• KSBB Journal
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• v.13 no.5
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• pp.599-605
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• 1998

Soybean peroxidase was extracted from soybean hulls and purified by ammonium sulfate precipitations (25% and 75% saturation), pl fractionation, and anionic exchange and gel filtration chromatographies (DEAE-Sephadex A-50 and Superose 12). Modlecular weight and pl value were estimated to be ca. 45 kD and 4.2, respectively. Purified soybean peroxidase had an RZ value of 0.43. Compared with horseradish peroxidase, it showed superior thermal and pH stability. Assuming the first-order kinetics, the thermal deactivation rate constant of soybean peroxidase at 80$^{\circ}C$ was about 8 times lower than that of horseradish peroxidase. Deactivation energy was calculated to be 69.3 kcal/mol. Soybean peroxidase showed about 10% higher H2O2 degradation capacity than horseradish peroxidase. Exploiting these advantages, the soybean peroxidase purified from the domestic soybean hull is expected to replace horseradish peroxidase in various applications.

• Journal of Life Science
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• v.8 no.4
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• pp.416-420
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• 1998

Soybean sprouts peroxidase can be used for enzymatic determination of glucose. Peroxidase from soybean sprouts was purified by ammonium sulfate precipitation and DEAE Sephacel column chromatography. The glucose could be quantitatively assayed by using glucose oxidase and soybean sprouts peroxidase. The optimum pH and temperature for glucose assay were of pH 5.5 and $40^{\circ}C$, respectively. The relationship between absorbance and glucose concentration was linear. And also the relationship between absorbance and reaction time was linear. The reducing agents such as L-cysteine, dithiothreitol inhibited the glucose assay by glucose oxidase and soybean sprouts peroxidase.

• Korean journal of applied entomology
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• v.21 no.1 s.50
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• pp.23-26
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• 1982

The present study was carried out to investigate the change of peroxidase activity of soybean seed infected with Cerrospora kikurhii. The protein content, polyphenol oxidase activity and peroxidase isozyme pattern in health and infected soybean seed were also compared. 1. The peroxidase activity was substantially higher in the infected soybean seeds than that in the healthy seeds either cracked or not. No significant differences in protein content were recognized among the seeds tested. 2. No significant differences in peroxidase activities and protein contents were notified between healthy and infected seeds from the measurements on each parts of dissected seeds, cotyledon and seedcoat, however the peroxidase activity in the seed coat of the stained seed was 2.5 times to healthy seed. 3. The activities of polyphenel oxidase were undectable in both healthy and diseased seeds. 4. The electrophoretic Patterns of the Peroridase isozyme were the same between healthy and in footed seed. 5. Therefore, the increase of peroxidase activity in infected soybean seedcoat was mainly due to the biochemical reaction against the pathogen.

• Korean Journal of Environmental Agriculture
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• v.7 no.1
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• pp.52-57
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• 1988

This study was carried out to investigate the specific activity fo peroxidase(POD) in conjunction with the phytotoxic effect of the tolerant soybean(Glycine max Merr.) and the susceptible crabgrass(Digitaria adscendens(L.) Scopol.) to acifluorfen. The POD activity increased during the growth of soybean and crabgrass seedlings. But after the foliar application of acifluorfen, the POD activity in the treated leaves was considerably higher than in controlled leaves, suggesting that soybean had higher tolerance to acifluorfen with growth. All the treated soybeans recovered from herbicidal injury in 14 days after treatment, while all the treated crabgrasses were dead with extreme necrosis and leaf burning. It was measured that the POD activity of crabgrass increased abruptly in 1 to 2 days after treatment and then significantly decreased in 5 days.

• Journal of the Korean Society of Food Science and Nutrition
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• v.27 no.6
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• pp.1143-1147
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• 1998

Enzymatic characterization of peroxidase(E.C. 1.11.1.7) from soybean sprouts was investigated. The optimum pH of the purified peroxidase was 7.0 and relatively stable at pH 6.0~7.0. And the optimum temperature was 50oC. The enzyme was most active with guaiacol as a substrate, followed by (＋)catechin, pyrogallol and p phenylenediamine. The Km values for guaiacol and H2O2 were 4.2mM and 2.5mM, respectively. L Ascorbic acid and 2 mercaptoethanol greatly inhibited the enzyme activity, while Cu2+, Co2+ and Ni2+ activated the enzyme.

• Journal of the Korean Society of Food Science and Nutrition
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• v.28 no.1
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• pp.81-86
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• 1999

The factors affecting thermostability and reactivation of peroxidase from soybean sprouts(Glycine max L.) were investigated. The enzyme was the most stable at pH 7.0 and below 60oC. Thermostability of the enzyme was reduced by addition of sodium chloride and saccharides. The partially inactivated enzyme by heat treatment at 75oC for 10 min was reactivated up to 211.5% at the optimal reactivation condition. The optimal pH and temperature for reactivation of the enzyme were pH 9.0 and 40oC, respectively. The reactivation was completely inhibited by addition of sulfhydryl reagent such as L cysteine.

• BMB Reports
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• v.29 no.6
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• pp.564-568
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• 1996

Bursts of ethylene production occurred in twice at an early exponential (EEP) and prestationary (PSP) phases, respectively, during growth of callus tissue isolated from the root of soybean seedlings. The second burst of ethylene production at PSP was smaller in magnitude than the earlier one at EEP, but was followed by increases in both guaiacol peroxidase (GuPOX) and ascorbate peroxidase (AsPOX). The increase in AsPOX activity was also preceded by an increase in lipoxygenase (LOX) activity. Treatment of the tissue with the ethylene antagonist 2,5-norbonadiene (NBD) resulted in substantial reduction in LOX and AsPOX activities during this period. GuPOX activity was reduced only slightly, if any, by NBD. Role of ethylene in the sequential induction of LOX and AsPOX in senescing callus tissue is discussed.

• Journal of Korean Biological Nursing Science
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• v.10 no.1
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• pp.1-10
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• 2008

Purpose: The purpose of this study was to investigate the cerebral infarction size, antioxidant enzyme activities and lipid peroxidation changes after 6 weeks of dietary soybean protein intake in a rat focal brain ischemia model. Method: Weaning Sprague-Dawley rats were fed with either modified AIN-93G diet containing casein 20% (control), 20% soybean protein isolate-based diet (S20), or 40% of soybean protein isolate-based diet (S40) for 6 weeks. The animals were subject to right middle cerebral artery occlusion for 2 hr. After 24 hr of recirculation, the rats were sacrificed. Antioxidant enzymes activities of superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPx) and thiobarbituric acid reactive substance (TBARS) level in the right brain were also measured. Result: There were no significant differences in the right cortical infarction volume, TBARS level, SOD and CAT activities among the three groups whereas the GPx activities of the S20 group were significantly higher than those of the control group (p=.02). Conclusion: Our results suggest that 20% of soybean protein may have a modulating effect on GPx and possibly have some protective effect against oxidative stress although it may enough to decrease cerebral infarction volume in rat focal brain ischemia model.

• Mycobiology
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• v.40 no.4
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• pp.258-262
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• 2012

cDNA of the glx1 gene encoding glyoxal oxidase (GLX) from Phanerochaete chrysosporium was isolated and expressed in Pichia pastoris. The recombinant GLX (rGLX) produces $H_2O_2$ over 7.0 nmol/min/mL using methyl glyoxal as a substrate. Use of rGLX as a generator of $H_2O_2$ improved the coupled reaction with recombinant manganese peroxidase resulting in decolorization of malachite green up to $150{\mu}M$ within 90 min.

• Journal of the Korean Society of Food Science and Nutrition
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• v.28 no.6
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• pp.1298-1303
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• 1999

For the purpose of improving the qualities of immatured soybean(Seoklyang), the effects of table height (0, 5, 10, 15mm) and time(60, 66, 72, 78 sec) for microwave blanching on physicochemical properties were investigated. Enzyme inactivities lipoxygenase and peroxidase for all there conditions were more de creased than for control and water blanching. Enzyme activity of each conditions was expressed as percentage on the enzyme activity of control. Lipoxygeanse activity and peroxidase activity of immatured soybeans were about 20% and 10% levels, respectively. Also the color showed the higher L(lightness), b(yellowness), chroma(brightness) values, but the lower a(redness) and hue angle. Vitamin C content was worse than for control, but was better than for water blanching. Hardness with a few exceptions showed the higher value for control.