• Korean Journal of Food Science and Technology
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• v.25 no.4
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• pp.327-333
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• 1993

The processing conditions and quality of sardine surimi were examined: Raw sardine meat was separated, washed in 0.2% $NaHCO_3$ and 0.15% NaCl solution, and then dewatered by centrifuge. The dewatered sardine meat was chopped, mixed with 20% emulsion curd (soybean protein : water : refined sardine oil=1:5:2.6), 4% sorbitol, 4% sucrose, 0.2% polyphosphate and 0.1% sodium erythorbate by stone mortar. The mixed sardine meat was frozen with contact freezer, packed in carton box and then stored at $-25{\pm}2^{\circ}C$. The moisture, crude protein and lipid contents of the sardine surimi product was 73.3%, 15.0% and 6.9%, respectively. Fatty acid composition of product consisted of 28.8% of saturates, 24.3% of monoenes and 47.7% of polyenes and the major fatty acids were 16:0, 20:5, 18:1, 22:6 and 16:1. The results of changes in POV, TBA value, fatty acids, texture and sensory score of products during frozen storage showed that lipid oxidation and freeze denaturation of product could be retarded, and flavor enhanced by addition 20% emulsion curd and 0.1% sodium erythorbate. In an attempt to apply sardine surimi in producing surimi-based product, it was concluded that pollack surimi could be substituted with sardine surimi up to 40% without showing any significant changes in texture and taste of surimi-based product.

• Journal of the Korean Chemical Society
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• v.29 no.1
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• pp.31-37
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• 1985

N-Acetyl-1-phenylalanyl-1-phenylalanine methyl ester (APhPhMe), N-acetyl-l-phenylalanine methyl ester (APhMe) and N-acetyl-1-phenylalanyl-1-alanine methyl ester (APhAlMe) were used as model compounds to investigate a protein denaturation under various temperatures and pressures. Overall, the solubility of APhPhMe in water increased with increasing pressure and that of APhMe decreased. However, the solubility of APhAlMe was nearly same. The values of volume change of APhPhMe were -0.9, -1.47, -1.09, -1.52 ml/mole at 20, 30, 40 and 50$^{\circ}C$, respectively, and those of APhMe were +6.0, +7.0, +7.5 ml/mole at 20, 30 and 40$^{\circ}C$, respectively. But those of APhAlMe were nearly zero at the measured temperature. The experimental result seems to be explained by the hydrophobic interaction and hydrogen bond of peptide bonds. In the compounds which have only peptide bonds and which have both a pretty large hydrophobic group and a peptide bond in the molecules, the hydrogen bond between peptide bonds is more dominant than the hydrophobic interaction. However, when the number of peptide bond and hydrophobic group increase simultaneously, the hydrophobic interaction seems to be more dominant.

• Korean Journal of Food Science and Technology
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• v.26 no.4
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• pp.436-441
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• 1994

To investigate the lowering effects of in vitro enzymatic hydrolysis by the treatment of chymotrypsin, trypsin, pancreatin, or protease from Aspergillus oryzae on the antigenicity of whey protein isolate (WPI) against rabbit anti ${\alpha}-LA$ antiserum, competitive inhibition ELISA (cELISA) and passive cutaneous anaphylaxis (PCA) test using guinea pig were performed. The results of cELISA showed that the monovalent antigenicity of the whey protein hydrolysates (WPH) to the antiserum was decreased to $10^{-2.5}-10^{-5.5}$ and less by the hydrolysis. The monovalent antigenicity of the WPH hydrolyzed by trypsin, or protease from Asp. nryzae was much lowered by the pretreatment of heat denaturation. The antigenicity of the WPH hydrolyzed by chymotrypsin, trypsin, or pancreatin was much lowered by the pretreatment of pepsin. Especially, the antigenicity of TDP (trypic hydrolysate with pretreatment of heat and pepsin) was found almost to be removed. However, there was not consistency between degree of hydrolysis(DH) and the monovalent antigenicity of the WPH. By the heterologous PCA it was found that all of the PGPH lost the polyvalent antigenicity regardless of the pretreatments although WPI and ${\alpha}-LA$ had the positive high antigenicity. The results suggested that the peptides derived from ${\alpha}-LA$ in WPH could bind specific antibodies but they could not induce allergy. Therefore, it was elucidated that the allergenicity of ${\alpha}-LA$ in whey protein could be destroyed easily by the enzymatic hydrolysis.

• KSBB Journal
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• v.10 no.1
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• pp.63-70
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• 1995

The effect of operating conditions on separation of soybean proteins in a home-made free-flow electrophoresis apparatus was investigated. Measurement of the pH, conductivity, and UV-absorbance(280 nm) were carried out at each run and the purity of the sample was tested with SDS-PAGE analysis. The soybean extract pretreated with Tris and boric acid was mixed with the amino acids composed of glutamic acid, histidine, arginine, glycine(1 mM each) with glycyl-glycine(2mM) and KCl(1mM). When the cellulose acetate was used as a compartment between the electrode and the buffer solution in the cell, pH distribution in the separation cell varied from 3.0 at the anodic side to 8.0 at the cathodic side and had two inflection point. The applied voltage was from 300V to 1000V and the separation was better at a higher voltage but the voltage was limited by the capability of the cooling system due to Joule heat. The proteins focused near the middle of the channel. From the change of pH and conductivity it was found that the ions in the channel moved out to the electrodes through the membrane. In the case when the concentration of the buffer solution was increased 5 times, proteins were focused at 300V. We could not increase up to the ten times of the concentration since the temperature difference between inlet and outlet was more than $25^{\circ}C$ and denaturation of proteins was expected. When ion-exchange membranes were used U-type pH distribution was set up due to the ionic polarization near the membrane. The commercial ampholytes, instead of the mixed amino acids showed not much improvements in purity of the separated sample.

• Korean Journal of Food Science and Technology
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• v.28 no.4
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• pp.624-631
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• 1996

Effect of fluctuation range and intervals of defrosting temperature on quality of frozen foods stored in a domestic refrigerator equipped with an automatic defrost system was evaluated. As defrost system was operated, temperatures of domestic refrigerators were elevated from $-18^{\circ}C\;to\;-5^{\circ}C\;and\;-15^{\circ}C$, and fluctuation intervals were l6 hrs and 30 hrs, respectively. Quality deterioration such as protein denaturation, vitamin loss, exudate production and changes in appearance of frozen foods was minimized by reducing temperature oscillation during storage. Considerable effects of thermal oscillation on ice crystal sizes were observed for frozen beef tissue and ice cream. TTI (time temperature indicator) system also proved that the temperature control of defrost system in domestic refrigerator can improve the quality of foods during storage.

• Korean Journal of Food Science and Technology
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• v.48 no.6
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• pp.548-554
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• 2016

Since some strains of kimchi lactobacilli can curdle milk, they can be used for making yogurt. However, the best Lactobacillus plantarum strains for curdling milk for yogurt are still unknown. In this study, we determined the best L. plantarum strains for curdling milk, and the physicochemical properties of yogurts made using different L. plantarum strains were examined. Three strains of L. plantarum useful for curdling milk were identified (YD2, YD9, YD12). The number of lactobacilli was lower in yogurts made with L. plantarum than in those made with control, and among the L. plantarum strains tested, YD12 had the highest bacterial counts. However, the microbial count reached $6.3{\times}10^8CFU/mL$ after 24-h fermentation in all yogurts. The pH of the yogurts decreased after 12-h fermentation, while the acidity increased. The low pH and high acidity decreased the viscosity in all the three types of yogurts, because the acids disturbed gel formation due to protein denaturation. Sensory evaluation revealed that the YD12 group showed a high percentage of completion similar to the control group. YD2 and YD9 showed a high sourness value and low sweetness value, whereas YD12 yielded optimal values for all the organoleptic characteristics. Therefore, YD12 would be a high quality bacterial strain for use as a yogurt starter culture.

• Korean Journal of Food Science and Technology
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• v.21 no.4
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• pp.480-485
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• 1989

Changes of color intensity and components during browning reaction of water extracts from white tail ginseng were investigated. Temperature dependence was described by the Arrhenius relationship with an activation energy of 16kcal/mole. Temperature sensitivities$(Q_{10}\;value)$ for water extracts of ginseng was 1.90 between $70^{\circ}C\;and\;80^{\circ}C$, 1.57 between $80^{\circ}C\;and\;90^{\circ}C$ and 1.46 between $90^{\circ}C\;and\;100^{\circ}C$. pH value of the solution treated at $90^{\circ}C\;and\;100^{\circ}C$ slightly increased with an increase in reaction time. Among ginseng saponins ginsenoside-Re was most unstable against heat-treatment, white diol group saponins were more stable against heat-treatment. Hydrogen donating activity (reducing activity for ${\alpha},\;{\alpha}'-diphenyl-{\beta}-picrylhydrazyl$) and 3,5-dinitrosalicylic acid(DNS) positive substances of browning reaction products increased in proportion to the length of browning reaction time and temperature, whereas folin positive substances decreased by heat-denaturation of ginseng protein at initial reaction time and then increased thereafter.

• KSBB Journal
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• v.15 no.6
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• pp.649-657
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• 2000

The factors affecting the back-extraction efficiency of Bovine Serum Albumin (BSA, Mw. 65kDa, pl 4.9) solubilized in an AOT reverse micellar solution, prepared by the injection method, to an excess aqueous phase were investigated. In particular, the effects of pH, the types of salts, alcohols added as cosurfactants, and their concentrations in the aqueous phase were examined. Furthermore, by comparing the CD spectra of the back-extracted BSA and the feed BSA, the structural changes of BSA during the extraction process were determined. The addition of 1:1 salt such as KCl or NaCl to the aqueous phase resulted in almost a 100% extraction to the aqueous phase at a pH higher than its isoelectric point pl. This high efficiency of back-extraction might be due to the change in the interactions between the protein and micellar aggregates driven by the added salt. For 1:2 salts like $CaCl_2$ and $MgCl_2$, BSA was back-extracted with lower than 20% extraction efficiency. Maximum extraction efficiencies were attained at about pH=7 and pH=8 for monovalent and divalent salts, respectively. The addition of alcohols as cosurfactants led to an improvement in monovalent and divalent salts, respectively. From the CD spectra of BSA extracted to the aqueous phase, it was observed that denaturation of BSA was not significant. In certain back-extraction conditions, the extracted BSA showed even higher activity than the feed BSA.

• The Korean Journal of Nuclear Medicine Technology
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• v.16 no.2
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• pp.139-148
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• 2012

Purpose : Since standard solution is the one that knows its exact concentration, the curve of the dissolution has been determined according to the amount of the solution, compared to the amount of the unknown sample. Therefore, the antigen that makes up standard materials should be made in a pure form. The configuration of the standard substance solution in the kit we use is a freeze-dried material, or made and comes as a liquid. Lyophilized reference material is used after dissolving in usually D.W. (Distilled Water), and if the antigen to use is too sensitive, reagents should be freeze-dried. Furthermore, when freeze-dried reference has to be frozen again after being dissolved, it should be kept under $-20^{\circ}C$ until the expiration date according to the reports. Since it is not expressed in the experiment if it is safe or stable to reuse the solution which was dissolved a few times, thus, this time it is tested and evaluated that the changes of the standard solution by freezing and melting several times, and its results and the effectiveness of it were compared to the solution which was kept in a fridge. Materials and Methods : Among Vitro diagnostic kits on the market made by radioimmunoassay, parathyroid hormone (PTH), adrenocorticotropic hormone (ACTH), luteinizing hormone (LH) are made of freeze-dried standard solution and all composed of the same Lot.NO. These hormones melted in D.W. and were separated into three groups. In the first group, melting and freezing were repeated, and in the second group, The solution only for one time use was put into a test tube after melting and freeze it. The third group was kept in the refrigerator. This experiment has been conducted from January to February in 2012. January to 2012. PH test was employed because ph is prone to changing depending on the change of protein. Each group of the standard solution, cpm (counter per minute), and the patient relative concentration values were compared by date, and Through the correlation coefficient and Paired t-test, the significant level of each group was analyzed. Results : ACTH, PTH, LH pH values were too subtle denaturation rather than numerical changes in the protein. In addition, when the standard solution of ACTH, PTH, LH was refrigerated, after 3 days and 7 days, there was a significant difference observed between the solution being kept in a refrigerator and a freezer within a significance level. Conclusion : Standard solution should be kept in a freezer, and being kept in a fridge, it is recommended to use the solution as soon as possible.

• Journal of the Korean Society of Food Science and Nutrition
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• v.39 no.6
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• pp.920-926
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• 2010

Marine alga, Chlorella vulgaris, was extracted by chloroform-methanol (2:1, v/v) solvents for lipid extraction at $35^{\circ}C$ for five hours (HCM-35) and its process was compared with conventional lipid extraction condition such as chloroform-methanol (2:1, v/v) at $65^{\circ}C$ for one hour (CM-65). This low temperature extraction process showed that 80% of total lipid was extracted and its residues contained relatively unchanged amounts of intact proteins and other minerals as well as amino acid profiles. Interestingly enough, the weight fraction of carbohydrate in the residues slightly increased due to less denaturation at low process temperature. The biological activities of the residues such as cytotoxicity and immune cell growth activation were not much changed after being extracted. The sensory evaluation were found to be very favorable for being used as a food additive and/or food supplement. This result could also help to maintain the economic feasibility of utilizing marine resources in food and other relevant industries.