• Applied Biological Chemistry
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• v.34 no.3
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• pp.249-257
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• 1991

To elucidate enzymatic properties of ${\alpha}-galactosidase$ (EC 3, 2, 1, 22) from germinated soybean, changes in the enzyme activities and oligosaccharide contents during germination of soybean were determined. ${\alpha}-Galactosidase$ from germinated soybean was purified by ammonium sulfate fractionation, ion exchange chromatography and gel filtration. Their chemical and enzymatic properties was investigated. ${\alpha}-galactosidase$ activity of sobeam was maximized when it was germinated at $25^{\circ}C$ for 120 hour. Raffinose and stachyose in soybean were decomposed completely after 96 hours and 120 hours of germination, respectively. Soybean ${\alpha}-galactosidase$ was purified by 6.6 fold by ammonium sulfate fractionation, ion exchange chromatography on DEAE-Cellulose and Sephadex A-50, and gel filtration on Sephadex G-150. Its specific activity was 825 Units/mg protein and the yield was 2.5% of the total activity of crude extracts. The purified ${\alpha}-galactosidase$ of soybean was found to be homogeneous by polyacrylamide gel electrophoresis and by HPLC. Isoelectric point of soybean ${\alpha}-galactosidase$ was determined analytical isoelectric focusing to be pH 4.8. The soybean ${\alpha}-galactosidase$ was monomeric and its molecular weight was estimated to be 30,000 by SDS-PAGE. The optimal temperature and pH for the soybeam ${\alpha}-galactosidase$ activity were $40^{\circ}C$ and pH 6.0 and 75% of its activity was lost by heating at $60^{\circ}C$ for 10 min. The enzyme was appeared to have higher affinity to raffinose than to stachyose. The Km value of soybean enzyme was 5.3 mM for ${\rho}-nitrophenyl-{\alpha}-D-galactopyranoside$ and the activation energy on PNPG was calculated to be 13.02 Kcal per mole.

• Journal of the East Asian Society of Dietary Life
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• v.17 no.6
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• pp.903-910
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• 2007

In order to make acquire a potential use for Opuntia humifusa as a natural functional food material, this study was performed to determine the quality properties of Jeung-pyun made with added Opuntia humifusa, or prickly pear powder. According to an analysis of its major components, we found that the prickly pear powder consisteds of nitrogen-free extracts (71.85%) and crude fiber (11.20%). Greater additions of prickly pear powder had resulted in significantly lower pH in the of Jeung-pyun. According to measurements on the degree of Jeung-pyun gelatinization, by means of ${\beta}$-amylase, greater additions of prickly pear powder led to the higher levels of isolated maltose, indicating that the gelatinization degree of the Jeung-pyun became higher. Also, samples with higher concentrations of prickly pear powder had a tendency toward lower water content, which allowed us to expect a longer storage duration for the Jeung-pyun. In the textural property tests the Jeung-pyun that had less hardness and greater adhesiveness (p<0.05) than the control group as the content of prickly pear powder became higher. Also, the Jeung-pyunhad lower gumminess and chewiness than the control group as the content of prickly pear powder became higher. Therefore, it is possible to prepare relatively soft Jeung-pyun using prickly pear powder. For the color differences of the Jeung-pyun samples, lower L- values, and higher a- and b -values (p<0.05) presented as the addition level of prickly pear powder became higher. According to SEM observations of the Jeung-pyun, the added prickly pear powder addition groups generally showed a smaller and more inconsistent pore size, but higher porosity, than the control group. According to sensory analyses of the Jeung-pyun, the P2 group scored highest for color item, and the P4 group generated the fermented scent. Higher additions content of prickly pear powder led to the lower score, but higher scores for adhesiveness. Finally, the P2 group achieved the highest score for overall taste.

• Proceedings of the Botanical Society of Korea Conference
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• 1987.07a
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• pp.133-148
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• 1987

Gibberellin(GA) 3-$\beta$ hydroxylation is very important for the shoot elogation in the higher plants, since only 3$\beta$-hydryoxylated GAs promote shoot elogation in several plants. Fluctuation of 3$\beta$-hydryoxylase activity was examined during seed maturation using two cultivars of , P. vulgaris, Kentucky Wonder (normal) and Masterpiece (dwarf). Very immature seeds of both cultivars contain high level of 3$\beta$-hydroxylase activity (per mg protein). Both cultivars showed maximum of enzyme activity (per seed) in the middle of their maturation process. Gibberellin 3$\beta$-hydroxylase catalyzing the hydroxylation of GA20 to GA1 was purified 313-fold from very early immature seeds of P. vulgaris. Crude soluble enzyme extracts were purified by 15% methanol precipitation, hydrophobic interaction chromatogrphy, DEAE ion exchange column chromatography and gel filtration HPLC. The 3$\beta$-hydroxylase activity was unstable and lost much of its activity duting the purification. The molecular weight of purified enzyme was extimated to be 42, 000 by gel filtration HPLC and SDS-PAGE. The enzyme exhibited maximum activity at pH 7.7. The Km values for [2.3-3H] GA20 and [2.3-3H]GA9 were 0.29 $\mu$M and 0.33 $\mu$M, respectively. The enzyme requires 2-oxoglutarate as a cosubstrate; the Km value for 2-oxoglutarate was 250 $\mu$M using 3H GA20 as a substrate. Fe2+ and ascorbate significantly activated the enzyme at all purification steps, while catalase and BSA activated the purified enzyme only. The enzyme was inhibited by divalent cations Mn2+, Co2+, Ni2+, Cu2+, Zn2+, Cd2+ and Hg2+. Effects of several GAs and GA anaogues on the putrified 3$\beta$-hydroxylase were examined using [3H]GA9 and GA20 as a substrates. Among them, GA5, GA9, GA15, GA20 and GA44 inhibited the enzyme activity. [13C, 3H] GA20 was converted by the partially purified enzyme preparation to [13C, 3H]GA1, GA5 and GA6, which were identified by GC-MS, GA9 was converted only GA4, GA15 and GA44 were converted to GA37 and GA38, respectively. GA5 was epoxidized to GA6 by the preparation. This suggests that 3$\beta$-hydroxylation of GA20 and epoxidation of GA5 are catalyzed by the same enzyme in P, vulgaris.

• The Korean Journal of Mycology
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• v.31 no.3
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• pp.148-154
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• 2003

Extracts from 52 samples of mushrooms were prepared by using water, ethanol and methanol, and then yields and angiotensin I-converting enzyme(ACE) inhibitory activity were investigated. Sample mushrooms contained crude proteins of $7.1{\sim}56.5%$, curde lipids of $0.2{\sim}4.4%$ and carbohydrates of $30.3{\sim}86.6%$. Among 52 samples, the water extract from fruiting body of Pholiota spp. ASI 24027 showed the highest extraction yield of 68%. Water extract of Pholiota spp. ASI 24012 fruiting body had potential ACE inhibitory activity of 66%. The optimal extraction condition of the ACE inhibitor from the fruiting bodyies of Pholiota spp. ASI 24012 was In water at $30^{\circ}C$ for 1 hr and ACE inhibitory activity was 67.6% on the condition with 0.2 mg of $IC_{50}$.

• Korean Journal of Food Science and Technology
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• v.35 no.4
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• pp.726-732
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• 2003

The crude extracts from Rhus javanica Linne showed comparatively strong antioxidative activity in test oils. Antioxidative components were isolated and identified by column chromatography, thin layer chromatography, UV, and NMR. These antioxidative components were added to several oils to compare antioxidative activity with several commercial antioxidants, such as BHA, BHT, and tocopherol. After the sixth column chromatography, one fraction (R-18-9-3-2-4-2) was separated from chloroform layer of Rhus javanica Linne. The R-18-9-3-2-4-2 fraction was identified as methyl gallate by $^1H-NMR$ and $^{13}C-NMR$ and confirmed with methyl gallate standard as authentic. The R18-9-3-2-4-2 fraction from chloroform layer of Rhus javanica Linne showed stronger activity than that of the ${\alpha}-,\;{\delta}-tocopherol$, BHT, and BHA at the same concentration.

• Korean Journal of Food Science and Technology
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• v.44 no.4
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• pp.460-466
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• 2012

Through an analysis of T-2 and HT-2 toxins in corn and brown rice, the effect of enzymatic deacetylation of T-2 toxin on HT-2 toxin was investigated. Gas chromatography (GC) with electron capture detection and high-performance liquid chromatography (HPLC) with fluorescence detection were used for quantitative determination. T-2 toxin was converted into HT-2 (84-86%) within 15 min in the presence of crude protein extracts from corn and brown rice. The absence of T-2 conversion was observed for autoclaved samples, in which the enzymes were inactivated. When phosphate buffered saline, followed by methanol, was used as the extraction solvent, recoveries of T-2 toxin spiked at 50 and 200 ${\mu}g/kg$ were from 60 to 87%, whereas those of HT-2 in the autoclaved samples were 0%. In non-autoclaved samples, recoveries of HT-2 were 37-66%, whereas those of T-2 were negligible. However, the conversion of T-2 into HT-2 was not observed when samples were extracted by methanol/water.

• Journal of the Korean Society of Food Culture
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• v.19 no.1
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• pp.94-105
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• 2004

The biochemical components of Namcheondlggae, Miryangdlkkae 25, Boradlggae and Ipdlkkae 1 were measured. The samples were extracted with hot water, 60% acetone or 80% ethanol for screening physiological activity. The crude protein content (4.36%) was found in the Miryangdlkkae 25 and calcium content (497.5 mg%) was found in the Namcheondlggae among the tested 4 perilla loaves. Fructose was 30.86 mg% in the Namcheondlggae and free amino acids at all perilla leaves was detected seventeen. In Boradlggae, glutamic acid and alanine were 25.37 and 11.91 mg%. Totally nine non-volatile organic acids were also detected and the contents of malic acid and glutaric acid were 28.34 and 14.57 mg% in Boradlggae. The Miryangdlkkae 25 had the highest vitamin C amount which was 113.24 mg%. Angiotensin converting enzyme (ACE) inhibition activity of 60% acetone extract of Miryangdlkkae 25 was 39.20% when added as addition of 200 ppm level and xanthine oxidase inhibition activity of 80% ethanol extract of Boradlggae was 46.71%. Electron denoting activity of 60% acetone extract from Namcheohndlggae was the strongest inhibition activity as 98.19% when 200 ppm level of the sample extracts were added.

• The Korean Journal of Mycology
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• v.22 no.3
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• pp.266-275
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• 1994

Brewer's yeast extract can be used as a good substrate for the culture of Lentinula edodes Mycelia(LEM). We found that it was better to filter the extract through three kinds of sieves and then to heat for hydrolysis and concentration at $90^{\circ}C$ prior to use. Also the maximum condition for the growth of LEM was investigated. We found that addition of inorganic salts such as calcium enhanced the growth of LEM. On the other hand, addition of carbon and nitrogen sources to the medium did not affect, and even inhibited under certain conditions, the growth of LEM. The maximum temperature for the growth of LEM was around $25^{\circ}C$. Also, it grows better when agitated by shaking at 100 rpm for airration. The appropriate concentration of the extract to use was 10%. Under these conditions, LEM could reach to the confluency after cultivation of 12 days. Our extract formula seems better than other available media for LEM growth, producing higher crude protein content and better taste.

• Applied Biological Chemistry
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• v.40 no.5
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• pp.375-379
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• 1997

Two ribosome-inactivating proteins, PRIP 1 and PRIP 2 have been isolated from the leaves of $Cucurbita\;moschata\;D_{UCHESNE}$. Crude extracts were purified through ammonium sulfate precipitation and column chromatography using DE-52 cellulose, S-Sepharose, FPLC Suprose 12 HR and FPLC Mono-S. The molecular weights of PRIP 1 and PRIP 2 were 31,000 and 30,500, respectively. PRIP 2 was thermostabe and maintained its activity even after the incubation of the protein at $50^{\circ}C$ for 30 min. In a cell free in vitro translation system using rabbit reticulocyte lysate, protein synthesis was inhibited by the addition of PRIP 1 and PRIP 2. The $IC_{50}$ of PRIP 1 and PRIP 2 were 0.82 nM and 0.79 nM, respectively. The comparison of N-terminal amino acid sequences of the PRIP 1 and PRIP 2 with known RIPs revealed that PRIP 1 shows sequence similarity with Luffin B from Luffa cylindrica and Trichokirin from Trichosanthes kirilowii Maximowicz and PRH) 2 has sequence similarity with Momordin II and MAP 30 from Momordica charantia.

• Journal of the Korean Society of Food Science and Nutrition
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• v.39 no.10
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• pp.1495-1502
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• 2010

This study was for the industrial application of functional food ingredients from whole fruits of sweet persimmon. Whole fruit and pulp of sweet persimmons were divided, and then lyophilized and powdered. Contents of crude fiber, vitamin C, and mineral were significantly higher in whole fruit than pulp of sweet persimmon. The amino acid content of whole fruit was 1.4 times higher than those of sweet persimmon pulp. In the biological activities of water and ethanol extracts from whole fruit and pulp of sweet persimmon, ethanol extract was higher than water extract, and whole fruit was higher than its pulp. The result which compared the biological activities of the water and ethanol extract from lyophilized sweet persimmon showed that total phenolic content was significantly higher in whole fruit of sweet persimmon, but flavonoid contents were not significantly different. Especially ABTS, NO radical scavenging activity, reducing power and tyrosinase inhibition activity were significantly higher in whole fruit extract than pulp extract of sweet persimmon. The relatively high content of fiber and vitamin C, and biological activity of whole fruit than pulp of sweet persimmon may be make it preferable as functional food materials for secondary processed goods.