Proteins in Fish Muscle. IV. Denaturation by Salt

1952 ◽  
Vol 8c (5) ◽  
pp. 325-331 ◽  
Author(s):  
J. D. Duerr ◽  
W. J. Dyer
Keyword(s):  
Sodium Chloride ◽  
Salt Concentration ◽  
Fish Muscle ◽  
Moisture Loss ◽  
Sudden Increase ◽  
Muscle Proteins ◽  
Salt Uptake ◽  
Critical Salt Concentration

Study of the denaturation of cod muscle proteins by sodium chloride shows that the myosin fraction is denatured when a critical salt concentration, about 8 to 10 per cent in the muscle, is reached. Paralleling the rapid denaturation, a sudden increase of salt uptake and of moisture loss occurs.

Proteins in Fish Muscle.: I. Extraction of Protein Fractions in Fresh Fish

1950 ◽  
Vol 7d (10) ◽  
pp. 585-593 ◽  
Author(s):  
W. J. Dyer ◽  
H. V. French ◽  
J. M. Snow
Keyword(s):  
Sodium Chloride ◽  
Salt Concentration ◽  
Total Protein ◽  
Muscle Protein ◽  
Fish Muscle ◽  
Fresh Fish ◽  
Cent Sodium ◽  
Optimum Ph ◽  
Muscle Myosin ◽  
Optimum Salt Concentration

Methods for the extraction of protein from fish muscle have been studied. Using the Waring Blendor to obtain fine subdivision, up to 95 per cent of the fish muscle protein can be extracted with 5 per cent sodium chloride. Optimum pH for extraction was pH 7–9, and the optimum salt concentration 3 to 5 per cent. About 3 per cent stroma protein, collagen and elastin, was found in cod and haddock muscle. Myosin constituted about 75 to 80 per cent of the total protein. Globulin X, myogen, and myoalbumin made up about 20 per cent of the protein.

TURBIDITY OF SUSPENSIONS AND MORPHOLOGY OF RED HALOPHILIC BACTERIA AS INFLUENCED BY SODIUM CHLORIDE CONCENTRATION

1960 ◽  
Vol 6 (5) ◽  
pp. 535-543 ◽  
Author(s):  
Dinah Abram ◽  
N. E. Gibbons
Keyword(s):  
Sodium Chloride ◽  
Salt Concentration ◽  
Morphological Changes ◽  
Halophilic Bacteria ◽  
Chloride Concentration ◽  
Chloride Content ◽  
Wall Structure ◽  
Abrupt Decrease ◽  
High Sodium ◽  
Rigid Cell Wall

The optical densities of suspensions of cells of Halobacterium cutirubrum, H. halobium, or H. salinarium, grown in media containing 4.5 M sodium chloride, increase as the salt concentration of the suspending medium decreases, until a maximum is reached at about 2 M; below this concentration there is an abrupt decrease in optical density. The cells are rod shaped in 4.5 M salt and change, as the salt concentration decreases, through irregular transition forms to spheres; equal numbers of transition forms and spheres are present at the point of maximum turbidity, while spheres predominate at lower salt concentrations. Cells suspended in 3.0 M salt, although slightly swollen, are viable, but viability decreases rapidly with the more drastic changes in morphology at lower salt concentrations. Cells grown in the presence of iron are more resistant to morphological changes but follow the same sequence. Cells "fixed" with formaldehyde, at any point in the sequence, act as osmometers and do not rupture in distilled water although their volume increases 10–14 times. The results indicate that the red halophilic rods require a high sodium chloride content in their growth or suspending medium to maintain a rigid cell wall structure.

scholarly journals Effect of Xanthan and Arabic Gums on Foaming Properties of Pumpkin (Cucurbita pepo) Seed Protein Isolate

2013 ◽  
Vol 3 (1) ◽  
pp. 87 ◽  
Author(s):  
Quirino Dawa ◽  
Yufei Hua ◽  
Moses Vernonxious Madalitso Chamba ◽  
Kingsley George Masamba ◽  
Caimeng Zhang
Keyword(s):  
Sodium Chloride ◽  
Salt Concentration ◽  
Seed Protein ◽  
Foam Stability ◽  
Chloride Concentration ◽  
Egg White ◽  
Protein Isolate ◽  
Foaming Properties ◽  
Ph Optimum ◽  
Pumpkin Seed

<p>Understanding how foaming properties of proteins are affected by factors such as pH, salt concentration and temperature is essential in predicting their performance and utilisation. In this study, the effects of pH and salt concentration were studied on the foaming properties of pumpkin seed protein isolate (PSPI) and PSPI- xanthan (XG)/Arabic (GA) gum blends. The foaming properties of the PSPI-GA/XG blends were also compared with egg white. Foam stability (FS) was significantly affected by pH with PSPI: GA (25:4) and PSPI: XG (25:1) having a significantly higher stability at pH 2 with the lowest foam stability at pH 4. Sodium chloride (0.2-1.0 M) did not significantly affect foaming properties although PSPI: GA (25:4) had the highest FC (89.33 ± 3.24%) and FS (76.83 ± 1.53 min) at 0.2 M sodium chloride concentration. The foaming capacity (FC) of PSPI: GA (25:4) blend (128.00 ± 0.91%) was significantly higher (<em>p </em><em>&lt; </em>0<em>.</em>05) than that of egg white (74.00 ± 1.33%) but its FS was significantly lower. It was further revealed that the FC of egg white (74.00 ± 1.33%) was comparable to the PSPI:XG (25:1) blend (74.00 ± 1.46%) but the FS for egg white (480.00 ± 2.67 min) was significantly higher (<em>p </em><em>&lt; </em>0<em>.</em>05) than the FS (116.21 ± 0.86 min) of PSPI:XG (25:1). The foaming properties of PSPI and PSPI-xanthan (XG)/Arabic (GA) blends were significantly affected by pH. Optimum foaming properties, PSPI:XG (25:1) and PSPI:GA (25:4) were observed at pH 2 and heat treatment temperature of 80 ºC.</p>

scholarly journals THE EFFECT OF SALTS ON THE IONISATION OF GELATIN

1930 ◽  
Vol 14 (2) ◽  
pp. 215-222 ◽  
Author(s):  
Kenneth V. Thimann
Keyword(s):  
Sodium Chloride ◽  
Salt Concentration ◽  
Acid Solutions ◽  
Ionic Structure ◽  
Complex Ions ◽  
Similar Action ◽  
Ion Formation ◽  
Copper Chlorides ◽  
Positive Ion ◽  
Complex Ion

The effect of the addition of sodium chloride to gelatin solutions is shown from the Donnan relationship to increase the ionisation of the gelatin, the increase produced in acid solutions reaching a maximum at about 1/1000 molar salt concentration. This effect is attributed to the formation of complex ions. From the similar action of calcium and copper chlorides the effective combining power of gelatin for complex positive ion formation is deduced. The bearing of complex ion formation on the zwitter-ionic structure and solubility phenomena of proteins is pointed out.

scholarly journals Thermal Gelation of Fish Muscle Proteins Treated with Electric Pulses and Air-Blowing.

1995 ◽  
Vol 42 (2) ◽  
pp. 131-136 ◽  
Author(s):  
Shoichiro ISHIZAKI ◽  
Toshiyuki KOHNO ◽  
Munehiko TANAKA ◽  
Takeshi TAGUCHI ◽  
Keishi AMANO
Keyword(s):  
Fish Muscle ◽  
Muscle Proteins ◽  
Electric Pulses ◽  
Thermal Gelation ◽  
Air Blowing

HYDROXYL RADICAL MODIFICATION OF FISH MUSCLE PROTEINS

1994 ◽  
Vol 18 (6) ◽  
pp. 405-425 ◽  
Author(s):  
SUBRAMANIAN SRINIVASAN ◽  
HERBERT O. HULTIN
Keyword(s):  
Hydroxyl Radical ◽  
Fish Muscle ◽  
Muscle Proteins

scholarly journals On the Denaturation of Fish Muscle Proteins by Dehydration

1956 ◽  
Vol 22 (7) ◽  
pp. 433-439 ◽  
Author(s):  
Masao MIGITA ◽  
Juichiro J. MATSUMOTO ◽  
Tomiko SAISHU
Keyword(s):  
Fish Muscle ◽  
Muscle Proteins

PROTEINS IN FISH MUSCLE: 16. ADENOSINETRIPHOSPHATASE ACTIVITY OF COD MYOSIN AND ACTOMYOSIN

1960 ◽  
Vol 38 (12) ◽  
pp. 1437-1447 ◽  
Author(s):  
J. R. Dingle ◽  
J. A. Hines
Keyword(s):  
Skeletal Muscle ◽  
Fish Muscle ◽  
Ionic Concentration ◽  
Rabbit Skeletal Muscle ◽  
Muscle Proteins ◽  
Skeletal Muscle Proteins

The adenosinetriphosphatase (ATPase) activities of actomyosin extracts of prerigor and postrigor cod muscle, and of myosins prepared from them by ultracentrifugation in the presence of ATP, have been measured at ionic concentration 0.1 and pH 7.3. The actomyosin ATPases were strongly activated by Mg++, while those of the myosins were suppressed by Mg++, in agreement with corresponding rabbit skeletal muscle proteins. Ca++ ion also moderately activated the actomyosin ATPases, but had little effect on the myosin ATPases. When actomyosin was precipitated by dilution in the presence of ATP and Mg++, the characteristic activation by Mg++ was lost. The myosin ATPases were very labile.

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