNOSIS OF DIABETES AND PREDIABETIC CONDITIONS | |
Planterose | Effect of inhibitors on the metabolism of cells in tissue culture and on foot-and-mouth disease virus synthesis | |
Cohen | [94] Determination and isolation of carbamylglutamic acid and related compounds | |
SU130630A1 (en) | Nutrient medium for tissue culture |