• Title/Summary/Keyword: Alkalophilic Bacillus

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Production and Characteristics of Lytic Enzyme against Streptococcus mutans Cell Wall from Alkalophilic Bacillus sp. 4830 (호알카리성 Bacillus sp. 4830이 생산하는 Streptococcus mutans 세포벽 분해효소의 분리와 특성)

  • Kim, Yun-Keun;Bai, Dong-Hoon
    • Korean Journal of Food Science and Technology
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    • v.35 no.6
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    • pp.1143-1149
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    • 2003
  • To elucidate a method of preventing dental caries, strains producing lytic enzymes were isolated and their characteristics were investigated. Among 5,00 alkalophilic strains isolated from soil, 22 strains showed lytic activity against Streptococcus mutans. Strain No. 4830, with the highest lytic activity, was selected for further study. Strain 4830 showed 94% sequence homology with the 16S rDNA sequence of Bacillus alcalophilus, but it was concluded to be different from Bacillus alcalophilus because of its biochemical characteristics. The strain was named Bacillus sp. 4830. The lytic enzyme from Bacillus sp. 4830 was purified by ethanol precipitation and CM-agarose column chromatography. The molecular weight of the lytic enzyme was determined to be 28 kDa by SDS-PAGE. The lytic enzyme was stable between pH 5.0 and pH 11 and up to $40^{\circ}C$. The optimal pH and temperature for the lytic activity was 9.0 and $50^{\circ}C$, respectively.

Nucleotide Sequence of a Bacteriolytic Enzyme Gene from Alkalophilic Bacillus sp.

  • Jung, Myeong-Ho;Ohk, Seung-Ho;Yum, Do-Young;Kong, In-Soo;Bai, Dong-Hoon
    • Journal of Microbiology and Biotechnology
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    • v.3 no.2
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    • pp.73-77
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    • 1993
  • The nucleotide sequence of Bacillus sp. bacteriolytic enzyme gene, lytP and its flanking regions were determined. A unique open reading frame for a protein of Mw. 27, 000, and a putative terminator sequence, were found behind a concensus ribosome binding site located 8 nt upstream from ATG start codon. The primary amino acid sequence deduced from nucleotide sequence revealed a putative protein of 255 amino acid residues with an Mw. of 27, 420. No significant homology could be found between the amino acid sequence of Bacillus sp. bacteriolytic enzyme and that of other cell wall hydrolases.

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Studios on the Glutamic Acid Production by an Alkalophilic Bacterium (알칼리성 세균에 의한 글루탐산 생산에 관한 연구)

  • Cho, Kae-Ran;Lee, Kang-Man;Bae, Moo
    • Microbiology and Biotechnology Letters
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    • v.17 no.6
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    • pp.563-567
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    • 1989
  • An alkalophilic bacterium isolated from compost was selected, identified and tested for the production of glutamic acid from ammonium fumarate. The bacterium was closely related to Bacillus brevis. The conditions for glutamic acid production were pH 8.0, 2% fumaric acid, and 0.8% nutrient broth. The mechanism of glutamic acid formation in this strain was postulated as following scheme. (1) Ammonium fumarate longrightarrow Aspartic acid (2) Aspartic acid + $\alpha$-Ketoglutaric acid longrightarrow Glutamic acid + Oxaloacetic acid.

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Characteristics of the Egg White Lysozymes from Ogol Fowl and Fowl for the Lysis of an Alkalophilic and Thermophilic Bacillus sp. TA-11 (호알칼리성, 고온성 Bacillus sp. TA-11에 대한 오골계 난백 Lysozyme의 용균특성)

  • 이성훈;조창호;안용근;이종수
    • The Korean Journal of Food And Nutrition
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    • v.9 no.4
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    • pp.447-451
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    • 1996
  • Lytic activities of the egg white lysozyme from Korea-native Ogol fowl against the alkalophilic and thermophilic Bacillus sp. TA-11 were investigated and compared. Lytic activity of the Ogol fowl lysozyme for Bacillus sp. TA-11 was the highest for the cell of post-logarithm phase and optimum concentration of the lysozyme was 0.25%, Optimum reaction pH and temperature were 4.5 and 35$^{\circ}C$, respectively. Lytic activity of egg white lysozyme from fowl for Bacillus sp. TA-11 was the highest for the cell of stationary phase and optimum concentration of the lysozyme was 0.5%. Optimum reaction pH and temperature were 5.5 and 4$0^{\circ}C$, respectively.

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Selection of the Constitutive Mutant of Bacillus firmus var. alkalophilus and its Characteristics of Cydodextrin Glucanotransferase Production

  • Lee, Yong-Hyun;Kim, Chan;Lee, Yong-Hyun
    • Journal of Microbiology and Biotechnology
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    • v.5 no.2
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    • pp.61-67
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    • 1995
  • To investigate the role of induction on CGTase production for alkalophilic Bacillus firm us var. alkalophilus H609, the constitutive mutants that form a halo around its colonies at non-inducible AG agar media containing amylose and glucose were selected. The selected constitutive mutants could produce CGTase in the range of 18.9 to 28.8 units/ml $\cdot A_{600}$ in the alkaline basal medium, and finally a constitutive mutant Bacillus firmus var. alkalophilus CM46 was selected. The constitutive nature of CM46 was also confirmed in protein level using SDS-PAGE. The effects of induction and catabolite repression for both parent strain Bacillus firmus var. alkalophilus H609 and constitutive mutant CM46 were also compared by adding soluble starch and glucose during cultivation. The selected mutant CM46 was a non-inducible but a catabolite regulated type mutant. Even though inductive regulation was released, the specific CGTase activity defined as CGTase activity per cell concentration was not increased compared with that of parent strain. The cell growth and CGTase production patterns of constitutive mutant Bacillus firmus var. alkalophilus CM46 were compared with the parent strain to identify CGTase production characteristics.

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Molecular Cloning and Expression of Alkaline Amylase Gene of Alkalophilic Bacillus sp. in Bacillus subtilis and Escherichia coli (알카리성 Bacillus sp.의 호알카리성 amylase 유전자의 Bacillus subtilis와 Escherichia coli로의 cloning과 발현)

  • Bae, Moo;Park, Shin-Hae
    • Microbiology and Biotechnology Letters
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    • v.17 no.2
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    • pp.160-164
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    • 1989
  • A 5.7Kb EcoRI fragment containing alkaline amylase gene of Bacillus sp. AL-8 obtained in the previons experiment (10) was transformed in B. subtilis via plasmid pUB110. The enzymatic proper-ties of the amylase produced by the transformants were Identical to those of the donor strain. Thus, the alkaline amylase activity from the transformant was maximum at pH 10 and 5$0^{\circ}C$. And the enzyme was very stable over the ranges of alkaline pH. In order to determine the location of the alkaline amylase gene within the 5.7Kb DNA fragment, the fragment was subcloned in E. coli. It was found that the alkaline amylase gene was located k EcoRI fragment of 3.7Kb.

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Biosynthetic Regulation of Intracellular Invertase from Alkalophilic and Thermoplilic Bacillus cereus TA-11 (호알칼리성, 고온성 Bacillus cereus TA-11으로 생산된 세포내 Invertase의 생합성 조절)

  • Yi, Sung-Hun;Song, Jung-Eun;Lee, Jong-Soo
    • The Journal of Natural Sciences
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    • v.18 no.1
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    • pp.29-38
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    • 2007
  • Regulation of invertase biosynthesis was studied with alkalophilic and thermophilic Bacillus cereus TA-11. Biosynthesis of invertase in Bacillus cereus TA-11 was effectively induced in the presence of 10 mM of sucrose for 180 min and 25 mM of raffinose for 90 min, respectively. Glucose repressed the invertase induction by sucrose and as late addition time of glucose, invertase formation was increased, indicating that glucose repression was occurred by inducer exclusion. Catabolite repression was not reduced by the addition of cAMP for 180 min of induction.

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Isolation of Novel Alkalophilic Bacillus alcalophilus subsp. YB380 and the Characteristics of Its Yeast Cell Wall Hydrolase

  • Yeo, Ik-Hyun;Han, Suk-Kyun;Yu, Ju-Hyun;Bai, Dong-Hoon
    • Journal of Microbiology and Biotechnology
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    • v.8 no.5
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    • pp.501-508
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    • 1998
  • An alkalophilic mi.croorganism (strain YB380), which produces yeast cell wall hydrolase extracellulary, was isolated from Korean soil. The rod-shaped cells were 0.3~0.4 by 2~4${\mu}{\textrm}{m}$ long, motile, aerobic, gram-positive, and spore-forming. The color of the colony was light yellow. The temperature range for growth at pH 9.0 was 25 to $45{\circ}C, with optimum growth at $35{\circ}C. The pH range for growth at $35{\circ}C was 8 to 11 with an optimum pH of 9.0. Therefore, the strain YB380 is an obligate alkalophile. The 16S rRNA of strain YB380 has a 99% sequence similarity with that of Bacillus alcalophilus. On the basis of physiological properties, cell wall fatty acid composition, and phylogenetic analysis, we propose that the isolated strain is Bacillus alcalophilus. The yeast cell wall hydrolase from Bacillus alcalophilus subsp. YB380 has been purified and partially characterized. The molecular weight was estimated to be 27,000 daltons with an optimum temperature and pH of $60{\circ}C and 9.0, respectively. The N-terminal amino acid sequence of the enzyme was analyzed as Gln- Thr- Val- Pro- Trp- Gly- Ile- Asn- Arg- Val.

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A study on Alkalophilic Bacteria Producing $\beta$-Galactosidase. -Isolations and Cultural Characteristics (I)- ($\beta$-Galactosidase를 생산하는 호알카리성 세균에 관한 연구 -균주의 분리 및 배양조건 (I)-)

  • Yun, Seong-Sik;Min, Do-Sik;Yu, Ju-Hyeon
    • The Korean Journal of Food And Nutrition
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    • v.1 no.2
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    • pp.68-75
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    • 1988
  • A strain of alkalophilic Bacillus sp. YS-309 has been isolated from domestic soil. It belongs to genus Bacillus from its morphological and biochemical characteristics. The strain grows better in the alkaline media rather than in the neutral media. The optimum pH and temperature for growth were observed at 8.5 and 4$0^{\circ}C$, respectively. Glucose, lactose and maltose were appeared as good carbon source but soluble starch and fructose were utilized uneffectively for growth. Concentrations of lactose had affected both the cellular growth and the enzyme productions. The maximum growth and the highest enzyme productions were obtained at 0.5%(w/e) of lactose added in the media. B-Galactosidase from Bacillus sp. YS-309 was produced inducibly into the cell and total enzyme activities per ml were gradually decreased when the concentration of glucose increased.

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Calcite Production by Bacillus amyloliquefaciens CMB01

  • Lee, Young-Nam
    • Journal of Microbiology
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    • v.41 no.4
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    • pp.345-348
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    • 2003
  • The bio-mediated production of calcite crystals by calcinogenic bacteria has great applicable value for the restoration of deteriorated calcareous monuments, because of its high purity and coherency. An investigation of the conditions for calcite production by an alkalophilic Bacillus amyloliquefaciens CMB01 strain was made. Optimal calcite precipitation occurred when the bacterium was cultured at pH 8.0 and 30$^{\circ}C$, and in B4 medium that consisted of 0.4% yeast extract, 0.5% glucose, and 1.5% calcium acetate. Calcium ion of the bacterially induced calcite was analyzed by an inductively coupled plasma (ICP) spectrophotometer. Optical and scanning electron microscopy (SEM) of the calcite revealed a typical rombohedral polycrystalline structure.