• Korean Journal of Fisheries and Aquatic Sciences
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• v.40 no.6
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• pp.337-342
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• 2007

The formation of lysinoalanine (LAL) in protein recovered from the belanger's croaker, Johnius grypotus, using a pH shifting process was measured by amino acid analysis. The LAL peak was detected at 49.24 min, between phenylalanine and histidine peaks in the amino acid analyzer. LAL was not detected in the fish muscle or in protein recovered using the alkaline pH shifting process. LAL was not formed in protein recovered after storage for up to 9 hrs at pH 11, but was detected in the soluble protein fraction at pH 11, followed heating at $90\;^{\circ}C$. The myosin heavy chain decreased with storage time at pH 11. The results suggest that the alkaline shifting process for recovering fish muscle protein is safe, and that no LAL forms.

• Food Science of Animal Resources
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• v.39 no.3
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• pp.503-509
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• 2019

The aim of this study was to compare the effects of number of washes and salt addition on the meat quality in protein recovered from Alaska Pollock compared with pork leg. Various properties of protein recovered from Alaska Pollock (C, washed twice, no salt) and pork leg (T1, washed twice, no salt; T2, two washes, salt added; T3, washed four times, no salt; and T4, washed four times, salt added) were assessed in this study. Pork leg samples exhibited better color (more whiteness, less yellowness) than Alaska Pollock samples. In pork leg samples, four washes (T3, T4) during processing yielded whiter, less yellow protein than two washes (T1, T2). Overall, the textural property measures were higher in pork leg samples (T2, T3, and T4) than in other samples. Breaking force, jelly strength, and folding resistance were significantly higher in salt-treated pork leg samples (T2, T4) than in the other samples. Our findings demonstrate that protein recovered from pork leg has better color parameters, and physical strength compared with Alaska Pollock-derived protein. A higher number of wash steps and treatment with salt during processing were furthermore found to yield better color, and physical strength in the protein samples.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.36 no.3
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• pp.204-209
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• 2003

Utilization of soluble protein recovered from surimi wastewater using calcium powder of cuttle bone were examined. The crude ash content of the heat-induced surimi gel was increased linearly by increasing substitution ratio of recovered protein-ATC toward commercial surimi. Moisture (approximately $76\%$) and lipid $(0.2\%)$ contents were not change, but their protein contents were decreased 15.7 to $14.3\%$ depend on increasing of substitution ratio. The white index of the heat-induced surimi gel by color meter was increased up to $10\%$ of substitution ratio. There were no difference between $0\%\;and\;5\%$ substituted surimi gel in the gel strength. The sensory score on white index and texture of the heat-induced surimi gel did not change in 0 to $10\%$ as a substitution ratio of recovered protein-ATC toward commercial surimi, while decreased in more $15\%.$ The optimal substitution ratio of recovered protein-ATC as a bulking agent was $10\%.$ The heat-induced surimi gel prepared with $10\%$ substitution of recovered protein-ATC was similar to the content and composition of total amino. acids, and superior to calcium content and the ratio of calcium and phosphorus toward those of commercial surimi.

• Journal of the Korean Society of Food Science and Nutrition
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• v.35 no.7
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• pp.903-907
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• 2006

Frozen stability of proteins recovered from white croaker and jack mackerel have been tested by measuring oxidation of residual lipid, browning, total plate count, and texture of gel during storage at $-20^{\circ}C$. The oxidation of residual lipid in recovered protein from Jack mackerel increased up to 60 days, and then decreased. Both browning values significantly was increased after 90 days. Total plate count was $1.2{\times}10^4\;CPU/g$ for proteins recovered from white croaker and $3.2{\times}10^4\;CPU/g$ for proteins recovered from jack mackerel in 60 days. The breaking force, deformation, and whiteness of gel formed from proteins recovered from white croaker did not change up th 120 days significantly, while proteins recovered from jack mackerel did not form heat-induced gel in 120 day. Frozen storage of the recovered protein was limited to 90 days for white croaker and to 60 days for jack mackerel considering the gelling ability and textural properties.

• Journal of the Korean Society of Food Science and Nutrition
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• v.33 no.10
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• pp.1676-1684
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• 2004

Gel properties of recovered protein from mackerel, frozen blackspotted croaker, chicken breast and pork leg using acidic and alkaline processing were evaluated. Myofibrillar protein from mackerel by acidic processing did not form a heat-induced gel. However, the recovered protein including sarcoplasmic protein formed heatinduced gel. Breaking force of gel from mackerel processed at pH 10.5 was the lowest. A deformation value of frozen blackspotted croaker was the highest, followed by chicken breast, pork leg and mackerel. Whiteness of frozen blackspotted croaker was the highest among heat-induced gel. Breaking force, deformation and whiteness were decreased by addition of recovered protein from mackerel, but price was increased. A breaking force and whiteness of heat-induced gel added recovered protein from chicken breast were increased, and the price was greatly decreased. When the constraint of breaking force, deformation and price of raw material were set up above 110 g, 4.5 mm and below 2,000 won/kg. A optimum formulation for blending protein was 36∼50% for frozen blackspotted croaker, 34∼40% for chicken breast, 14∼25% for pork leg. The heat-induced gel of recovered protein from frozen blackspotted croaker showed compact structure compared to that of recovered protein from mackerel. A formulation of chicken breast and pork leg based on blackspotted croaker can be used in surimi based seafood products having various texture.

• Journal of the Korean Society of Food Science and Nutrition
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• v.33 no.10
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• pp.1668-1675
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• 2004

The effect of pH on surface hydrophobicity, sulfhydryl group, infrared spectrum, SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) pattern and enthalpy was investigated in recovered protein from mackerel and frozen blackspotted croaker by alkaline processing. Hydrophobic residue in myofibrillar protein exposed to the surface of protein, and hydrophobic interaction were the highest around 6$0^{\circ}C$. The surface hydrophobicity was different between myofibrillar protein and myofibrillar protein including sarcoplasmic protein (recovered protein). The peak at 1636 c $m^{-l}$ was increased with pH, and the recovered protein was unfolded in alkali pH. Difference of surface and total sulfhydryl group at pH 7.0 and 10 was comparative high, and decrease of surface sulfhydryl group indicated formation of S-S bonds. Mackerel and frozen blackspotted croaker in alkaline pH showed bands of polymerized myosin heavy chain on SDS-PAGE pattern. The transition temperatures of recovered protein were 33.1, 44.3 and 65.5$^{\circ}C$. Gelation of recovered protein from alkali processing was estimated by increase of $\beta$-sheet structure by pH treatment, S-S bonds by oxidation of surface sulfhydryl group in heating, polymerization of myosin heavy chain in order.r.

• Journal of Life Science
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• v.18 no.6
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• pp.832-838
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• 2008

Mackerel water-soluble protein fraction produced by washing the mackerel meat were concentrated by isoelectric point shifting precipitation process, and the concentrates were utilized as the alternative feed of fish meal. In the 1st aquaculture diet experiment for Israel common carp, the feed conversion ratio decreased in proportion to the rise in the percentage of the recovered protein containing a residual lipid, which was added to the fish meal. It was supposed that the low feed efficiency was because of lipid oxidation in the recovered protein fraction. In addition, 2nd aquaculture diet experiment for Israel common carp was conducted after removing the oxidized lipid in the recovered protein fish meal. When a portion of the fish meal was substituted by the recovered protein devoid of the residual lipid, the feed conversion ratio increased in proportion to the amount of the substitute being added to the fish meal. Therefore, the recovered protein fraction of the mackerel washing wastewater from mackerel processing factory could be used as the alternative feed of fish meal.

• Journal of the Korean Society of Food Science and Nutrition
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• v.35 no.8
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• pp.1045-1050
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• 2006

Optimum operation condition for pilot scale of alkaline processing for fish muscle was investigated by measuring protein solubility, yield, texture, and water-holding capacity. Recovered protein yield was 33.2% for whole fish and 61.8% for minced muscle. Optimum homogenized speed and time, using industrial scale homogenizer, were 3,000 rpm and 5 min, respectively. Limited centrifugal force of continuous cylinder type was 4,000 rpm for recovering soluble protein, and 2,000 rpm for recovering precipitated proteins. The pH control agents such as citric acid, sodium phosphate and calcium oxide decreased the breaking force and deformation of recovered protein gel. The breaking force and deformation of the recovered proteins were high compared to conventional surimi. The breaking force and deformation were decreased by addition of salt, starch and bovine plasma proteins. Whiteness of recovered protein gel was lower than that of conventional surimi. Alkaline processing greatly decreased nitrogen content and chemical oxygen demand in waste water. The results suggest that alkaline processing has a potential as industrial production for recovering the proteins from fish muscle.

• The Korean Journal of Food And Nutrition
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• v.9 no.3
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• pp.319-324
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• 1996

The functional properties of protein recovered from red crab (Chitinonecetes opiiie) processing in water (RCP) were examined and compared with those of soybean protein isolate at pH 2~10 in water and NaCl solu5ion. The solubilities of RCP and SPI were miniumu at pH 4, the isoelectric point and increased significantly at lower or higher than pH 4. Solubilities in NaCl solution for both proteins decreased with incr NaCl concentration increase at all pH ranges. Emulsion capacity for both proteins was also minimum at pH 4 and increased as protein concentration increased from 2 to 6%. Emulsion capacity of RCP was higher than these of SPI at pH 6∼10 and all protein concentrations. Emulsion stability showed a similar trend to that of emulsion capacity. RCP had higher oft absorption capacity and lower water absorption capacity than SPI.

• Biomolecules & Therapeutics
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• v.7 no.1
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• pp.1-6
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• 1999

Effects of Panax ginseng on the morphine toxicity were studied in relation to its effects on the opioid receptor-G protein interactions. Morphine treatments (3 days) reduced the body weight increment rate and the weight of the thymus and spleen. These changes were usually recovered by the concomitant administration of ginseng total saponin (GTS) but occasionally further deteriorated. This discrepancy was studied in relation to the opioid receptor coupling to G protein, that is, the effects of morphine and GTS on the opioid receptors were studied using the antagonist-agonist competitive binding studies. When GTS recovered the morphine toxicity, morphine shifted the striatal $\delta$ receptors to slightly higher affinity state, and this was partly recovered by the GTS treatment. However, morphine did not have any effect on the affinity state of $\delta$ receptor from NG108-15 cells, suggesting that additional factors were needed for the modulation of the affinity states of $\delta$ receptor. Effects of morphine and GTS on $\mu$ receptor were complicate and variable, and we could not reach a clear conclusion. The morphine toxicity might accompany complicate biological involvements, and the modulation of the affinity states of the opioid receptors might explain a part of the effects of GTS on the morphine toxicity.