• 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.

• 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.

• 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.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.51 no.4
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• pp.351-361
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• 2018

This study investigated the potential of collagenous protein fractions (CPFs) as functional foods. The specific CPFs studied were recovered from the roe of bastard halibut (BH), Paralichthys olivaceus; skipjack tuna (ST), Katsuwonus pelamis; and yellowfin tuna (YT), Thunnus albacares through the alkaline solubilization process at pH 11 and 12. The buffer capacity, water-holding capacity and solubility of CPFs with pH-shift treatment were significantly better at alkaline pH (10-12) than at acidic pH (2.0). At pH-shift treatment (pH 2 and 12), the foaming capacities of CPFs from ST and YT were improved compared to those of controls, but they were unstable compared to BH CPFs. The emulsifying activity index (EAI, $m^2/g$ protein) of CPFs (controls) was 16.0-21.1 for BH, 20.1-23.9 for ST and 9.3-13.7 for YT (P<0.05). CPFs adjusted to pH 12 showed improved EAI and YT CPFs showed significantly greater emulsifying ability than those from BH and ST. CPFs recovered from fish roe are not only protein sources but also have a wide range of food functionalities, confirming the high availability of fish sausage and surimi-based products as protein or reinforcing materials for functional foods and alternative raw materials.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.23 no.5
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• pp.401-406
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• 1990

In order to assess fish meal as food protein source which contains heat denatured pro-tein, functional properties of fish meal protein to be treated with alkaline were examined. Ratio of fish meal to 0.2N NaOH solution for extract solvent which were 1:10 showed good results of extracted and recovered amount of fish meal protein. pH 4.5, solubility of protein treated with alkaline revealed the lowest value. Until concentrations of alkaline treated protein solution reached $0.7\%$, its emulsifying capacity steeply decreased. Emusifying capacity of alkali treated protein were higher value at pH 9.0 than pH 4.0 and 7.0, and also were higher quantity in 0.5M NaCl solution than that of 0.1M. Heating time of fish meal protein to be treated with alkaline reached until 30 mins, its fat binding capacity indicated little change and that of heating time 60 mins decreased. Gel forming concentrations of fish meal protein to be treated with alkali for 15 mins or less were $20\%$ but those of 30 and 60 mins were $25\%$. When treating time of fish meal protein with alkali solution reached till 20 mins, viscosity of alkali treated protein solution steeply decreased.

• 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 the Korean Society of Food Science and Nutrition
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• v.35 no.10
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• pp.1394-1398
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• 2006

Functionalities of drum-dried fish muscle protein from pH shifting process have been investigated by determining solubility, emulsion activity, rehydration, fat-adsorption capacity, viscosity, and color. Solubility was higher in recovered protein at pH 7.0 than that at pH 5.5, and not dependent on ionic strength. Solubility of the dried protein recovered at pH 7.0 depended on pH of solvent, and lowest in the range of pH 3 to pH 6. The dried protein showed relatively low emulsion capacity in all the samples. Emulsion stability, foam capacity and foam stability were not observed in the samples. Viscosity was in the range of $50,200\sim39,000cP$. Rehydration and fat-binding capacities were $2.63\sim2.89g$-water/g and $2.13\sim2.17g$-oil/g, respectively, and not dependent on particle size and pH. Drum-dried fish muscle protein has a potential application as an ingredient of meat patty products.

• Asian-Australasian Journal of Animal Sciences
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• v.8 no.5
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• pp.433-441
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• 1995

A series of experiments was conducted to determine the influence of various pepsin-HCL pretreatment factor, hereby the factors of duration of washing for the retrieved bags, inherent to the mobile nylon bag technique (MNBT), on apparent ileal digestibility of crude protein (AIDCP) and apparent ileal digestibility of dry matter (AIDDM). At last, the AIDCP and apparent ileal digestibility of amino acids (AIDAA) in maize, barley, wheat, rapeseed meal, cottonseed meal and three mixed diets were determined with the MNBT and ileo-rectal anastomis pigs (IRAT). For the MNBT techniques, bag measuring $25{\times}40$ MM and containing 0.75 g feedstuff samples, after pre-digestion in vitro, were introduced into the ileo-rectal anastomis pigs (IRAT) gastrointestinal tract through a duodenal cannula and recovered in the ileal digesta between 6 and 12 h. later. 1. The apparent ileal digestibility of dry matter (AIDDM) and crude protein (AIDCP) of the tested samples, with the exception of fish meal, determined by MNBT were not affected by the different pepsin-HCL pretreatment times in vitro between 2.5 h. and 4 h. 2. There was no significant (p > 0.05) difference of the AIDCP and AIDDM of maize determined by the MNBT among different pepsin concentration (0.03%, 0.07% and 0.1 %) treatment in vitro. 3. The AIDCP determined with the MNBT was affected by the washed and unwashed recovered bags from the ileal digesta. 4. The AIDCP and AID amino acids (AIDAA) of maize, barley, wheat, rapeseed meal, soya-bean meal, cottonseed meal and three mixed diets from the MNBT, with a solution of 0.01N HCL (PH 2) and 0.1% of pepsin concentration, a pepsin-HCL pretreatment time in vitro or 4h. and a washing time of the recovered bag from the ileal digesta compared well with those from the IRAT. The linear regression analysis showed a significant correlation (p < 0.01) of AIDCP and AIDDA between the IRAT and MNBT.