• Korean journal of food and cookery science
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• v.4 no.2
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• pp.57-64
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• 1988

The present study was conducted to characterize lipoxygenase isoenzymes isolated from germinating soybean seeds to obstain pH profiles, carbonyl Production, carotene bleaching abilities, and stability to heat. The roles of these lipoxygenase isoenzymes in the generation of volatile carbonyl compounds were investigated to associate with off-flavor and odor of soybean sprouts cooked to different temperatures. Lipoxygenase isoenzymes were isolated from soybean sprouts using ammonium sulfate fractionation, gel filtration and ionexchange chromatography. Two main lipoxygenases exhibited maximum activity at pH 6.5 (lipoxygenase 2) and at pH 9.5 (lipoxygenase 1), respectively. Both lipoxygenase 1 and 2 produced 280 nm absorbing carbonlys and bleached carotene. The abilities of hydroperoxide formation, 280 nm absorbing carbonyl production and carotene bleaching of lipoxygenase isoenzymes were decreased significantly as the cooking temperature raised. Sensory evaluation data presented that raw and $50^{\circ}C$ cooked soybean sprouts showed significantly higher grassy odor than $80^{\circ}C$and $100^{\circ}C$ cooked soybean sprouts. On the other hand beany odor was significantly higher in $50^{\circ}C$ and $80^{\circ}C$ cooked soybean sprouts than in raw and $100^{\circ}C$ cooked soybean sprouts. These results indicate that lipoxygenase plays a role in the development of off-odor and flavors in soybean sprouts under the condition of chewing and inadequate heating.

• Journal of Life Science
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• v.25 no.12
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• pp.1370-1376
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• 2015

The 1, 1- diphenyl 2-picrylhyorazyl (DPPH) is a well-known radical and a trap (scavenger) for other radicals. Hyaluronidase (HAase) is an enzyme that depolymerizes the polysaccharide hyaluronic acid (HA) in the extracellular matrix of connective tissue. Lipoxygenase (LOX) enzyme was reported to convert the arachidonic, linoleic and other polyunsaturated fatty acid into biologically active metabolites involved in the inflammatory and immune responses. The purpose of the present study is to evaluate plant extracts as sources of natural antioxidants and to examine whether Achyranthes japonica having significant DPPH, HAase and LOX inhibitory activity. The inhibitory effect of HAase by A. japonica was assayed using a Morgan microplate assay. The antioxidant activity of the A. japonica extracts was measured on the basis of the scavenging activity of the stable 1, 1- diphenyl 2-picrylhyorazyl (DPPH) free radical. DPPH scavenging activity of matured roots of A. japonica was evaluated at 4.0 mg/ml was 87.8% and that of young roots was 86.2% at same concentration. The roots of A. japonica showed maximum inhibition of HAase activity (IC₅₀ = 27.7 μg/ml). The highest LOX inhibition was recorded in the root extract among three vegetative parts. Inhibition of HAase activity of roots may contribute towards the development of herbal medicines. Although percent inhibition of lipoxygenase by Achyranthes japonica for all young and matured groups for leaves, stems, and roots at different concentrations, there were not show a statistically significant difference (p<0.05).

• Korean Journal of Food Science and Technology
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• v.30 no.5
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• pp.1012-1017
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• 1998

This study was performed to investigate the change of lipoxygenases and urease activities, trypsin inhibitor, tannin and phytic acid contents during heat treatment of Jinpum soybean. The lipoxygenase-1 and urease possessed their activities after heating at $60^{\circ}C$ for 100 min, but their activities disappeared rapidly at $80^{\circ}C$ and $100^{\circ}C$ for 20 and 10 min. There were no lipoxygenase-2 and -3 activities in Jinpum soybean with and without heating. Trypsin inhibitor was lost 91.9%, 78,1% and 58.6% of the activity after heat treatment at $100^{\circ}C$ for 50 min, at $80^{\circ}C$ for 100 min and at $60^{\circ}C$ for 100 min, respectively. The tannin content was increased by heat treatment. The content of and phytic acid was increase after heating at $60^{\circ}C$ for 100 min, unchanged at $80^{\circ}C$ for 100 min and decreased at $100^{\circ}C$ for 100 min.

• BMB Reports
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• v.40 no.1
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• pp.100-106
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• 2007

The wound-inducible lipoxygenase obtained from maize is one of the nontraditional lipoxygenases that possess dual positional specificity. In this paper, we provide our results on the determination and comparison of the kinetic constants of the maize lipoxygenase, with or without detergents in the steady state, and characterization of the dependence of the kinetic lag phase or initial burst, on pH, substrate, and detergent in the pre-steady state of the lipoxygenase reaction. The oxidation of linoleic acid showed a typical lag phase in the pre-steady state of the lipoxygenase reaction at pH 7.5 in the presence of 0.25% Tween-20 detergent. The reciprocal correlation between the induction period and the enzyme level indicated that this lag phenomenon was attributable to the slow oxidative activation of Fe (II) to Fe (III) at the active site of the enzyme as observed in other lipoxygenase reactions. Contrary to the lagging phenomenon observed at pH 7.5 in the presence of Tween-20, a unique initial burst was observed at pH 6.2 in the absence of detergents. To our knowledge, the initial burst in the oxidation of linoleic acid at pH 6.2 is the first observation in the lipoxygenase reaction. Kinetic constants (Km and kcat values) were largely dependent on the presence of detergent. An inverse correlation of the initial burst period with enzyme levels and interpretations on kinetic constants suggested that the observed initial burst in the oxidation of linoleic acid could be due to the availability of free fatty acids as substrates for binding with the lipoxygenase enzyme.