• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.6
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• pp.833-838
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• 1993

A strain of Penicillium sp. extracellularly produced an inhibitory substance for lipoxygenase. These purification procedures were followed : ethanol treatment, chromatographies on Dowex 50W, Sephadex G-25, silica gel column and HPLC. The inhibitor was stable in pH range from 3.0 to 5.0 at $25^{\circ}C$, and a treatment at 10$0^{\circ}C$ for 2 hours didn't diminish its original activity. The purified inhibitor was charred at temperature near 22$0^{\circ}C$~23$0^{\circ}C$ and decomposed. Molecular weight of the inhibitor was estimated to be approximately 270 by Sephadex G-25 column chromatography. The inhibitor rapidly formed EI complex with lipoxygenase and inhibited enzyme activity.

• Applied Biological Chemistry
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• v.38 no.5
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• pp.408-413
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• 1995

Investigations of the effects of pickle product ingredients on lipoxygenase (LOX) and methemoglobin (MHG, a nonenzymatic oxidant) catalyzing oxidation of linolenic acid were conducted. In addition, activities of LOX, peroxidase (POD) and catalase (CAT) in dry spices used in pickle products were determined. Some commercial pickle brines were observed to inhibit oxidation of linolenic acid by LOX and MHG. The ingredients in pickle products, such as dill oil emulsion, onion concentrate, oil cassia, polysorbate 80 and turmeric acid, reduced LOX and MHG catalyzed oxidation. Lipoxygenase activity was present in garlic, mustard seed and red pepper. Only in mustard seed, peroxidase activity was observed. Catalase activity was observed in garlic, black pepper, allspice and red pepper.

• 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.

• Applied Biological Chemistry
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• v.37 no.6
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• pp.451-455
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• 1994

To detect naturally occurring bioactive compounds from unused marine resources, the screening for the 5-lipoxygenase(potato lipoxygenase-II) inhibitors in Asterina pectinifera, Halocynthia roretzi skin, Nototodarus sloani ink, Anthocidaris crassispina skin, Sargassum horneri, Agarum cribrosum, Odonthalia corymbifera and Desmarestia ligulata was carried out. Water, ether, acetone and methanol fractions extracted from Sargassum horneri had strong inhibitory effect on enzymatic lipid oxidation by potato lipoxygenase-II, and their $IC_{50}$ were 320, 18, 9.5 and $100\;{\mu}g/mL$, respectively. The $IC_{50}$ of ether fraction extracted from Asterina pectinifera and acetone fraction extracted from Nototodarus sloani ink were 29.5 and $34.3\;{\mu}g/mL$, and these extracts showed relatively excellent inhibitory activity. Nonpolar solvent (ether, acetone) extracts of tested marine organisms had more inhibitory effect against 5-lipoxygenase than the polar solvent(water) extracts.

• Korean Journal of Food Science and Technology
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• v.31 no.1
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• pp.115-121
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• 1999

Changes of free sugars, lipoxygenase activity and effects of chitosan treatment were analyzed during cultivation of soybean sprout. Free sugars(sucrose, raffinose and stachyose) were more rapidly decomposed in the cotyledon of soybean sprout. Contents of sucrose and raffinose in control group were decreased more rapidly than those of chitosan treated soybean sprouts (CTSS). But the decreasing rate of stachyose was higher in the CTSS. In the hypocotyl, 82% of L-2/3 activity were decreased, whereas 42% of the activity were decreased in the cotyledon after 132 hours of germination. The effect of chitosan treatment on the lipoxygenase activity was more effective on L-2/3 isozyme than L-1. After the germination period of 132 hours, L-2/3 activity of control group was 82.7unit/mg and that of CTSS was 56unit/mg.

• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.1
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• pp.110-115
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• 1994

To investigate the effect of potato lipoxygenase on the farinograph characteristics of wheat flour dough, composite flours containing enzyme-active potato flor (EPF) and hot-ar dried potato flour(HPF) were used. EPF was made by freeze-drying potato tuber. DPF (denaturated potato flour) was prepared by holding EPF at 8$0^{\circ}C$ for 18 hr in a dry oven. The potato flours were added to wheat flour at a level of 10% , respectivley. EPFB (enzyme-active potato flour blends, 90% wheat flour +105 enzyme -active potato flour) containing lipoxygenase activity gave higher farinogram peak time and higher stability values, lower MTI (mixing tolerance index ) and lower weakness values than those of HPFB(hot-air potato flour blends, 90% wheat flour + 10 % hot-air potato flour). Moreover, then lipoxygenase was added to DPFB(denatured potato flour blends , 90% wheat flour + 10% denatured potato flour) at a level of EPFB, it resulted in increasing stability, peak time and decreasing MTI , weakness at a level of EPFB. When the lipoxugenase was added to wheat flour with fumaric acid at alevel of 6.5 $\times$ 10units/g flour, lipoxygenase overcame the deleterious effects that fumaric acid including activated double-bond compounds have at mixing stability. Also the addition of liposxygenase with linoleic acid to defatted wheat flour resulted in the increase in stability and decrease in MTI value compared with those of linoleic acid and defatted wheat flour.

• The Korean Journal of Pharmacology
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• v.29 no.2
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• pp.237-244
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• 1993

The effect of nicotine on the secretion of $[Met^{5}]-enkephalin$ (ME) in addition to proenkephalin A (proENK) mRNA levels and effects of indomethacin, nordihydroguaiaretic acid (NDGA), and captopril on nicotine-induced responses were studied in bovine adrenal medullary chromaffrin (BAMC) cells. Long-term exposure of BAMC cells to nicotine at a concentration of $10{\mu}M$ significantly increased proENK mRNA level and the secretion of ME into the medium. Treatment of BAMC cells with NDGA (a lipoxygenase inhibitor, $10{\mu}M$), indomethacin (a cycloooxygenase inhibitor) or captopril (an angiotensin converting enzyme inhibitor) alone did not affect ME secretion and proENK mRNA levels. The pretreatment of BAMC cells with NDGA inhibited the increased ME secretion and proENK mRNA level induced by nicotine. However, indomethacin and captopril did not affect nicotine-induced responses. Our results indicate that neuronal regulations of ME secretion and proENK mRNA level induced by nicotine in BAMC cells are in part mediated by a lipoxygenase-but not cyclooxygenase-and endogenous renin-angiotensin pathway.

• Journal of Microbiology and Biotechnology
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• v.24 no.3
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• pp.359-362
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• 2014

15-Hydroxyeicosatetraenoic acid (HETE), as a mammalian biologically active metabolite, has anticarcinogenic effect. The conditions of producing 15-HETE from arachidonic acid by using soybean lipoxygenase were optimal at pH 8.5 and $20^{\circ}C$ with 9 g/l arachidonic acid, 54.4 U/ml soybean lipoxygenase, and 4% methanol. Under these optimized conditions, the enzyme produced 9.5 g/l 15-HETE after 25 min, with a molar conversion yield of 99% and a productivity of $22.8gl^{-1}h^{-1}$. To the best of our knowledge, this is the first biotechnological production of 15-HETE.

• Journal of Life Science
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• v.5 no.2
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• pp.70-75
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• 1995

The effect of lipoxygenase (LOX) on the oxidation and co-oxidation of lipid fraction was studied in the model system of rainbow trout. For the reaction in model system 1 g of lipid fraction and 50mL of enzyme extract(LOX, 140 unit in 50mL phosphate buffer solution at pH 7, 4)), which were obtained from rainbow trout, were homoginized in the presence of Tween 20 and kept at 23$\circ$C for 3 days. The activity of LOX was decreased to 43% of initial level during the reaction in the model system. The initial composition of rainbow trout lipid was showed to be consisted of trigliceride(TG;82%) and free fatty acid(FFA;0.1%), while this converted to 59% of TG and 20% of FIFA, respectively after reaction in model system. Change of fatty acid composition was also observed and the content of linoleic acid, one of the major fatte acids, was decreased to 13% from 54% in the content of total fatty acids after reaction. The carotenoids in rainbow trout were composed of 0.4% $\alpha$-carotene, 1.6% $\beta$ -carotene, 80% canthaxanthin, 7% lutein and 11% zeaxanthin, thus the canthaxanthin was the major component. This canthaxanthin was the most degraded carotenoid by lipoxygenase catalyzed co-oxidation during the reaction. On the other hand the tocopherol isomers found in the rainbow trout were $\alpha$ and $\beta$ -tocopherol, and $\alpha$-tocopherol had a higher degradation rate by the lipoxygenase catalyzed co-oxidation than of $\beta$-tocopherol in the reaction of model system.

• Applied Biological Chemistry
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• v.38 no.5
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• pp.414-421
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• 1995

In order to establish informations important to the measurement of lipoxygenase (LOX) activity, providing conditions most favorable for its action and determining factors that inhibit activity, the influence of extraction buffer, substrate, pH, storage, temperature, NaCl, $CaCl_2$, other cations and antioxidants on LOX activity, and localization of LOX in cucumber tissues were carried out. The most favored substrate for LOX was linolenic acid followed by linoleic and arachidonic acids. LOX activity in both peel and mesocarp tissue extracts was maximum at pH 5.5 and relatively stable at $40^{\circ}C\;and\;50^{\circ}C$ temperature. The condition of 0.2 M NaCl with pH 5.0 was observed to provide optimum LOX stability. The enzyme activity was reduced by addition of cations, $Mn^{2+},\;Cu^{2+}\;or\; Al^{3+}$, except $Ca^{2+}$ which stimulated activity of LOX. Butylated hydroxy anisole (BHA) and propyl gallate decreased LOX activity with increasing concentration. Cucumber peel had higher activity than other tissues, locule or mesocarp, of cucumber.