• Journal of Microbiology
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• v.45 no.6
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• pp.521-527
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• 2007

Several yeast strains degrading malic acid as a sole carbon and energy source were isolated from Korean wine pomace after enrichment culture in the presence of malic acid. Among them, the strain designated as KMBL 5774 showed the highest malic acid degrading ability. It was identified as Issatchenkia orientalis based on its morphological and physiological characteristics as well as the nucleotide sequences of the internal transcribed spacer (ITS) 1-5.8S rDNA-ITS II region. Phylogenetic analysis of the ITS I-5.8S rDNA-ITS II sequences showed that the KMBL 5774 is the closest to I. orientalis zhuan 192. Identity of the sequences of the KMBL 5774 was 99.5% with those of I. orientalis zhuan 192. The optimal pH of the media for the growth and malic acid degradation by the yeast was between 2.0 and 3.0, suggesting that the strain is an acidophile. Under the optimized conditions, the yeast could degrade 95.5% of the malic acid after 24 h of incubation at $30^{\circ}C$ in YNB media containing 2% malic acid as a sole carbon and energy source.

• 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.

• Economic and Environmental Geology
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• v.43 no.2
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• pp.109-121
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• 2010

The bioleaching experiment under $42^{\circ}C$ was effectively carried out to leach the more valuable element ions from the pyrite in the Gangyang mine waste. Bacteria can survive at this temperature, as indigenous acidophilic bacteria were collected in the Hatchobaru acidic hot spring, in Japan. To enhance the bacterial activity, yeast extract was added to the pyrite-leaching medium. The indigenous acidophilic bacteria appeared to be rod-shaped in the growth-medium which contained elemental sulfur and yeast extract. The rod-shaped bacteria ($0.7\times2.6\;{\mu}m$, $0.6\times7\;{\mu}m$, $0.8\times5\;{\mu}m$ and $0.7\times8.4\;{\mu}m$) were attached to the pyrite surface. The colonies of the rod-shaped bacteria were selectively attached to the surroundings of a hexagonal cavity and the inner wall of the hexagonal cavity, which developed on a pyrite surface. Filament-shaped bacteria ranging from $4.92\;{\mu}m$ to $10.0\;{\mu}m$ in length were subsequently attached to the surrounding cracks and inner wall of the cracks on the pyrite surface. In the XRD analysis, the intensity of (111), (311), (222) and (320) plane on the bacteria pyrite sample relatively decreased in plane on the control pyrite sample, whereas the intensity of (200), (210) and (211) increased in these samples. The microbiological leaching content of Fe ions was found to be 3.4 times higher than that of the chemical leaching content. As for the Zn, microbiological leaching content, it was 2 times higher than the chemical leaching content. The results of XRD analysis for the bioleaching of pyrite indicated that the indigenous acidophilic bacteria are selectively attacked on the pyrite specific plane. It is expected that the more valuable element ions can be leached out from the mine waste, if the temperature is increased in future bioleaching experiments.

• Food Science and Preservation
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• v.19 no.2
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• pp.308-314
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• 2012

Two hundred and twenty three yeast strains were randomly isolated from Korean traditional $nuruk$. Among them, six urease producing yeast strains (designated JJA, JJB, JJ22, SHA, SHC and SH10) were selected on the Christensen urea agar plates. They showed the same pattern in the PCR-RFLP analysis of the ITS I-5.8S-ITS II region digested with $Hae$III and $HinF$1 restriction endonucleases. Its DNA sequences showed 100% (strains SHA, SHC and SH10) and 99.8% (strains JJA, JJB and JJ22) identity with those of $Issatchenkia$ $orientalis$ type strain ATCC 24210. Phylogenetic analysis resulted in that all the strains were closely related to $I.$ $orientalis$. Two representative strains, JJ22 and SH10, showing the highest urease activities were selected for further characterization. Their morphological, physiological and biochemical characteristics were also the same as $I.$ $orientalis$. Therefore, both the two strains were identified as $I.$ $orientalis$. They could grow at a wide range of temperature between $20-40^{\circ}C$ as well as pH between 2.0 and 10.0. However, a higher level urease activity were obtained at acidic pH than that at alkalic pH. The maximal level of urease activity was obtained at $30^{\circ}C$ (strain SH10) or $35^{\circ}C$ (strain JJ22) and in a liquid medium adjusted to the initial pH 5.0.

• Journal of Microbiology and Biotechnology
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• v.8 no.4
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• pp.353-360
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• 1998

A bacterial strain PN33 producing large amounts of extracellular pectin lyase (PNL, EC 4.2.2.10) was isolated from soil. The isolated bacterium was identified as a strain of Bacillus sp. Production of PNL by the strain was induced only by pectins, with a higher degree of esterification, which had been added to the culture medium as a sole carbon source. The optimal medium for PNL production was determined to consist of 10 g pectin, 2 g yeast extract, 4 g $K_2HPO_4{\cdot}3H_2O$, 0.6 g $MgSO_4$, and 0.11 g $CaCl_2$ per liter (pH 7.0). The PNL activity in the culture supernatant reached the highest level of 132 mU/ml after 32 h cultivation at $37^{\circ}C$ in the optimal medium. The PNL produced was purified to homogeneity by ammonium sulfate fractionation (50~80%), and cation exchange and size exclusion chromatographies. The molecular mass of the enzyme was estimated to be approximately 52 kDa by SDS-PAGE. Almost the same mass was determined by nondenaturing PAGE, indicating that the functional enzyme had a monomeric structure. As expected, the PNL exhibited higher activities on the highly esterified pectins whereas it gave no detectable activity on polygalacturonic acid. The enzyme showed the highest activity at the acidic pH of 6.0, exceptional for a bacterial PNL. Maximum activity was measured at $40^{\circ}C$, although the stability f the purified enzyme was poor at this temperature. alcium (1 mM) was found to activate the PNL activity by $50\%$, and also remarkably increased the thermal stability f the enzyme. Phenylmethylsulfonylfluoride (PMSF) and iethylpyrocarbonate (DEPC) inhibited the PNL activity lmost completely at the concentration of 5 mM. This result ndicates that some serine and histidine residues of the nzyme may play an essential role for catalytic function of he enzyme.