• Korean Journal of Food Science and Technology
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• v.28 no.4
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• pp.750-755
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• 1996

Citrus juice was treated with supercritical carbon dioxide $(SC-CO_{2})$ and the effect of temperature and pressure on quality of citrus juice was determined. Pectinesterase (PE) was inactivated by $(SC-CO_{2})$ below temperatures necessary for thermal inactivation. There was no significant change in the pH, Brix and total acidity of citrus juice before and after $(SC-CO_{2})$ treatment, but brightness was improved. More ascorbic acid was retained during $(SC-CO_{2})$ treatment of citrus juice than thermal treatment $(93^{\circ}C/0.66\;min)$.During storage of supercritically treated citrus juice at $4^{\circ}C$, activity of PE was reversible. Sensory evaluation showed that color, flavor, taste and overall acceptance of $(SC-CO_{2})$ treated juice were not significantly different from untreated juice. This method offers potentially beneficial processing avenues for citrus juice and other juices, especially in the area of minimally processed products.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.23 no.2
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• pp.109-124
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• 1990

A rapid processing method for fish sauce of high quality stability and favorable flavor was investigated using mackerel waste as starting material. The chopped waste was homogenized with water and hydrolyzed by commercial proteolytic enzymes such as Complex enzyme-2000($2.18\cdot10^4$ U/g solid, Pacific Chem. Co.) and Alcalase ($1.94\cdot10^4$ U/g solid, Novo) in a cylindrical vessel with 4 baffles and 6-bladed turbine impeller. Optimal pH and temperature for the hydrolysis with Complex enzyme-2000 were 8.0 and $50^{\circ}C$, and those with Alcalase were 9.0 and $55^{\circ}C$. In both cases, the reasonabe amount of added water and enzyme concentration based on the waste weight were $40\%,\;3\%$ and hydrolyzing time was 100 min. Thermal treatment of the hydrolysate with $6\%$ of invert sugar for 2 hours at $90^{\circ}C$ was adequated to inactivation of the enzymes and pasteurization of the hydrolysate. Flavor, taste and color of the hydrolysate were improved during the thermal treatment in which the browning reaction products might participate and result in antioxidative and bactericidal effects. Combined use of $0.005\%$ of Caryophylli flos with $6\%$ of invert sugar was also effective for the improvement of taste. Yield of the fish sauce based on the total nitrogen of the raw waste was $93.7\~94.9\%$, and $87.6\~87.9\%$ of the total nitrogen in the fish sauce was in the from of amino nitrogen. The pH, salinity and histamine content of the fish sauce prepared with $15\%$ of table salt were $6.1\~6.2$, $14.0\~14.5\%$ and less than $10mg\%$, respectively. The fish sauce was stable on bacterial growth during the storage of 60 days at $26\pm3^{\circ}C$ and the quality was also maintained.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.19 no.1
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• pp.10-19
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• 1986

A study on the rapid fermentation of fish sauce has been carried out for effective utilization of sardine. The frozen sardine was thawed at room temperature, chopped, homogenized with equal amount of water and then hydrolyzed by addition of commercial proteolytic enzymes such as bromelain, papaya protease, ficin and a enzyme mixture under different conditions of hydrolysis. The effect of wheat gluten for masking fishy odor and color development during thermal treatment were also tested. The reaction mixture was heated for 30 minutes at $100^{\circ}C$ for enzyme inactivation, pasteurization and color development and then centrifuged for 20 minutes at 4,000 rpm. Finally, table salt and benzoic acid were added for bacteriostatic effect. The results were summarized as follows ; 1. The hydrolyzing temperature, time, pH and the concentration of enzymes based on the weight of whole sardine for optimal hydrolysis were as follows: autolysis, $52.5^{\circ}C$, 4 hours, pH 8.0: with $0.25\%$ bromelain, $52.5^{\circ}C$, 4 hours, pH 6.6 :with $0.25\%$ ficin, $52.5^{\circ}C$, 4 hours, pH 6.8: with $0.3\%$ papaya protease, $52.5^{\circ}C$, 4 hours, pH 6.6: with $6\%$ enzyme mixture, $52.5^{\circ}C$, 4 hours, pH 6.9, respectively. But pH control was not much beneficial in increasing yield. 2. The hydrolytic reaction of chopped sardine with proteolytic enzymes could be interpreted as a first order reaction that devided into 2 periods with different reaction rate constsnts. $Q_{10}$ values of the first period prior to 4 hours were 1.23 to 1.31, and those of post 4 hours were 1.25 to 1.55. The corresponding activation energies were $1.81{\times}10^4\;to\;2.34{\times}10^4\;kJ/kmol$ and $1.92{\times}10^4\;to\;3.77{\times}10^4\;kJ/kmol$, respectively. 3. The reasonable amount of $75\%$ vital wheat gluten for addition was $9\%$ of chopped sardine. 4. The dark brown color was mainly developed during the thermal treatment for 30 minutes at $100^{\circ}C$ and not changed during storage.

• Korean Journal of Food Science and Technology
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• v.16 no.2
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• pp.235-241
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• 1984

Two fractions of pectinesterase from Chinese cabbage were isolated by ammonium sulfate fractionation, ion exchange chromatography on DEAE-cellulose and Sephadex G-150 gel filtration. The fraction F-A and F-B were purified approximately 340- and 10-fold. The similar salt effects and pH optima (pH 7.5-8.0) were obtained for the two pectinesterase fractions. The maximum activity of both two. fractions were obtained at 20-50mM of divalent rations and at 250mM of monovalent rations. The apparent Michaelis constant of the F-A was 0.01% for citrus pectin. The temperature optima for F-A and F-B were $48^{\circ}$ and $55^{\circ}C$, respectively and both fractions were stable in the region of pH 5.0-8.0 at room temperature. The thermal inactivation of the two fractions followed the first order reaction kinetics. From D and Z-values obtained the thermal resistance of the two fractions were characterized.

• Journal of Animal Science and Technology
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• v.46 no.5
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• pp.871-878
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• 2004

Pulsed electric fields(PEF) technology is one of the latest nonthermal methods of food processing for obtaining safe and minimally processed foods. This technology can be effectively explored for obtaining safe food with minimum effect on nutritional, flavor, rheological and sensory qualities of food products. The process involves the application of high voltage(typically 20 ${\sim}$ 80 kv/cm) to foods placed between two electrodes. The mode of inactivation of microorganism; by PEP processing has been postulated in term; of electric breakdown and electroporation. The extent of destruction of microorganisms in PEF processing depends mainly on the electric field strength of the pulses and treatment time. For each cell types, a specific critical electric field strength and specific critical treatment time are required depending on the cell characteristics and the type and strength of the medium where they have been present. The effect also depends on the types of microorganisms and their phase of growth. A careful combination of processing parameters has to be selected for effective processing. The potential applications of PEF technology are numerous ranging from biotechnology to food preservation. With respect to food processing, it has already been established that, the technology is non-thermal in nature, economical and energy efficient, besides providing minimally processed foods. This article gives a brief overview of this technology for food processing applications.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.18 no.5
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• pp.455-463
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• 1985

Thermal-denaturation of myofibrillar protein of dorsal skeletal muscle from file fish was investigated by measuring denaturation constant($K_D$) and thermodynamic parameters at various temperatures. The protective effects of sucrose, sorbitol and amino acids when added individually or combined were also discussed. The denaturation rate as reflected in inactivation of myofibrillar protein Ca-ATPase was followed the first order reaction. The $K_D$ values at $25^{\circ}C,\;30^{\circ}C,\;and\;35^{\circ}C$ were $19.52{\times}10^{-5},\;112.25{\times}10^{-5},\;and\;247.20{\times}10^{-5}$, respectively. The activation energy of the reaction at $30^{\circ}C$ was 43 kcal/mole. The protective effects of sucrose, sorbitol, glycine, alanine and Na-glutamate were increased with the concentration but the effects of sorbitol and Na-glutamate decreased beyond 1.0 mole. Basic amino acids such as arginine and lysine did not revealed any protective effect on the thermal denaturation. In case of mixed addition, the effects of Na-glutamate to glycine, sorbitol to glycine, and sorbitol to sucrose or sorbitol to Na-glutamate were enhanced 1.2 to 7.0 times as much as that of control (ratio of mixing; 1:1, range of concentration; 0.5 to 1.25 mole). Under the frozen condition at $-20^{\circ}C$, two mixtures such as Na-glutamate to glycine and sorbitol to sucrose apparently revealed the protective effects.

• Korean Journal of Food Science and Technology
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• v.30 no.3
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• pp.630-637
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• 1998

Enzymatic properties of immobilized transglucosidase (TG) from Aspergillus niger was characterized and compared with soluble TG. Michaelis-Menten constant $(K_m)$ and maximum velocity $(V_{max})$ of immobilized TG were $122\;mM,\;3.9{\times}10^{-2}\;mM/min$ and in case of soluble TG, 21 mM, 0.4 mM/min. The optimum pH of immobilized TG was pH 5.0 like soluble TG but immobilized TG showed 16% and 45% higher activity than soluble TG at pH 5.0 and pH 6.0. Both of immobilized TG and soluble TG were stable from pH 2.0 to pH 9.0, and therefore their activities in these pH ranges were remained more than 90%. The temperature was optimal at $60{\sim}70^{\circ}C\;and\;70{\sim}80^{\circ}C$ for soluble TG and immobilized TG, respectively. The thermal stability of immobilized TG was significantly improved than that of soluble TG, and immobilized TG retained $32{\sim}40%$ higher activity than soluble TG. D-values from thermal inactivation of immobilized TG were 7690 sec at $65^{\circ}C$, 83 sec at $75^{\circ}C$, 7.2 sec at $80^{\circ}C$. Z-values of soluble and immobilized TG were $6.4^{\circ}C\;and\;5.3^{\circ}C$, respectively. The little difference of activation energies of soluble TG and immobilized TG supposed that there was little difference in mass transfer limitation during the reaction of soluble TG and immobilized TG.

• Korean journal of applied entomology
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• v.15 no.3 s.28
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• pp.137-145
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• 1976

Orchids have been propagated vegetatively for a long time without adequate control measures against virus diseases in Korea. As a result, it is presumed that most of the orchid varieties in Korea may have been degenerated. Nevertheless there has been little work on the virus diseases of orchids in Korea. Therefore studies were initiated to isolate an4 characterize the orchid viruses occurring in Korea. The results obtained are summerized as follows. 1. Symptoms of virus diseases on orchid varieties can be grouped 1) mosaic, 2) necrotic streak with mosaic, 3) ring necrosis, 4) chlorotkc ring and 5) necrotic spot. 2. A total of 102 orchid plants representing 4 genera were investigated on the occurrence of Cymbidium mosaic virus and tobacco mosaic virus by serological agar-gel double diffusion test. The test revealed that approximately $45\%$ of the orchids were infected with Cymbidium mosaic virus. None of the plants were found to be infected with tobacco mosaic virus. 3. Local lesions appeared on the inoculated leaves of Chenopodium amaranticolor Cassia occidentalis and Datura stramonium 7-12 days after mechanical inoculation with Cymbidium mosaic virus. 4. Physical properties of the Cymbidium mosaic virus determined by inoculation on Chenopodium amaranticolor were as follows: Thermal inactivation Point; $75-80^{\circ}C$, dilution end Point; $10^{-5}-10^{-6}\%$ aging in vitro; 8 days. 5. Three different buffers at pH 7.0 and pH 9.0 were compared for the efficiency of agar-gel double diffusion test with Cymbidium mosaic virus. Phosphate, imidazol and tris buffer at pH 7.0 gave equally satisfactory results. 6. Electron microscopic examination of the Cymbidium mosaic virus revealed rod shaped particles measuring 460-580mu.

• Clean Technology
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• v.22 no.3
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• pp.175-180
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• 2016

Tyrosinases catalyze the hydroxylation of a monophenol (monophenolase activity) and the conversion of an o-diphenol to o-quinone (diphenolase activity), which are mainly involved in the modification of tyrosine residues into 3,4-dihydroxyphenyl-alanine (DOPA) and DOPA/DOPAquinone-derived intermolecular cross-linking. Previously, we obtained a slightly acidic and cold-active tyrosinase, tyrosinase-CNK, by our recombinant protein approach. The enzyme showed optimal activity at pH 6.0 and 20 ℃ with an abnormally high monophenolase/diphenolase activity ratio and still had approximately 50% activity compared with the highest activity even in ice water. Here, we investigated reaction stability of the recombinant tyrosinase-CNK as a psychrophilic enzyme. The enzyme showed remarkable thermal stability at 0 ℃ and the activity was well conserved in repeated freeze-thaw cycles. Although water-miscible organic solvent as reaction media caused the activity decrease of tyrosinase-CNK as expected, the enzyme activity was not additionally decreased with increased concentration in organic solvents such as ethanol and acetonitrile. Also, the enzyme showed high salt tolerance in chaotropic salts. It was remarkably considered that 2⁺ metal ions might inhibit the incorporation of Cu²⁺ into the active site. We expect that these results could be used to design tyrosinase-mediated enzymatic reaction at low temperature for the production of catechols through minimizing unwanted self-oxidation and enzyme inactivation.

• Korean Journal Plant Pathology
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• v.1 no.1
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• pp.3-11
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• 1985

Three mild mutant strains of tobacco mosaic virus (TMV) were isolated from Nicotiana tabacum var. Samsun incubated at $38^{\circ}C$ for 10 days after inoculation with a wild type of TMV-OM strain. They were designated into Tg 5272, Tw 227 and Tw 333. All mild strains could be distinguished from TMV-OM by their reactions on different indicator plants. The mild strains induced the mild mottling without distinct symptoms, whereas the wild strain produced severe mosaic, rugose and stunting on tobacco and red pepper plants. Tw 227 and Tw 333 produced smaller necrotic spots than those of Tg 5272 and TMV-OM on N. glutinosa and Datura stramonium. The former two strains also produced ring spots and mosaic on Gomphrena globosa compared with necrotic spots by the latter strains. Three mild strains were serologically identical to TMV-OM. Their physical properties were thermal inactivation point $80-85^{\circ}C$, dilution end point between $10^{-4}\;and\;10^{-6}$, and longevity in vitro 7days or longer. Ultraviolet absorption spectra of purified preparations of the mild strains and TMV-OM were identical, with a minimum at 247nm, a maximum at 260nm, and a slight shoulder at 290nm. Electrophoresis of the strains in polyacrylamide-agarose gel showed that all the strains formed one major band and two minor bands, except for one minor band of Tw 333. However, when sodium dodecyl sulfate was added to the purified viruses before electrophoresis, each strain formed only one major band.