• Microbiology and Biotechnology Letters
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• v.23 no.6
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• pp.687-694
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• 1995

Alkalophilic Bacillus sp. HJ-12 producing $\beta $-1, 4-D-arabinogalactanase was isolated from soil in the alkalic condition, pH 10.0. $\beta $-1, 4-D-arabinogalactanase was maximaly produced in the medium consisting of 2% soybean arabinogalactan (SAG), 0.5% yeast extract, 0.5% polypeptone, 0.5% NaCl, 0.1% K$_{2}$HPO$_{4}$, 0.02% MgSO$_{4}$$\cdot $7H$_{2}$O, 0.1% Na$_{2}$CO$_{3}$ under the aerobic condition (pH 8.2). $\beta $-1, 4-D-arabinogalactanase is inducible enzyme so that its activity has been increased 10 fold in the SAG medium than in the glucose medium. Through the ammonium sulfate precipitation, DEAE- Sephadex A-50 ion chromatography, and Sephadex G-75 gel chromatography procedures, this enzyme was purified with a single protein of 11% vield and 110 fold's purity. $\beta $-1, 4-D-arabinogalactanase is endo type enzyme producing ollgosaccharide from SAG.

• Journal of Microbiology and Biotechnology
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• v.10 no.2
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• pp.187-194
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• 2000

An actinomycetes strain, T-2, which produces transglutaminase (EC 2.3.2.13), was isolated from soil and identified as belonging to the Actinomadura sp., based on taxonomc studies. The conditions for the transglutaminase production and its enzymatic properties were investigated. The optimum components for the transglutaminase production were 2% glucose, 1% polypeptone and soytone, and 0.1% MnCl2. The optimum pH and temperature of the enzyme reaction were pH 8.0 and $45^{\circ}C$, respectively. The enzyme was stable within the pH range of 5.0-9.0 and $30^{\circ}C-45^{\circ}C$. The novel enzyme required no calcium ions for its activity. This enzyme polymerized various proteins such as casien, soy protein, hemoglobin, egg white, gelatin, and soybean milk.

• Microbiology and Biotechnology Letters
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• v.24 no.2
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• pp.143-148
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• 1996

Thousand actinomycetes and 50 soil samples were used for the isolation of microorganisms producing yeast cell wall lytic enzymes. Among 493 strains producing large clear zones on autolysed washed yeast (AWY), 117 strains were selected on living yeast cell agar plates. With the method of lytic activity, one strain (St-1702) was selected, which was temporarily identified as Streptomyces eurythermus. The optimal condition for enzyme production of this strain was partially determined as follows: incubation of the strain for 3 days at 30$\circ$C in the medium containing 2% freeze dried yeast cell, 1% glucose, 1% K$_{2}$HPO$_{4}$, 0.01% MgSO$_{4}$'7H$_{2}$O, 0.5% peptone, and 0.2% (NH$_{4}$)$_{2}$CO$_{3}$ with pH 7.0. The protoplast formation of yeast by using the enzyme produced by this strain was compared with commercial enzymes.

• The Korean Journal of Food And Nutrition
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• v.13 no.2
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• pp.176-180
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• 2000

Microbial protease has been interesting due to the biological roles in the producing microorganism. A thermophilic Actinomyces produing protease was isolated from soil. The optimal medium composition and culture conditions for maximum protease production was as follows 0.5% soluble starch, 0.5% yeast extract. 0.1% K2HPO4, 0.05% CaCl2, initial pH 8.0 at 50$^{\circ}C$ for 48hours. The protease was purified by the procedure of ammonium sulfate precipitation, anion exchange chromatography(LC), DEAE high performance liquid chromatography and GPC HPLC. The purification fold of the purified enzyme was increased about 22.6. The optimal pH and temperature for reaction of the purified enzyme were 7.5 and 60$^{\circ}C$. The purified enzyme was stable for the pH range from 6.0 to 8.5, but was unstable when treated at 80$^{\circ}C$ for 10 minutes. The activity of the enzyme was inhibited by Ag+ and Cu2+.

• Journal of Microbiology and Biotechnology
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• v.27 no.12
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• pp.2180-2189
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• 2017

Psychrophilic phytases suitable for aquaculture are rare. In this study, a phytase of the histidine acid phosphatase (HAP) family was identified in Morchella importuna, a psychrophilic mushroom. The phytase showed 38% identity with Aspergillus niger PhyB, which was the closest hit. The M. importuna phytase was overexpressed in Pichia pastoris, purified, and characterized. The phytase had an optimum temperature at $25^{\circ}C$, which is the lowest among all the known phytases to our best knowledge. The optimum pH (6.5) is higher than most of the known HAP phytases, which is fit for the weak acidic condition in fish gut. At the optimum pH and temperature, MiPhyA showed the maximum activity level ($2,384.6{\pm}90.4{\mu}mol{\cdot}min^{-1}{\cdot}mg^{-1}$, suggesting that the enzyme possesses a higher activity level over many known phytases at low temperatures. The phytate-degrading efficacy was tested on three common feed materials (soybean meal/rapeseed meal/corn meal) and was compared with the well-known phytases of Escherichia coli and A. niger. When using the same amount of activity units, MiPhyA could yield at least $3{\times}$ more inorganic phosphate than the two reference phytases. When using the same weight of protein, MiPhyA could yield at least $5{\times}$ more inorganic phosphate than the other two. Since it could degrade phytate in feed materials efficiently under low temperature and weak acidic conditions, which are common for aquacultural application, MiPhyA might be a promising candidate as a feed additive enzyme.

• Mycobiology
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• v.46 no.3
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• pp.224-235
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• 2018

Temperature is an important environmental factor that can greatly influence the cultivation of Auricularia cornea. In this study, lignin peroxidase, laccase, manganese peroxidase, and cellulose in A. cornea fruiting bodies were tested under five different temperatures ($20^{\circ}C$, $25^{\circ}C$, $30^{\circ}C$, $35^{\circ}C$, and $40^{\circ}C$) in three different culture periods (10 days, 20 days and 30 days). In addition, the V4 region of bacterial 16S rRNA genes in the substrate of A. cornea cultivated for 30 days at different temperatures were sequenced using next-generation sequencing technology to explore the structure and diversity of bacterial communities in the substrate. Temperature and culture days had a significant effect on the activities of the four enzymes, and changes in activity were not synchronized with changes in temperature and culture days. Overall, we obtained 487,694 sequences from 15 samples and assigned them to 16 bacterial phyla. Bacterial community composition and structure in the substrate changed when the temperature was above $35^{\circ}C$. The relative abundances of some bacteria were significantly affected by temperature. A total of 35 genera at five temperatures in the substrate were correlated, and 41 functional pathways were predicted in the study. Bacterial genes associated with the membrane transport pathway had the highest average abundance (16.16%), and this increased at $35^{\circ}C$ and $40^{\circ}C$. Generally, different temperatures had impacts on the physiological activity of A. cornea and the bacterial community in the substrate; therefore, the data presented herein should facilitate cultivation of A. cornea.

• Korean Journal of Soil Science and Fertilizer
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• v.38 no.5
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• pp.281-286
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• 2005

The effect of oyster shell meal, which is made of a simple crushing and alkaline calcium materials, on soil microbial properties, microbial biomass C, N and P contents, and enzyme activities were evaluated in silt loam soil. The oyster shell meal fertilizer was added at the rates of 0, 4, 8, 12 and $16Mg\;ha^{-1}$. Microbial biomass C, N and P contents were significantly increased with increasing application of oyster shell meal. Soil enzyme activities, such as urease, ${\beta}$-glucosidase and alkaline phosphomonesterase were increased significantly by shell meal application, due to increased soil pH towards neutral range and increased nutrient availability in soil. In particular, the increased microbial biomass P content and phosphomonoesterase activities were strongly correlated with available P content in soil. Conclusively, oyster shell meal fertilizer could be a good supplement to improve soil microbial activities.

• Korean Journal of Soil Science and Fertilizer
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• v.45 no.1
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• pp.66-73
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• 2012

Plant growth promoting traits like production of indoleacetic acid (IAA), ammonia, hydrogen cyanide (HCN), siderophore, and like the enzyme activities of catalase, ACC deaminase, cellulase, chitinase and protease were assayed in vitro for twenty one phosphorus solubilizing bacteria isolated from soil isolates. Except SPP-5 and SPP-15 strains, all the other isolated strains produced IAA in various amounts of 10 to $23{\mu}g\;ml^{-1}$. All strains showed positive response for ammonia production and ACC deaminase activity implying that they are capable of growing in a N-free basal medium. Catalase activity was found to be superior in SPP-2, SPP-7, SPP-12 and SPP-17 compared to the other strains tested. HCN production was detected by 15 strains and among them SPP-9, SPP-15, SAph-11, and SAph-24 were found to be strong HCN producers. Except the isolates SPP-10, SPP-12, SPP-13 and SPP-14, all the other isolates produced more than 80% siderophore units. None of the strains showed cellulose and chitinase activity. SAph-8, SAPh-11, SAPh-24 and SPP-15 strains showed 35.84, 50.33, 56.64 and 34.78 U/ml protease activities, respectively. SPP-1, SPP-2, SPP-3, SPP-11, SPP-17, SPP-18, SAph-11 and SAph-24 strains showed positive response for all the tested plant growth promotion traits except cell wall degrading enzyme activities. According to the results, all the tested phosphorus solubilizing isolates could exhibit more than three or four plant growth promoting traits, which may promote plant growth directly or indirectly or synergistically. Therefore, these phosphorus solubilizing strains could be employed as bio-inoculants for agriculture soils.

• Journal of Korean Society of Forest Science
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• v.87 no.1
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• pp.106-112
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• 1998

This study was conducted to figure out the relationships among soil chemical properties and bacterial biomass related to denitrification and sulfur-reducing and the activity of dehydrogenase, and ultimately to consider the usefulness of dehydrogenase activity as a tool for evaluating the dynamics of forest soil ecosystem. Four sites were selected for the collection of soil samples within two regions(Onsan industrial estate as a polluted region and Mt. Mani at Kanghwa island as a clean area) with two forest types (coniferous and deciduous stands). The soils of Mt. Mani showed higher amount of organic matter, total nitrogen and available phosphorus than those collected from Onsan industrial estate, which indicated that the soils were more beneficial for microbial growth than those of Onsan. The dehydrogenase activity was more sensitive than the denitrifying bacteria or sulfur-reducing bacteria since the activity was significantly different between the regions and season while the two bacterial biomass were not significantly different between the two regions. In addition, the dehydrogenase activity showed relatively high correlation coefficients with organic matter(r=0.53, p=0.004), total nitrogen(r=0.41, p=0.008) and C/Ava. P-ratio(r=-0.52, p=0.001), which was thought to be closely related with microbial activity. Thus, the dehydrogenase activity was thought to be a useful index of soil ecosystem dynamics with considering that the technique need to be applied with the same soil texture for the comparison of the activity as other researchers indicated.

• Microbiology and Biotechnology Letters
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• v.2 no.1
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• pp.13-17
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• 1974

A strain of Streptomyces sp. which producing a metal containing proteolytic enzyme was isolated from soil and some properties of this enzyme were investigated. The following results were obtained. 1. Optimal pH and temperature of this enzyme were pH7.0 and 37$^{\circ}C$ 2. This enzyme was easily inactivated with heat treatment: for example, by the treatmentat 37$^{\circ}C$ for 100 minutes the activity of the enzyme was decreased to about 50 per cent of intial actively but this enzyme was stable at neutral pH. 3. The activity of this enzyme was not inhibited by $Mg^{＋＋}$, $_Mn^{＋＋}$, $Ca^{＋＋}$, Pb$^{＋＋}$, or $Ba^{＋＋}$ ect. but strongly inhibited by Hg$^{＋＋}$, Co$^{＋＋}$, Ag$^{＋}$, Cu$^{＋＋}$, or Cd$^{＋＋}$. 4. This enzyme was strongly inhibited by EDTA but was not inhibited by oxalic acid, citric acid, 2, 4-dinitrophenol, $\varepsilon$-aminocaproic acid, cysteine, or thiourea.