WO1990005462A1 - Procede permettant d'ameliorer la qualite de la viande recuperee mecaniquement - Google Patents
Procede permettant d'ameliorer la qualite de la viande recuperee mecaniquement Download PDFInfo
- Publication number
- WO1990005462A1 WO1990005462A1 PCT/DK1989/000272 DK8900272W WO9005462A1 WO 1990005462 A1 WO1990005462 A1 WO 1990005462A1 DK 8900272 W DK8900272 W DK 8900272W WO 9005462 A1 WO9005462 A1 WO 9005462A1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- mrm
- activity
- viscosity
- maximum
- meat
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Ceased
Links
Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
- A23L13/40—Meat products; Meat meal; Preparation or treatment thereof containing additives
- A23L13/48—Addition of, or treatment with, enzymes
Definitions
- MRM mechanically recovered meat
- MRM covers meat from all kinds of animals, principally cows, calves, pigs and poultry.
- MRM is isolated as indicated in Meat Science, vol. 5 (1980 - 81), Applied Science Publishers Ltd., London, p. 171 - 200, or in Food, July 11983, p. 26 - 30.
- the MRM is produced by high pressure extrusion or by hard pressing with pressure treat ⁇ ment, and any meat material produced similarly, but not necessarily a meat product, which would undoubtedly be classified as MRM, is considered an MRM in relation to this invention.
- MRM is used as an ingredient in comminuted meat products like sausages, luncheon meat and pates.
- methods for production of MRM used today partly denature the MRM protein, whereby the functional properties thereof are impaired, MRM has been upgraded by addition of non-meat proteins like blood plasma or other proteinaceous emulsi- fiers.
- non-meat proteins like blood plasma or other proteinaceous emulsi- fiers.
- dilution with relatively large amounts of non-meat proteins is unwanted, and also, the organoleptic properties of the upgraded MRM is not always satisfactory; furthermore, the cost related to the upgrading is relatively big.
- MRM which should not involve any dilution with relatively large amounts of non-meat proteins, which should give rise to satisfactory organoleptic and functional properties, and which should be relatively cheap. According to the invention surprisingly it has been found that the above need can be fulfilled, if the MRM is treated with an enzyme selected from a narrow class of enzymes, and if the enzymatic treatment is effectively interrupted at a specified stage.
- the method according to the invention for upgrading of MRM is characterized by the fact that MRM is treated with an endo- protease with a pH-activity optimum above neutrality with a proteolytic activity related to a weight unit of dry protein which will generate a maximum viscosity increase in relation to the initial viscosity of at least 50%, for a period of time corresponding to a resulting viscosity of the MRM which is between 100 and 75% of the maximum viscosity generated by the enzyme treatment, whereafter the enzymatic activity is destroyed by means of any method which .does not harm the functionality of the meat.
- pH-activity optimum should be determined according to the Anson method, for instance as described in NOVO Enzymes Product Sheet, B273c- GB 1500 Sept. 1987.
- trypsin-like proteases are the proteases originating from St. griseus, St. fradiae, and St. crythreus.
- NEUTRASE a neutral protease produced by means of B. subtilis
- Sumyzyme an acid fungal protease produced by means of Aspergillus niger
- pepsin an acid fungal protease produced by means of Aspergillus niger
- viscosity of the MRM means the viscosity of the MRM mass per se, or ordinarily the viscosity of an MRM containing aqueous suspension, if water is added in order to facilitate handling.
- proteases belonging to the above indicated class if used in a certain minimum concentration measured in Anson units per g of MRM generates a temporary viscosity increase of the MRM, whereas in all other cases belonging to the prior art, when a protein is treated with a protease, a viscosity decrease is observed.
- proteases belonging to the group which comprises endo- proteases with a pH-activity optimum above neutrality the applicant has performed experiments with several proteases in regard to their effect on the viscosity of an aqueous MRM suspension, i.e. pepsin, Sumyzyme AP protease, and NEUTRASE protease .
- FIG. 1 which shows the typical viscosity curve corresponding to an MRM suspension treated with protease not belonging to the group comprising endo-proteases with a pH-activity optimum above neutrality. Details in regard to Fig. 1 will appear in a later part of this specification. Also, reference can be made to fig. 2, which shows the atypical viscosity curve corresponding to an MRM suspension treated with a protease belonging to the group comprising endo-proteases with a pH-activity optimum above neutrality, i.e. trypsin. Details in regard to Fig. 2 will appear in a later part of this specification. It appears from Fig.
- a dosage of 0.033 Anson units/g of protein is outside the scope of the invention, as the minimum dosage of enzyme should generate a viscosity increase of at least 50%.
- Fig. 3 is a graph which shows the viscosity versus time with different proteases. In each case 0.154 Anson units/g of protein is added at zero time, except for the blind. The temperature is 35°C, the pH is 6.4 and the substrate concentration is 10%. It clearly appears from the graph that the proteases belonging to the group comprising endo-proteases with a pH-activity optimum above neutrality all generate a temporary viscosity increase, whereas the other proteases do not generate such viscosity increase.
- Enzyme inhibition by pH adjustment deteriorates the meat quality.
- the enzyme process can be terminated by heat inactivation and/or by addition of an inhibitor for the endo-protease used, for instance a specific trypsin inhibitor on soy base, if trypsin is the endo-protease used.
- GB patent application no. 2,021,921 describes a process for stabilization of aqueous protein containing suspensions by means of treatment with proteases, and from Example 1 in this GB application it appears that the process is accompanied by a viscosity increase.
- the present invention is exclusively concerned with a most specific starting material, viz . MRM, which is not described in the GB patent application.
- MRM most specific starting material
- the second place it is correct that a viscosity increase is observed in the prior art process, but this viscosity increase is expected because it is associated with the conversion of the casein due to the milk clotting activity of the added protease; the viscosity increase in relation to the present invention is still surprising.
- MRM is treated with trypsin with a proteo ⁇ lytic activity of 0.05 Anson units/g of dry protein or above. With this minimal proteolytic activity a maximum viscosity increase in relation to the initial viscosity of at least 50% will appear, and thus an important improvement of the functional properties is secured.
- the water is added to MRM before the enzymatic treatment, the ratio between water and MRM, calculated as MRM dry matter, being within 0 and 1.0. If the ratio between water and MRM is more than 1.0, the dilution is too high, and the quality of the corresponding forcemeat will be inferior.
- the concentration of the enzyme is between 0.05 and 0.15 Anson units/g of dry protein. If the concentration of the enzyme is below 0.05 Anson units/g of dry protein, the improvement of the functional properties is too low, and if the concentration of the enzyme is above 0.15 Anson units/g of dry protein, the enzyme cost tends to be too high.
- the treatment time corresponds to a result ⁇ ing viscosity of the MRM between 100 and 90% of the maximum viscosity generated by the enzymatic treatment.
- the water binding ability of the treated MRM is as high as possible, and thus the functional property thereof is as good as possible.
- the enzyme is heat inactivated during that part of the process which corresponds to 75% of the maximum activity (initial) to maximum activity to 75% of the maximum activity (final), whereby the heat inactivation is termi ⁇ nated at a stage corresponding to or almost corresponding to the maximum activity.
- the inactivation is carried out in a very simple manner, and no addition of inhibitor is needed.
- the enzyme is inactivated during that part of the process which corresponds to 75% of the maximum activity (initial) to maximum activity to 75% of the maximum activity (final), whereby inactivation is performed by a combined heat treatment and a treatment with a trypsin in ⁇ hibitor, preferably a soy trypsin inhibitor.
- a trypsin in ⁇ hibitor preferably a soy trypsin inhibitor.
- MRM contains as an average 16.5% protein
- a 20% (w/w) excess of trypsin inhibitor is added.
- 300 ml of soy oil or 200 ml of ion exchanged water is added, and the mixture is homogenized for 5 minutes at the lowest speed.
- the forcemeat is transferred to tared cans, which are closed and heat treated at 90°C for 25 minutes, and immediately after cooled in running, cold water for 30 minutes.
- the cans are stored in a refrigerator at 5°C for around 24 hours.
- the cans are weighed, and then opened, and the separated soy oil or water fraction is drained from the cans, which again are weighed. Now the fat retention ability or the water retention ability can be calculated. These values for the fat retention ability and the water retention ability correspond to a hydrolysis time of 10 minutes. By addition of trypsin inhibitor and soy oil or water at earlier or later stages values for the fat retention ability and the water retention ability at earlier or later stages during hydrolysis can be obtained. In this manner a curve of percentage of oil retention versus hydrolysis time (Fig. 4) and of percentage of water retention versus hydrolysis time (Fig. 5) can be drawn up. It appears from Figs.
- forcemeat prepared with the upgraded MRM produced according to the invention shows improved functional properties both in regard to oil retention ability and water retention ability, corresponding to the surprising viscosity rise generated by the activity of endo-proteases with a pH-activity optimum above neutrality.
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Microbiology (AREA)
- Health & Medical Sciences (AREA)
- Nutrition Science (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Meat, Egg Or Seafood Products (AREA)
Abstract
Procédé permettant d'améliorer la qualité de la viande récupérée mécaniquement, où l'on traite ladite viande au moyen d'une endoprotéase, ayant une valeur optimale d'activité pH supérieure à la neutralité et une activité protéolytique en rapport avec l'unité de masse d'une protéine sèche, qui génèrera une augmentation maximale de la viscosité de 50 % au moins par rapport à la viscosité initiale, et ce pendant un laps de temps correspondant à une augmentation représentant entre 75 % et 100 % de la viscosité maximale de ladite viande obtenue par traitement enzymatique. L'activité enzymatique est ensuite arrêtée par tout procédé ne nuisant pas à la fonctionnalité de la viande. Ledit procédé, qui est, par ailleurs, peu coûtuex et ne comprend aucune dilution de quantités relativement élevées de protéines non animales, comporte des propriétés fonctionneles et organoleptiques intéressantes.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DK652088A DK652088D0 (da) | 1988-11-23 | 1988-11-23 | Fremgangsmaade til kvalitetsforbedring af ad mekanisk vej udvundet koed |
| DK6520/88 | 1988-11-23 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| WO1990005462A1 true WO1990005462A1 (fr) | 1990-05-31 |
Family
ID=8148837
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| PCT/DK1989/000272 Ceased WO1990005462A1 (fr) | 1988-11-23 | 1989-11-17 | Procede permettant d'ameliorer la qualite de la viande recuperee mecaniquement |
Country Status (3)
| Country | Link |
|---|---|
| CA (1) | CA2003525A1 (fr) |
| DK (1) | DK652088D0 (fr) |
| WO (1) | WO1990005462A1 (fr) |
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1992013964A1 (fr) * | 1991-02-06 | 1992-08-20 | Novo Nordisk A/S | Preparations proteiques |
| WO1994001003A1 (fr) * | 1992-07-03 | 1994-01-20 | Novo Nordisk A/S | Procede de production d'un hydrolysat carne, et application de celui-ci |
| US5866357A (en) * | 1990-03-09 | 1999-02-02 | Novo Nordisk A/S | Method for hydrolyzing proteins with gluyasp specific protease |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3723250A (en) * | 1967-10-03 | 1973-03-27 | Novo Terapeutisk Labor As | Proteolytic enzymes, their production and use |
| GB1507380A (en) * | 1976-09-01 | 1978-04-12 | Aarhus Oliefabrik As | Process for the production of foodstuffs containing clottable milk proteins and proteins of vegetable or microbial origin |
| GB2021921A (en) * | 1978-05-31 | 1979-12-12 | Unilever Ltd | Stabilised milk proteins- containing compositions |
| US4388331A (en) * | 1981-01-23 | 1983-06-14 | Devro, Inc. | Collagen sausage casing |
-
1988
- 1988-11-23 DK DK652088A patent/DK652088D0/da not_active Application Discontinuation
-
1989
- 1989-11-17 WO PCT/DK1989/000272 patent/WO1990005462A1/fr not_active Ceased
- 1989-11-21 CA CA002003525A patent/CA2003525A1/fr not_active Abandoned
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3723250A (en) * | 1967-10-03 | 1973-03-27 | Novo Terapeutisk Labor As | Proteolytic enzymes, their production and use |
| GB1507380A (en) * | 1976-09-01 | 1978-04-12 | Aarhus Oliefabrik As | Process for the production of foodstuffs containing clottable milk proteins and proteins of vegetable or microbial origin |
| GB2021921A (en) * | 1978-05-31 | 1979-12-12 | Unilever Ltd | Stabilised milk proteins- containing compositions |
| US4388331A (en) * | 1981-01-23 | 1983-06-14 | Devro, Inc. | Collagen sausage casing |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5866357A (en) * | 1990-03-09 | 1999-02-02 | Novo Nordisk A/S | Method for hydrolyzing proteins with gluyasp specific protease |
| WO1992013964A1 (fr) * | 1991-02-06 | 1992-08-20 | Novo Nordisk A/S | Preparations proteiques |
| US5523237A (en) * | 1991-02-06 | 1996-06-04 | Novo Nordisk A/S | Protein preparations |
| WO1994001003A1 (fr) * | 1992-07-03 | 1994-01-20 | Novo Nordisk A/S | Procede de production d'un hydrolysat carne, et application de celui-ci |
| US5532007A (en) * | 1992-07-03 | 1996-07-02 | Novo Nordisk A/S | Method for production of a meat hydrolyzate |
Also Published As
| Publication number | Publication date |
|---|---|
| CA2003525A1 (fr) | 1990-05-23 |
| DK652088D0 (da) | 1988-11-23 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| EP1260144B1 (fr) | Procede de production d'un hydrolisat de proteine de soja | |
| Nalinanon et al. | Improvement of gelatin extraction from bigeye snapper skin using pepsin-aided process in combination with protease inhibitor | |
| EP0782393B1 (fr) | Procede de traitement d'une solution proteinique aqueuse pour tuer les micro-organismes qu'elle contient sans induire de coagulation | |
| Kristinsson et al. | Kinetics of the hydrolysis of Atlantic salmon (Salmo salar) muscle proteins by alkaline proteases and a visceral serine protease mixture | |
| US3857966A (en) | Process for bland, soluble protein | |
| US4220723A (en) | Enzymatic treatment of proteinaceous animal waste products | |
| CA2132302C (fr) | Methode de production d'un produit similaire au lait, le produit similaire au lait, et utilisation de ce produit | |
| RU2185075C2 (ru) | Способ получения съедобного гидролизата (варианты) | |
| Gómez‐Guillén et al. | Functional and thermal gelation properties of squid mantle proteins affected by chilled and frozen storage | |
| US4677069A (en) | Clam derived proteinases | |
| JP3325892B2 (ja) | 肉加水分解産物の製造方法及び肉加水分解産物の使用 | |
| AU670370B2 (en) | Method for production of a not acidified edible gel on milk basis, and use of such gel | |
| JPH09208A (ja) | 肉パティの製造方法 | |
| US4386160A (en) | Thermal destabilization of bacillus serine proteases | |
| CRONLUND et al. | Solubilization of collagen in restructured beef with collagenases and α‐Amylase | |
| US4600588A (en) | Milk protein hydrolysate and process of preparation | |
| JP2626700B2 (ja) | 低アレルゲン化したホエータンパク加水分解物及びその製造法 | |
| WO1990005462A1 (fr) | Procede permettant d'ameliorer la qualite de la viande recuperee mecaniquement | |
| JPH10165106A (ja) | 改質された大豆蛋白素材の製造方法 | |
| Pongsetkul et al. | Characterization of endogenous protease and the changes in proteolytic activity of Acetes vulgaris and Macrobrachium lanchesteri during kapi production | |
| Sessa et al. | Chemical inactivation of soybean trypsin inhibitors | |
| de Barros Soares et al. | Influence of some commercial proteases and enzymatic associations on the hydrolytic solubilization of deboned poultry meat proteins Influencia de algunas proteasas comerciales y preparados enzimáticos en la solubilización hidrolitica de las proteínas de la carne de pollo separada mecánicamente | |
| Morrissey et al. | Tenderisation of meat: a review | |
| Ashie et al. | α; 2‐Macroglobulin Inhibition of Endogenous Proteases in Fish Muscle | |
| JP2804220B2 (ja) | 食用骨粉の製造法 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| AK | Designated states |
Kind code of ref document: A1 Designated state(s): DK FI HU JP NO SU US |
|
| AL | Designated countries for regional patents |
Kind code of ref document: A1 Designated state(s): AT BE CH DE ES FR GB IT LU NL SE |