• Microbiology and Biotechnology Letters
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• v.20 no.3
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• pp.295-301
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• 1992

An alkaline protease producing microorganism was isolated from soil and identified as Streptomyces griseus HC-1141. The optimum pH and temperature for the purified enzyme activity were 8.0 and $60^{\circ}C$, respectively. The enzyme was relatively stable in the pH range of 7.0-9.0 and at the temperature below $60^{\circ}C$. The activity of purified enzyme was inhibited by $Hg^{2+}$, $Cu^{2+}$, $Zn^{2+}$, $Ba^{2+}$ and $Fe^{2+}$, whereas activated by $Mn^{2+}$ and $Ca^{2+}$. $\varepsilon$-Amino caproic acid, 2,4-dinitrophenol and iodine did not show inhibitory effect on the activity of alkaline protease, but p-chloromercuribenzoic acid, ethylendiaminetetraacetic acid showed inhibitory effect on the enzyme activity. These result suggested that the protease was metalloenzyme, and require a reactive SH group for the activity. The reaction of this enzyme follows typical Michaelis-Menten kinetics with the $K_m$ value of $2.229{\times}10^{-4}$M and the $V_{max}$ of $46.08 {\mu}$g/min for casein. The activation energy for the alkaline protease calculated by Arrhenius equation was 3.643 kcal/mol. This enzyme hydrolyzed casein more rapidly than the hemoglobin and egg albumin.

• Journal of Ginseng Research
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• v.41 no.3
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• pp.307-315
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• 2017

Background: Red-skin root disease has seriously decreased the quality and production of Panax ginseng (ginseng). Methods: To explore the disease's origin, comparative analysis was performed in different parts of the plant, particularly the epidermis, cortex, and/or fibrous roots of 5-yr-old healthy and diseased red-skin ginseng. The inorganic element composition, phenolic compound concentration, reactive oxidation system, antioxidant concentrations such as ascorbate and glutathione, activities of enzymes related to phenolic metabolism and oxidation, and antioxidative system particularly the ascorbate-glutathione cycle were examined using conventional methods. Results: Aluminum (Al), iron (Fe), magnesium, and phosphorus were increased, whereas manganese was unchanged and calcium was decreased in the epidermis and fibrous root of red-skin ginseng, which also contained higher levels of phenolic compounds, higher activities of the phenolic compound-synthesizing enzyme phenylalanine ammonia-lyase and the phenolic compound oxidation-related enzymes guaiacol peroxidase and polyphenoloxidase. As the substrate of guaiacol peroxidase, higher levels of $H_2O_2$ and correspondingly higher activities of superoxide dismutase and catalase were found in red-skin ginseng. Increased levels of ascorbate and glutathione; increased activities of $\text\tiny L$-galactose 1-dehydrogenase, ascorbate peroxidase, ascorbic acid oxidase, and glutathione reductase; and lower activities of dehydroascorbate reductase, monodehydroascorbate reductase, and glutathione peroxidase were found in red-skin ginseng. Glutathione-S-transferase activity remained constant. Conclusion: Hence, higher element accumulation, particularly Al and Fe, activated multiple enzymes related to accumulation of phenolic compounds and their oxidation. This might contribute to red-skin symptoms in ginseng. It is proposed that antioxidant and antioxidative enzymes, especially those involved in ascorbate-glutathione cycles, are activated to protect against phenolic compound oxidation.

• Korean Journal of Environmental Agriculture
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• v.27 no.4
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• pp.456-459
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• 2008

Quality of rice grain changes during dry storage with internal physiological changes and external injury by organism. Storage rice changes by condition with respiration via variable temperature, hydrolysis enzyme reaction, lipid peroxidation occurs with change of palatability. During dry storage, physiological change with protein variation pattern was examined by image analysis on proteomic technology. Analysis revealed that protein activity had no change store at room temperature and store at $40^{\circ}C$, but decreased store at $60^{\circ}C$. Analysis of variable hydrophobic protein pattern revealed that protein activity of beta-tubulin, protein disulfide isomerase, vacuolar ATPase b subunit, globulin was not significantly decreased all dry and store condition. However, heat shock protein 70, and glutathione transferase was significantly decreased when rice dried at $60^{\circ}C$ compared with room temperature and $40^{\circ}C$ dry condition.

• KSBB Journal
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• v.14 no.1
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• pp.103-108
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• 1999

A bacterium having strong fibrinolytic activity, S7-16 strain, was isolated from soil. The isolated bacterium was identified and named as Bacillus sp. S7-16. The optimal composition of the medium for the production of fibrinolytic enzyme by Bacillus sp. S7-16 was 0.5%(w/v) polypeptone, 0.5%(w/v) yeast extract, 0.3%(w/v) NaCl, 0.1% (w/v) $KH_2PO_4,\;0.3%(w/v)\;K_2PHO_4,\;and\;0.01%(w/v)\;MgSO_4{\cdot}7H_2O$. The optimal temperature and initial pH of the medium for the production of the enzyme were $35^{\circ}C$ and 7.0, respectively. The maximum production of the fibrinolytic enzyme was obtained after 24 hours of the incubation. Under the above conditions, the culture supernatant had strong fibrinolytic activity. Within pH4~11, the crude fibrinolytic enzyme was stable. The enzyme was stable up to $50^{\circ}C$. The optimum pH and temperature for the enzyme activity were around 7.5 and $40^{\circ}C$, respectively.

• Microbiology and Biotechnology Letters
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• v.21 no.3
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• pp.263-268
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• 1993

Seventeen strains were isolated from soil, cattle rumen, cereal sewage dregs, insect on agar plate containing insoluble glucan as a sole carbon source from immobilized Streptococcus mutans, which produced alpha-1,3 glucanase for lysis of dental plaque. Among these strains isolated from soil, SW-522 and SW-713 that had appeared to produce the high level of alpha-1,3 glucanase, degraded insoluble glucan from S. mutans 97.6% and 49.4%, respectively in 5 hours. The activity of crude alpha-1,3 glucanase from SW-522 was 1.3mg insoluble glucan/min.mg protein. This enzyme was entirely degraded insoluble glucan on glass tube which produced by S. mutans in TH medium with 5% sucrose.

• Journal of Microbiology and Biotechnology
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• v.7 no.5
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• pp.305-309
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• 1997

Bacillus stearothermophilus No. 236, an effective xylanolytic bacterium, produced an extracellular carboxymethyl cellulase when the strain was grown on xylan. The carboxymethyl cellulase was purified to homogeneity as judged by SDS-PAGE and zymogram, The carboxymethyl cellulase had a pI of 4.0, and a molecular mass of 95 kDa. The highest level of enzyme activity was observed at pH 6.5 and $60^{\circ}C$. The $K_m$, and $V_{max}$ values of the enzyme to carboxymethyl cellulose were 20.8 mg/ml and $0.63 {\mu}mole$/min/mg protein, respectively, The enzyme was found to act also on filter paper and xylan as well as carboxymethyl cellulose. Therefore, it is expected that this xylanolytic strain isolated from soil could be efficiently used for xylan biodegradation.

• Microbiology and Biotechnology Letters
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• v.21 no.3
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• pp.256-262
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• 1993

Nine novel cyclodextrin glycosytransferase-producing bacteria were isolated from soil in a low acidic pH (3-4) medium at high temperature (45-60C). The isolated acidophilic bacteria were identified as Bacillus acidocaldarius. Highest yield of enzyme was obtained by using the following medium: 4% raw potato, 1% peptone, 0.1% yeast extract, 0.02% (NH4)2SO4, 0.05% MgSO4, 0.02% CaCl2, 0.3% KH2PO4. The crude enzyme showed a very broad pH-activity curve and had two optium pH ranges at 30 and 5.0-6.0. The crude enzyme was most active at 90C.

• Journal of Microbiology and Biotechnology
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• v.19 no.12
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• pp.1514-1519
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• 2009

A gene encoding the xylanase of Bacillus subtilis AMX-4 isolated from soil was cloned into Escherichia coli and the gene product was purified from the cell-free extract of the recombinant strain. The gene, designated xylA, consisted of 639 nucleotides encoding a polypeptide of 213 residues. The deduced amino acid sequence was highly homologous to those of xylanases belonging to glycosyl hydrolase family 11. The molecular mass of the purified xylanase was 23 kDa as estimated by SDS-PAGE. The enzyme had a pH optimum of 6.0-7.0 and a temperature optimum of $50-55^{\circ}C$. Xylanase activity was significantly inhibited by 5 mM $Cu^{2+}$ and 5 mM $Mn^{2+}$, and noticeably enhanced by 5 mM $Fe^{2+}$. The enzyme was active on xylans including arabinoxylan, birchwood xylan, and oat spelt xylan, but it did not exhibit activity toward carboxymethylcellulose or p-nitrophenyl-$\beta$-xylopyranoside. The predominant products resulting from xylan and xylooligosaccharide hydrolysis were xylobiose and xylotriose. The enzyme could hydrolyze xylooligosaccharides larger than xylotriose.

• Microbiology and Biotechnology Letters
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• v.31 no.2
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• pp.157-164
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• 2003

An alkali-tolerant bacterium producing the xylanase was isolated from soil and identified as Bacillus alcaiophilus. This strain, named B. alcalophilus AX2000, was able to grow and produce xylanase optimally at pH 10.5 and $37^{\circ}C$. The maximum xylanase production was obtained when 0.5%(w/v) birchwood xylan and 0.5%(w/v) polypeptone and yeast extract were used as carbon source and nitrogen source, respectively. The biosynthesis of xylanase was under the catabolite repression by glucose in the culture medium, and inhibited in the presence of high concentration of xylose. The maximum activity of xylanase was observed at pH 10.0 and $50^{\circ}C$ and the enzyme activity remained was over 80% at $60^{\circ}C$ and from pH 5.0 to 11.0.

• Microbiology and Biotechnology Letters
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• v.50 no.2
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• pp.245-254
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• 2022

Cellulases are a group of biocatalyst enzymes that are capable of degrading cellulosic biomass present in the natural environment and produced by a large number of microorganisms, including bacteria and fungi, etc. In the current study, we isolated, screened and characterized cellulase-producing bacteria from soil. Three cellulose-degrading species were isolated based on clear zone using Congo red stain on carboxymethyl cellulose (CMC) agar plates. These bacterial isolates, named as HB2, HS5 and HS9, were subsequently characterized by morphological and biochemical tests as well as 16S rRNA gene sequencing. Based on 16S rRNA analysis, the bacterial isolates were identified as Bacillus cerus, Bacillus subtilis and Bacillus stratosphericus. Moreover, for maximum cellulase production, different growth parameters were optimized. Maximum optical density for growth was also noted at pH 7.0 for 48 h for all three isolates. Optical density was high for all three isolates using meat extract as a nitrogen source for 48 h. The pH profile of all three strains was quite similar but the maximum enzyme activity was observed at pH 7.0. Maximum cellulase production by all three bacterial isolates was noted when using lactose as a carbon rather than nitrogen and peptone. Further studies are needed for identification of new isolates in this region having maximum cellulolytic activity. Our findings indicate that this enzyme has various potential industrial applications.