• Journal of the Korean Society of Food Science and Nutrition
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• v.26 no.2
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• pp.180-185
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• 1997

This work was carried out to investigate change of polygalacturonase activities and polygalacturonase patterns by gel filtration chromatography during softening of persimmon and jujube fruits. During softening of two kinds of fruit, polygalacturonase activities of water-soluble and salt-soluble proteins were increased, but that of cell wall-bound proteins was decreased. In water-soluble and salt-soluble proteins of persimmon fruits, two peaks of polygalacturonase activity were separated in mature stages, but one peak in soft stages. During softening of those fruits, the peaks of polygalacturonase activity in water-soluble and salt-soluble proteins appeared on the same fraction with the peaks of polygalacturonase activity in cell wall-bound proteins.

• Korean Journal of Food Science and Technology
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• v.20 no.3
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• pp.371-379
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• 1988

To investigate on the biochemical characteristics of myofibrillar proteins between cold(pollack, salmon) and warm current fish (yellow corbina, shark), myofibrils and actomyosin were prepared, and their biological activities, effect of temperature on the myofibrillar ATPase activities and SDS-polyacrylamide gel electrophoretic patterns of myofibrils were compared. SDS-polyacrylamide gel electrophoretic analysis showed that electrophoretic patterns of myofibril vary from fish to fish. Difference in KCl concentration dependency of myofibrillar ATPase activities and ATPase activity- pH curve were found among fish species. Myofibrillar proteins from cold current fish showed higher specific activity at low temperature $(5^{\circ}C-10^{\circ}C)$ than those from warm current fish.

• Journal of the Korean Society of Food Science and Nutrition
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• v.18 no.3
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• pp.279-286
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• 1989

The alkaline protease producing mold isolated from and identified as Aspergillus fumigatus. It was found that the production of alkaline protease reach to maximum was cultured for 3 days at $30^{\circ}C$. The enzyme was purified 86.13 fold and yield of the enzyme purification was 6.4%, The purification procedure include ammonium sulfate treatment, gelfiltration on Sephadex G-25, G-75, G-150 and DEAE-cellulose ion-exchange chromatography. When the purified enzyme was applied sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the molecular weight was estimated about 63000. This enzyme composed 17 amino acids and main amino acids of this enzyme were glycine and glutamic acid.

• Journal of the Korean Society of Food Science and Nutrition
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• v.12 no.2
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• pp.93-98
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• 1983

Apple sugaring and apple nectar gel were treated with coating agent, and then the rate of weight loss, browning reaction and fungi growth on the storage conditions of those were investigated. The results obtained were summarized as follows; The composition of sucrose, D-sorbitol, corn syrup, gelatin, arabia gum, citric acid, sodium citrate and sodium ascorbate as a nontoxic coating agent was desirable to repress weight loss browning reaction and fungi growth of apple sugaring and apple nectar gel. It was the most effective method that apple sugaring was treated with the coating agent and refrigerated with double packaging. The contraction by weight loss, browning reaction and fungi growth of apple nectar gel treated with the coating agent and freezed with double packaging were repressed.

• Food Science of Animal Resources
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• v.34 no.1
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• pp.122-126
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• 2014

This study was performed to evaluate the effects of chicken breast meat on the quality of mackerel sausages. The mackerel sausages were manufactured by additions of 5%, 7%, and 10% of chicken breast meat. The lightness of mackerel sausages showed no significant differences between the control and addition groups. The redness increased in a dose-dependent manner, but the yellowness decreased significantly with the addition of 7% chicken breast meat (p<0.05). The whiteness value of mackerel sausage added with 7% chicken breast meat was significantly higher than those of the other groups (p<0.05). In texture analysis, the hardness and adhesiveness of the mackerel sausage added with 5% of chicken breast meat showed no significant differences as compared to the control. However, the mackerel sausages added with 7% and 10% of chicken breast meat showed a dose-dependent decrease. The gel strength of the mackerel sausage added with 5% chicken breast meat was not significantly different from the control, but the addition of 7% and 10% chicken breast meat reduced the gel strength of the mackerel sausage. In sensory evaluation, the mackerel sausages prepared with chicken breast meat have higher scores in smell, taste, texture, hardness, chewiness, and overall preference as compared to the no addition group. Therefore, these results suggest that the optimal condition for improving the properties within mackerel sausages was 5% addition of chicken breast meat.

• Korean Journal of Food Science and Technology
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• v.39 no.4
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• pp.438-446
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• 2007

The fermented soybean product, cheonggukjang, is favored by many people, partly due to its bio-functional ingredients. Since the fermentation process of cheonggukjang is mediated by enzymes, including proteases, produced by microbes, analysis of the proteome profile changes in cheonggukjang during fermentation would provide us with valuable information for fermentation optimization, as well as a better understanding of the formation mechanisms of the bio-functional substances. The soluble proteins from cheonggukjang were prepared by a phenol/chloroform extraction method, in order to remove interfering molecules for high resolution 2-D gel analysis. Proteomic analysis of the cheonggukjang different fermentation periods suggested that most of the soluble soy proteins were degraded into smaller forms within 20hr, and many microbial proteins, such as mucilage proteins, dominated the soluble protein fraction. The proteomic profile of cheonggukjang was very different from natto, in terms of the 2-D gel protein profile. Among the separated protein spots on the 2-D gels, 50 proteins from each gel were analyzed by MALDI-TOF MS and PMF for protein identification. Due to database limitations with regard to soy proteins and microbial proteins, identification of the changed proteins during fermentation was restricted to 9 proteins for cheonggukjang and 15 for natto. From de novo sequencing of the proteins by a tandem MS/MS, as well as by database searches using BLASTP, a limited number of proteins were identified with low reliability. However, the 2-D gel analysis of proteins, including protein preparation methods, remains a valuable tool to analyze complex mixtures of proteins entirely. Also, for intensive mass spectrometric analysis, it is also advisable to focus on a few of the interestingly changed proteins in cheonggukjang.

• Asian-Australasian Journal of Animal Sciences
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• v.16 no.2
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• pp.269-276
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• 2003

We studied the gel properties of porcine collagen with microbial transglutaminase (MTGase) as a catalyst. A creep meter was used to measure the mechanical properties of gel. The results showed samples with high concentration of MTGase gelled faster than those with a low concentration of MTGase. The gel strength increased with incubation time and the peaks of breaking strength for 0.1, 0.2 and 0.5% MTGase were obtained at 40, 20 and 10 min incubation time, respectively. According to SDS-PAGE, the MTGase was successfully created a collagen polymer with an increase in molecular weight, whereas no change in formation was shown without MTGase. The sample with 0.5% MTGase began to polymerize after 10 or 20 min incubation at $50^{\circ}C$, and complete polymerization occurred after 40-60 min incubation. Scanning electron microscopic analysis revealed that the gel of porcine collagen in the presence of MTGase produced an extremely well cross-linked network. The differential scanning calorimetric analysis showed the peak thermal transition of porcine collagen gel was at $36^{\circ}C$, and that with MTGase no peak was detected during heating from 20 to $120^{\circ}C$. The melting point of porcine collagen gel could be controlled by MTGase concentration, incubation temperature and protein concentration. Knowledge of the structural and physicochemical properties of porcine collagen gel catalyzed with MTGase could facilitate their use in food products.

• Korean Journal of Food Science and Technology
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• v.23 no.4
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• pp.428-432
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• 1991

This study was carried out to investigate the effect of NaCl, pH and phosphate on the functional properties of a mixed system of plasma protein and myofibrillar proteins. The solubility of plasma protein, myofibrillar protein and the mixture (plasma+myofibrillar protein) increased according to the increase of NaCl concentration ($0{\sim}4%$) and pH $pH4{\sim}8$). The solubility, emulsifying activity and capacity of the mixture were lower than those of plasma protein, whereas higher than those of myofibrillar protein. The gel strength of the mixture and myofibrillar protein showed a significant increase when NaCl concentration was increased from 2 to 3%. The gel strength of myofibrillar protein increased about four times when 0.3% polyphosphate added to the sample containing 2% NaCl, whereas the moisture loss of the mixture and myofibrillar protein decreased significantly. The gel strength of plasma protein, myofibrillar protein and the mixture increased slightly at $3{\sim}5%$ protein concentration, whereas the gel strength of those increased significantly as the protein concentration increased from 5 to 9%.

• Applied Biological Chemistry
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• v.41 no.2
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• pp.175-180
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• 1998

As a part of investigation for quality improvement of surimi gel from fish with a red muscle by addition of calcium-based powder from fish bone, we investigated the processing condition of calcium-fortified mackerel surumi gel and its quality stability during storage at $5^{\circ}C$. Judging from the results of the soluble calcium content and jelly strength, the reasonable addition concentration of calcium-based powder from Alaska pollack bone for improvement of functional properties in surimi gel was revealed 0.9% on the weight basis of the chopped mackerel meat. The soluble calcium content of the calcium-fortified surimi gel (105.0 mg/100 g) was more than that of the ordinary surumi gel (2.9 mg/100 g). During cold storage of calcium-fortified surumi gel, the moisture contents, amino acid compositions, soluble calcium and phosphorus contents were little changed, the pH, volatile basic nitrogen contents, histamine contents, peroxide values and brown pigment formation were slightly increased and viable cell counts and coliform groups were not detected. The calcium-fortified surimi gel was superior in the lysine and calcium contents, EPA and DHA compositions to the ordinary surumi gel. Judging from the results, it was suggested that calcium-fortified surumi gel was nutritive, functional and safety foods.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.44 no.5
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• pp.435-442
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• 2011

This study was conducted to optimize the processing of high quality surimi gel from unmarketable cultured bastard halibut Paralichthys olivaceus. According to endogenous enzyme activity and processing optimization, high quality surimi gel from unmarketable cultured bastard halibut was prepared by mixing 3.0% (w/w) salt, 2.4% (w/w) starch, 5.0% (w/w) egg white and 4.8% (w/w) ice water in a Stephan mixer, set at $5^{\circ}C$ for 24 h, followed by boiling for 30 min, and finally cooling for 30 min. The strength of the surimi gel from unmarketable cultured bastard halibut prepared by the above processing method was $1,257\;g{\times}cm$, which was 33% higher than that of a commercial surimi gel from Alaska pollock, grade SA.