• Microbiology and Biotechnology Letters
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• v.18 no.5
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• pp.490-495
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• 1990

The extracellular inulinase from Bacillus spp. was purified to a single protein through a sequence of operations including ammonium sulfate fractionation, heat treatment, DEAE Sepharose C1-6B ion exchange chromatography, Sephadex 6-100 and Sephadex 6-150 gel filtration. The purified enzyme was confirmed to be a $\beta$ -D-fructofuranosidase(EC 3.2.1.26) which was much more active on sucrose than on inulin(I/S = 0.2). The maximal inulinase activity was observed at pH 6.0 and at the temperature of $50^{\circ}C$. The mo1ecular weight of the enzyme was about 56, 000. Tryptophan and histidine residues of the enzyme molecule were found to be essential for its catalytic activity.

• Journal of Korean Society for Atmospheric Environment
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• v.13 no.6
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• pp.439-450
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• 1997

Atmospheric fine particles $(PM_{2.5})$ were collected at the background sites, Kangwha, Taean, and Kosan and characterized to understand their behaviors at the sites. Daily samples of $PM_{2.5}$ mass were measured and ionic species, carbonaceous species, and gaseous species were analyzed. Four-day backward trajectory analysis was also carried out. The mean concentrations of anthropogenic species were highest at Kangwha among three sites, while contributions from sea salts wree highest at Taean during the measurement period due to higher wind speed at Taean. Major chemical components in fine particles were sulfate, organic carbon, nitrate, and ammoniu. Most of the non-sea-salt (nss) sulfates in $PM_{2.5}$ might be present as ammonium sulfates at these sites. Most air parcels arriving at Kangwha and Taean were from northern China. Therefore, both sites were thought to be affected by the same air parcel. At Kosan, during the measurement period, air parcels were from either northern China or sourthern China. The nss sulfate concentration in the air parcels from southern China was higher, while the nss calcium, nitrate, and ammonium concentrations were higher when the air parcels were from northern China.

• Korean Journal of Food Science and Technology
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• v.12 no.1
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• pp.1-5
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• 1980

Crude invertase was obtained from the water extracts of Korean ginseng, Panax ginseng C. A. Meyer, by fractionation with $0.8{\sim}1.0$ saturation of ammonium sulfate. The properties of the crude invertase were as follows: Crude invertase was stable in the pH range between 5 and 9, and at the temperature below $35^{\circ}C$. Crude invertase showed the optimum pH at 5.0 and the optimum temperature at $50^{\circ}C$. The activity of the crude invertase was inhibited by $Ag^{+}\;Mn^{+}\;Hg^{+}\;Zn^{+},\;and\;Rb^{+}$, while $Ca^{+}\;Cu^{+},\;and\;Fe^{3+}$ demonstrated remarkable increasing effects on the enzyme activity.

• Applied Biological Chemistry
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• v.21 no.2
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• pp.112-118
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• 1978

Xanthine oxidase from bovine thyroid glands was purified to apparent homogeneity when judged by analytical disc gel electrophoresis. The purification procedures include pancreatin digestion, butanol extraction, ammonium sulfate precipitation, calcium phosphate gel adsorption, ultrafiltration, calcium phosphate gel-cellulose column chromatography, gel filtration, preparative Sephadex G-25 column electrophoresis, and preparative polyacrylamide gel electrophoresis. The enzyme was enriched 1,000-fold. However, its specific activity was markedly low as compared with highly purified milk enzyme. Thyroidal xanthine oxidase exhibited a low specificity for substrates and electron acceptors. The kinetic properties of thyroid xanthine oxidase were found to be similar to those of the milk enzyme on the basis of Michaelis constants for common substrates.

• Transactions of the Korean hydrogen and new energy society
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• v.17 no.4
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• pp.371-378
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• 2006

Effect of $(NH_4)_2SO_4$ precipitation and heat-treatment on hydrogenase which was extracted from the cytoplasmic fraction of the phototrophic purple sulfur bacterium Thiocapsa roseopersicina NCIB 8347 was studied. Crude enzyme extract was prepared by centrifugation($28,000{\times}g$, $400,000{\times}g$) after sonication of cells grown under photosynthetic condition for 96 hrs. Various conditions of $(NH_4)_2SO_4$ precipitation and heat-treatment were examined and the effect of protein concentration was analyzed by SDS-electrophoresis between the treatments. Optimum conditions for $(NH_4)_2SO_4$ precipitation and heat-treatment for evolution hydrogenase activity were 40-60% saturation and $60^{\circ}C$ for 20 min, respectively, which exhibited the specific hydrogenase activity of 0.78 U/mg-protein. Specific hydrogenase activity was decreased to 31.6% when the heat-treatment at $60^{\circ}C$ increased from 20 min to 5 hrs.

• Biotechnology and Bioprocess Engineering:BBE
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• v.9 no.4
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• pp.313-317
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• 2004

The nutritional requirements for Prevotella sp. 4PCCNB2 isolated from the rumen of a native goat in Korea and those of the ATCC 19189 strain isolated from the bovine rumen were investigated. The two strains grew well with ammonium sulfate as the sole added nitrogen source. However, neither a complex of amino acids nor casein hydrolysate effectively replaced ammonium sulfate. Biotin, p-aminobenzoic acid, and vitamin $B_12$ were essential to culture the ATCC 19189 strain. Unlike the ATCC 19189 strain, however, $B_12$ was only stimulatory for the growth of the 4PCCNB2 strain. The 4PCCNB2 strain grew well in the basal medium without an individual acid such as acetic acid or valeric acid. In contrast, either acetic or valeric acid was absolutely required for the growth of the ATCC 19189 strain.

• Journal of Plant Biotechnology
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• v.31 no.4
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• pp.319-323
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• 2004

Soluble latex protein fraction excreted from Euporbia lathyris laticifer was resolved by 10% SDS-polyacrylamide gel electrophoresis to identify distinctively displayed latex major protein bands including ELp65, ELp55, ELp43, ELp32 and ELp23. Among them, ELp65 was purified by ammonium sulfate precipitation, gel permeation chromatography and ion exchange chromatography. Its N-terminal amino acid sequencing revealed its homology to the leading region of mature peptide of tomato p69a subtilisin-like protease, suggesting a certain role involved in plant defense system. In the analysis of Southern blot hybridization using PCR-amplified tomato p69a probe DNA, E. lathyris genome was suggested to have a gene family consisting of 3-5 gene members putatively encoding subtilisin-like proteases.

• Korean Journal of Microbiology
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• v.27 no.3
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• pp.245-249
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• 1989

Extracellular proteases of Bacillus licheniformis were partially purified using ammonium sulfate fractionation and Sephadex G-75 gel filtration chromatography. The partial purification permited the weparation of two different protease activities, type I and type II. Protease type I is an enzyme with rather high protealytic activity toward dasein and was highly susceptible to organofluoride and EDTA inhibitions. It showed maximal proteolytic activity at pH 7.5 and was rapidly denatured at $71^{\circ}C$. Protease type II is a protease with relatively lower proteolytic activity than the type I. It was also inhibited by 10mM of EDTA and 1mM of PMSF by 30 min incubation. The enzyme showed maximal activity at pH 8.0 and was denatured relatively slowly at $71^{\circ}C$.

• The Korean Journal of Mycology
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• v.32 no.2
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• pp.138-141
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• 2004

The effect of culture parameters on the production of Colletotrichum gloeosporioides growth inhibitory substance from Bacillus subtilis was investigated. The maximal growth inhibition zone was observed in the medium of pH 7.0. Among the tested carbon sources, glucose showed the largest growth inhibition zone above two fold than other carbon sources. Ammonium sulfate and organic nitrogen sources were effective on the production of growth inhibitory substance. Luria Bertani (LB) medium was the best on the production of antifungal substance from B. subtilis.

• BMB Reports
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• v.29 no.2
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• pp.163-168
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• 1996

Glycosylated polyphenol oxidase was purified from potato tuber using ammonium sulfate fractionation, Sephadex G-100, and concanavalin A Sepharose column chromatography. Two or three types of polyphenol oxidase were separated on concanavalin A Sepharose. Type I and II polyphenol oxidases did not bind to concanavalin A Sepharose. Type I seemed to be an aggregated form of polyphenol oxidase. Type III polyphenol oxidase, which is presumed to be glycosylated because it was bound to concanavalin A Sepharose and eluted with $\alpha$-D-methyl glucopyranoside, was further purified by chromatography on Econo-Pac Q and Superose 12. Glycosylated polyphenol oxidase was purified 130-fold from the dissolved ammonium sulfate pellet resulting in about $6\;{\mu}g$ of the enzyme from 100 g of potato tuber periderm. The molecular weight of the glycosylated enzyme determined by SDS-polyacrylamide gel electrophoresis was about 64,000. Optimum temperature and pH of both II and type III potato polyphenol oxidases were $20^{\circ}C$ and pH 7.0, respectively. Glycosylated form of polyphenol oxidase (type III) preferred catechol to catechin as a substrate, whereas type II enzyme showed the reverse substrate preference.