• Applied Biological Chemistry
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• v.39 no.3
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• pp.222-226
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• 1996

Lipoxygenase, peroxidase and catalase activities were determined in tissues and brines of refrigerated dill pickling cucumbers in response to pickling process, storage and $H_2O_2$. Lipoxygenase was almost inactivated within 1 day exposure to dill pickling brine, and then gradually declined during storage. In contrast, peroxidase activity in cucumber tissue decreased steadily for 4 days after exposure to dill pickling brine. Catalase was present in fresh cucumber tissues, but only slight activity was observed after submerging cucumbers in pickling brine. Lipoxygenase, peroxidase and catalase activities were rapidly inactivated in cucumbers exposed to brine containing $H_2O_2$.

• Journal of Environmental Science International
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• v.31 no.3
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• pp.265-274
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• 2022

Lipoxygenase is an enzyme, mainly produced by plants, capable of converting unsaturated fatty acids to fatty acids. It has vast application potential in the food, pharmaceutical and agricultural industries. The aim of this study was to isolate novel lipoxygenase-producing bacteria from the environment and to investigate the lipoxygenase enzymatic properties for industrial production. The strain, NC1, isolated from cultivation soils, was identified as Bacillus subtilis based on the phenotypic characteristics and 16S rRNA gene sequencing. This strain formed a pink color around the colony when cultured on indamine dye formation plates. The production of lipoxygenase by B. subtilis NC1 was influenced by the composition of the medium and linoleic acid concentrations. The optimum temperature and pH for lipoxygenase activity was determined to be 40 ℃ and pH 6, respectively. The enzyme showed relatively high stability at temperatures ranging from 20-50 ℃ and acid-neutral regions. In addition, the lipoxygenase produced by B. subtilis NC1 was able to degrade commercially available oils including sunflower seed oil and Perilla oil. In this study, a useful indigenous bacterium was isolated, and the fundamental physicochemical data of bacterial lipoxygenase giving it industrial potential are presented.

• Korean Journal of Food Science and Technology
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• v.29 no.1
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• pp.145-149
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• 1997

Lipoxygenase activity from brown rice varieties (Tongjinbyeo, Kumohbyeo and Kanchukbyeo) was investigated using spectrophotometric method. In all three varieties, there was an increase in the enzyme activity with the reaction time. Enzyme activity was tested at different concentration of the substrate. The $V_{max}\;and\;K_m$ values of Tongjin, Kumoh and Kanchukbyeo were 57.89, 19.85 and 31.38 units/mg protein and 0.054, 0.045 and 0.035 mM. The study of lipoxygenase activity at different pH levels showed that all the varieties had maximal activities around $pH\;7.0{\sim}7.6$. The enzyme activity and specific activity on milled fractions of different brown rice varieties, fraction II was superior to the other fractions and fraction IV was inferior to the other fractions. As the result of microwave heating for 0, 30, 60 and 90 sec, the enzyme activity and specific activity of all the varieties were decreased by the elapse of heating time.

• The Korean Journal of Physiology and Pharmacology
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• v.2 no.2
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• pp.241-249
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• 1998

Platelet-activating factor(PAF) enhanced interleukin-1(IL-1) activity by the interaction with a specific receptor in rat alveolar macrophages. In this study, we investigated the role of endogenous arachidonate metabolites and intracellular calcium mobilization in the PAF-induced IL-1 activity. Alveolar macrophages were preincubated with 5-lipoxygenase and cyclooxygenase inhibitors 30 min before the addition of PAF and lipopolysaccharide(LPS). After 24h culture, IL-1 activity was measured in the supernate of sample using the thymocyte proliferation assay. Inhibition of 5-lipoxygenase by nordihydroguaiaretic acid and AA-861 completely blocked the PAF-induced enhancement of IL-1 activity with $IC_{50}\;of\;2\;{\mu}M\;and\;5\;{\mu}M$, respectively. In contrast, the inhibition of cyclooxygenase pathway by indomethacin and ibuprofen resulted in the potentiation in PAF-induced IL-1 activity with maximal effect at $1\;{\mu}M\;and\;5\;{\mu}M$, respectively. In addition, leukotriene $B_4$ and prostaglandin $E_2$ production were observed in PAF-stimulated alveolar macrophage culture. As could be expected, 5-lipoxygenase and cyclooxygenase inhibitors abolished PAF- stimulated leukotriene $B_4$ and prostaglandin $E_2$ production, respectively. The effects of PAF on intracellular calcium mobilization in alveolar macrophages were evaluated using the calcium-sensitive dye fura-2 at the single cell level. PAF at any dose between $10^{-16}\;and\;10^{-8}$ M did not increase intracellular calcium. Furthermore, there was no effective change of intracellular calcium level when PAF was added to alveolar macrophages in the presence of LPS or LPS+LTB4, and 4, 24 and 48h after treatment of these stimulants. Together, the results indicate that IL-1 activity induced by PAF is differently regulated through subsequent induction of endogenous 5-lipoxygenase and cyclooxygenase pathways, but not dependent on calcium signalling pathway.

• Applied Biological Chemistry
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• v.46 no.1
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• pp.23-27
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• 2003

Lipoxygenase is the enzyme responsible for the formation of $C_6$-alcohols and $C_6$-aldehydes ($C_6$-compounds), which are well blown contributors to various types of 'green odor' In green tea. Changes in lipoxygenase activity and volatile compounds of green tea leaves were monitored daily during early growing season. The enzyme activity was spectrophotometrically measured using linoleic acid as a substrate. The volatile compounds were extracted through Solid Phase Micro-Extraction, and were subjected to GC and GC-MS analyses. Results showed that lipoxygenase activity and levels of $C_6$-compounds concomitantly increased or decreased during the early growing season, probably caused by the fluctuation in the daily temperature; increase in temperature led to the increase in enzyme activities and $C_6$-compound levels, whereas leaves plucked too early had low volatile compound levels. In this study, optimum plucking time of tea leaves for the production of high quality green tea with a wellbalanced aroma was determined.

• Journal of Applied Biological Chemistry
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• v.42 no.3
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• pp.130-133
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• 1999

Lipoxygenase activities of three cultivars of black rice (Chindo, Suwon-415, Yongkeum-1) were determined using an oxygen polargraphic method to measure oxygen uptake. Studies at different pH levels revealed that the optimum pH was about pH 7.0 for Suwon-415 and pH 7.5 for Chindo and Yongkeum-1. The specific activities of Chindo, Suwon-415 and Yongkeum-1 at optimal pH were 41.0, 27.3, and 29.6 unit/mg-protein, respectively. In all the cultivars, there was an increase in the activity with increase in reaction temperature. Enzyme activity was tested at different concentrations of the substrate. The resulting $K_m$ and $V_{max}$ values of Chindo, Suwon-415, and Youngkeum-1 were 0.059, 0.050, and 0.066 mM and 2020, 2283, and 1616 unit/g-grain, respectively. Enzyme activity decreased at all storage temperatures(25, 4, and $-40^{\circ}C$).

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.6
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• pp.777-784
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• 1993

The bleaching effect of potato lipoxygenase Isoenzymes on ${\beta}-carotene$ was studied. Two lipoxygenase Isoenzymes(LOX-1, LOX-2) from potato tuber were purified by CM-cellulose, DEAE-cellulose ion exchange chromatography. LOX-1 and LOX-2 seemed to have bleaching effect on ${\beta}-carotene$ in the presence of linoleic acid, which the decrease in the formation of conjugated dienes. LOX-2 was founded to have a greater pigment bleaching activity than that of LOX-1.

• Journal of the Korean Society of Food Science and Nutrition
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• v.17 no.3
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• pp.185-190
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• 1988

Soybean lipoxyeenase isozymes were isolated from acetone-defatted soybean seeds(Glycine max [L.] Merr. variety AmSoy) by ammonium sulfate fractionation, eel filtration, and ion exchange chromatoeraphy. The final preparation of lipoxygenase-1 and -2 obtained was 19- and 32-fold purified, respectively, to the crude extract. But a considerable loss of total enzyme activity occurred during purification. On 7% polyacrylamide gel electrophosis at pH 9.0, employing lipoxigenase specific staining technique, lipoxyeenase-1, -2, and -3 showed distinctive Rf values of 0.38, 0.29, and 0.33, respectively.

• The Korean Journal of Food And Nutrition
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• v.9 no.1
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• pp.52-58
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• 1996

This study was carried out 19 investigate the characteristics of pectinesterase (PE), polygalacturonase (PG), lipoxygenase(LOX) and peroxidase (POD) in hot pepper to know the effect of hot pepper on food quality during food processing and storage. The results were as follows : 1. The optimum pH of PE was pH 7.5 and the activity of PE below pH 5.5 was revealed scarcely, The concentration of NaCl and $CaCl_2$ that showed the highest activity of PE were 0.2M and 0.05M, respectively. 2. The optimum pH of PG was pH 6.0 and the activity of PG in acidity was higher than that in alkalinity. The activity of PG was maximum at 0.3M NaCl and 0.2mM $CaCl_2$. Above the concentration of 0.5M NaCl and 0.5M $CaCl_2$, the activity of PG was lower than that of PG not adding these salts 3. The optimum pH of LOX was pH 7.0 and pH 8.5. 4. The optimum pH of POD was pH 6.0 and the activity of POD was higher in weak acidity and neutrality than in alkalinity. POD activity was slightly decreased by the increase of NaCl and $CaCl_2$ concentration.

• Korean Journal of Environmental Agriculture
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• v.3 no.2
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• pp.37-42
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• 1984

The effect on the activities of peroxidase and lipoxygenase by chemicals was determined. Peroxidase activities of horseradish and apple were inhibited strongly by maneb and comparativelyby mancozeb, zineb. The inhibitory rate of enzyme activity was ranged in $12.5{\sim}34.5%$ by maneb, $11.0{\sim}30.5%$ by mancozeb, and $9.7{\sim}27.5%$ by zineb in the level of $10{\sim}30\;ppm$ at the final concentration. No signification was in the peroxidase activity of apple during ripening between control and plot, treated with 500 ppm mancozeb. On the activity of purified soybean lipoygenase, zineb inhibited it more strongly than carbofuran or phosphamidon, but maneb did not have inhibitory effect on that. The inhibition ranges of $14.0{\sim}40.0%$ by zineb, $6.5{\sim}20.0%$ by carbofuran and $4.5{\sim}13.0%$ by phosphamidon were shown in the final pesticide concentration of $10{\sim}30$ ppm. But in $100{\sim}200$ ppm, lipoxygenase activity was almost inhibited by carbofuran and phosphamidon.