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1

Charakterystyka strukturalna, biochemiczna i funkcjonalna miesni zewnetrznych galki ocznej

100%
Majerczak J., Zoladz J. A., Duda K.
Postępy Biologii Komórki
|
2005
|
tom 32
|
nr 3
395-408
2

Funkcjonalne wlasciwosci preparatu bialek miesniowych z kregoslupow dorsza baltyckiego

100%
Skierka E., Sadowska M., Rzezuchowska E.
Medycyna Weterynaryjna
|
2009
|
tom 65
|
nr 06
422-426
The aim of the investigation was to establish the functional properties of muscle protein isolates from Baltic cod (Gadus morhua) spine which were also compared with a commercially available pork protein preparation. The muscle proteins were extracted in mild condition with 0.1M NaOH solution at 4°C and subsequently were precipitated at pH 4.5. The amino acid composition of protein isolates is similar to fresh muscle protein. At the basic pH values, the obtained preparation is almost three times more soluble than the commercially available pork protein. Cod proteins were in 25 and 90% solubilized at pH 8 and 12, respectively. At these pH values, after an increase of the ionic strength of the solution to 0.35, the protein solubility decreased about 10 and 15%, respectively. Spinal proteins at a pH range of 6-12 have a 16-time higher foaming capacity than that for pork proteins. The obtained proteins also have a two-times lower oil holding capacity and almost 5.5-times lower water holding capacity in comparison with the commercial preparation. The preparation of muscle proteins from Baltic cod had an ability to hold 0.26 g oil or 0.94 g water per g of protein. Its quite good functional properties encourage continuing research on the deodorization method. After deodorization this protein preparation could find an application in the food industry.
3

Wybrane własciwości karagenów - mechanizm żelowania oraz interakcje z białkami mięśniowymi

100%
Szacilo K., Cierach M.
Mięso i Wędliny
|
2005
|
nr 1
4

Optymalizacja odzyskiwania bialek miesniowych z kregoslupow dorsza baltyckiego

100%
Skierka E., Sadowska M., Majewska J.
Medycyna Weterynaryjna
|
2006
|
tom 62
|
nr 05
579-582
The aim of the study was to establish the optimum conditions for recovering non-collagen proteins from the backbones of cods by solvent extraction. The proteins were extracted in three different ways: twice in 24 h with 5% sodium chloride or 0.1 M sodium hydroxide solution, or firstly using 5% sodium chloride solution over 24 h, and then 0.1 M sodium hydroxide solution in 24 h. Different ratios of backbone to solution were tested, 1 : 2; 1 : 4; 1 : 6; 1 : 8; 1 : 10; 1 : 12. All procedures were performed at 4°C. 0.1 M solution of sodium hydroxide was more effective in extracting protein than 5% solution of sodium chloride. A 100% yield of non-collagen protein was recovered from fresh backbone by double 24 h extraction with sodium hydroxide solution, while this was 70%with sodium chloride solution. About 80% of the protein was soluble when extraction was conducted in the first stage with sodium chloride solution and then with sodium hydroxide solution. After 5 months of storing the backbone at -18°C, protein recovery decreased by about 40% for sodium chloride solution and about 20% for sodium hydroxide solution, and about 30% for mixed extraction. The extraction yield had no influence on the ratio of extracted material to solution. Collagen losses during extraction did not exceed 0,4%.
5

Enzymatyczna hydroliza bialek miesniowych kregoslupow dorsza baltyckiego

84%
Skierka E., Sadowska M., Mankowska J., Lipinska-Beyer A.
Medycyna Weterynaryjna
|
2008
|
tom 64
|
nr 05
677-680
Enzymatic hydrolysis was conducted to recover the potentially addible high protein hydrolysate from cod backbones. The commercially available alcalase and trypsyne was used for hydrolysis at enzyme concentrations of 2.5; 5; 10; 15; 20; 30 and 40 mg/g backbones. The enzymatic deproteinization was conducted for 24 and 48 h. All procedures were performed at pH 7.0 and 4°C. The yield of enzymatic hydrolysis increases with the growth of trypsine and alcalase concentration up to 20 and 10 mg/g backbone, respectively. The increase of these values did not influence the yield of enzymatic deproteinization. After the treatment by trypsyne, maximum recovery of protein from cod backbone was 60%, while by alcalase it was 55%. The yield of enzymatic hydrolysis was the same after 24 and 48 h. Collagen losses did not exceed 0.2%.
6

Charakterystyka bialek miesniowych i niemiesniowych stosowanych w przetworstwie miesa

84%
Makala H.
Gospodarka Mięsna
|
1998
|
tom 50
|
nr 10
24-25
7

Występowanie, budowa i funkcja α-aktyniny

84%
Kuznicki J.
Kosmos
|
1990
|
tom 39
|
nr 2-3
8

Strukturotwórcze funkcje białek mięśniowych i niemięsniowych

84%
Tyszkiewicz I.
Gospodarka Mięsna
|
1991
|
tom 43
|
nr 02
9
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Śródmięśniowy kolagen a kruchość mięsa

84%
Gorska M.
Wszechświat
|
2015
|
tom 116
|
nr 10-12
10

Modyfikacja wlasciwosci modelowych farszow miesno-tluszczowych technologia wysokich cisnien

84%
Kwiatkowska A., Dudkiewicz J., Cierach M.
Roczniki Instytutu Przemysłu Mięsnego i Tłuszczowego
|
2005
|
tom 42-43
179-188
11

Próba określenia katabolizmu białek mięśniowych u szczurów żywionych dawkami o obniżonym poziomie białka z dodatkiem Ridzolu

84%
Kaptur T.
Roczniki Naukowe Zootechniki
|
1985
|
tom 12
|
nr 2
12

Wpływ procesu poubojowego dojrzewania mięsa wieprzowego na zmiany profilu białek i kruchość

84%
Iwanska E., Mikolajczak B., Grzes B., Pospiech E.
Medycyna Weterynaryjna
|
2016
|
tom 72
|
nr 07
The aim of the study was to evaluate the post mortem proteolysis of centrifugal drip protein derived from pork. The varied course of the process of meat tenderization in muscles using the isoelectric focusing (IEF) technique was observed. The experimental material was the longissimus lumborum et thoracis muscle excised from 24 pigs of known origin, breeding and rearing conditions. Meat of normal quality (RFN) was examined in this study. On the basis of shear force values, the experimental muscles were divided into 4 groups of different courses of tenderization: A – meat remaining tough during the entire 6-day period of post-slaughter changes; B – meat characterized by a typical tenderization process, i.e. tough 48 h after slaughter and tender after 6 days of storage; C – tender or relatively tender meat on both dates of examination; D – meat which was the toughest 48 hours after slaughter and the most tender 144 hours after slaughter. Proteins for electrophoretic analysis on the agarose gel of the centrifugal drip fraction were submitted after 48 h and 144 h post mortem. The separation of the proteins was performed in a horizontal layout, using an FBE-3000 apparatus and an ECPS power pack (Pharmacia). On every path of the proteins separation, four ranges of pH value were evaluated, namely: 4.0 ÷ 6.0 pI, 6.1 ÷ 7.2 pI, 7.3 ÷ 7.7 pI and > 7.7 pI. Meat tenderness on the second day after slaughter was influenced by proteins, in which their pI was in the range of 6.1 ÷ 7.2 and 4.0 ÷ 6.0. From the evaluation which was carried out in the immunoblotting analysis of proteins using troponin T (9D) antibodies it was demonstrated that 48 h after slaughtering the most intense reactions were observed in the range of pI of 5.5 ÷ 5.9, which is the pH range corresponding to the isoelectric point of troponin T. However, after 144 h post mortem the most intense reaction was demonstrated in the range of pI of 6.1÷ 7.7. This indicates the breakdown of troponin T and an increase of the number of degradation products of this protein occurring while the meat tenderization process progresses. The degradation products of troponin T identified by IEF can be an indicator of meat tenderization.
13

55 Międzynarodowy Kongres Nauki o Mięsie i Technologii. Część I

67%
Szymanski P., Janiszewski P.
Gospodarka Mięsna
|
2010
|
tom 62
|
nr 01
14

Porównanie zmian wskaźników denaturacji zachodzącej w zamrażalniczo przechowywanym mięsie

67%
Lesiow T.
Chłodnictwo
|
1988
|
tom 23
|
nr 08
15

Bilansowanie białka

67%
Rybak K.
Magazyn Przemysłu Mięsnego
|
2006
|
nr 10
16

Jakość mięsa drobiowego podczas zamrażania i zamrażalniczego przechowywania

59%
Chwastowska-Siwiecka I., Skiepko N.
Gospodarka Mięsna
|
2013
|
tom 65
|
nr 07
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