• 제목/요약/키워드: Bacillus subtilis

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전통장류에서 Biogenic Amines 분해 능력을 가지는 Bacillus subtilis 및 Bacillus amyloliquefaciens 균주의 분리 (Isolation of Biogenic Amines-Degrading Strains of Bacillus subtilis and Bacillus amyloliquefaciens from Traditionally Fermented Soybean Products)

  • 김용상;조성호;정도연;엄태붕
    • 미생물학회지
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    • 제48권3호
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    • pp.220-224
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    • 2012
  • 전통 장류 제품 내 유해한 biogenic amines 양을 감소하기 위해, 83종의 전통 장류에서 biogenic amines을 분해할 수 있는 5종의 균주들을 분리하였다. 이들 균주들을 histamine, tyramine, putrescine, cadaverine이 각각 5.3% 함유된 삶은 콩에 접종하여 10일 간 발효시킨 결과 biogenic amines 함량을 27-92% 수준으로 감소시켰다. 선발한 균주들의 형태 및 생화학적 특성, 16S rRNA 유전자 서열 해독 결과 5종의 균주들은 Bacillus subtilis 또는 B. amyloliquefaciens에 속했다. 이 선발 균주들을 사용함으로서 biogenic amines 수준을 제어하기 힘든 전통 장류의 제조에 이 선발 균주들의 사용은 이들 함량을 줄일 수 있는 효과적 방안이 될 수 있다.

Bacillus licheniformis WL-12의 cellulase 유전자 클로닝과 발현 (Cloning and Expression of A Bacillus licheniformis Cellulase Gene)

  • 윤기홍
    • 미생물학회지
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    • 제42권4호
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    • pp.313-318
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    • 2006
  • 가정에서 제조된 된장으로부터 cellulase 생산균으로 분리된 고온성 WL-12는 형태적 특성, 생화학적 성질 및 16S rRNA의 염기서열에 근거하여 Bacillus licheniformis로 동정되었다. B. licheniformis WL-12의 cellulase 유전자를 클로닝하여 그 염기서열을 결정한 결과 cellulase 유전자(celA)는 517 아미노산으로 구성된 단백질을 코드하며 1,551 뉴클레오티드로 이루어졌다. 아미노산 잔기배열을 분석한 결과 WL-12의 cellulase는 활성영역과 cellulose 결합영역으로 구성되어 있었으며, glycosyl hydrolase (GH) family 5에 속하는 B. licheniformis, B. subtilis와 B. amyloliquefaciens의 cellulase와 높은 상동성을 보였다. 클론된 celA를 발현용 vector에 도입하여 B. subtilis에서 발현시켜 cellulase 최대생산성이 7.0 units/ml에 이르렀다.

Probiotics용 복합효소 분비 Bacillus sp.의 분리 및 원료사료를 이용한 균주 생산을 위한 배지 조건의 최적화 (Isolation of Bacillus sp. Producing Multi-enzyme and Optimization of Medium Conditions for Its Production Using Feedstuffs for Probiotics)

  • 양시용;송민동;김언현;김창원
    • 한국미생물·생명공학회지
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    • 제29권2호
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    • pp.110-114
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    • 2001
  • 가축 사료첨가용 probiotics용 균주를 얻기 위해 특히 내열성이 높아 가공사료에 적합한 Bacillus sp.를 위주로 하여 가축에게 유용한 효소인 phytase를 비롯하여 protease, cellulase, xylanase, amylase의 활성을 모두 나타내는 4-3 균주를 얻어 동정한 결과 Bacillus subtilis로 밝혀졌으며, 이를 B. subtilis 4-3으로 명명하였다. 본 균주를 원료사료에 순수배양하여 사료의 항영양인자인 phytic acid 분해율을 검토한 결과 대두박 및 쌀겨에 있어서는 phytic acid 분해율이 낮았으나, 밀기울의 경우 80.63%로 상대적으로 높은 phytic acid 분해율을 나타내었다. 원료 사료를 이용한 균주의 생산 조건은 대두박 1%(w/v)와 당밀 2%(w/v)가 가장 적합한 균주 생산을 위한 배지조성으로 검토되었다.

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Polyacryloyl- 및 Polymethacryloylcephradine의 합성과 항균작용에 관한 연구 (Synthesis and Antimicrobial Activity of Polyacryloyl- and Polymethacryloylcephradine)

  • 김선일;차월석;나재운;김영호;고옥현
    • 대한화학회지
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    • 제36권2호
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    • pp.282-286
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    • 1992
  • Polyacrylic acid와 polymethacrylic acid를 N-hydroxysuccinimide에 반응시켜 poly(N-acryloxysuccinimide)와 poly(N-methacryloxysuccinimide)를 합성하고, 이것과 cephradine을 반응시켜 polyacryloylcephradine과 polymethacryloylcephradine을 합성하였다. 이들 중합체약의 항균성을 2단계 희석법에 의하여 최소 발육저지 농도로서 조사하였다. Polyacryloylcephradine 중합체에 대한 최소 발육저지 농도는 Staphylococcus aureus ATCC 25923, Staphylococcus aureus FDA 209P, Bacillus subtilis ATCC 6633, Bacillus licheniformis ATCC 14580, Escherichia coli BE 1186 및 Salmonella typhimurium TV 119 균주들에 항균성이 대체적으로 우수하였다. Polymethacryloylcephylococcus aureus FDA 209P, Bacillus subtilis ATCC 6633, Escherichia coli BE 1186 및 Salmonella typhimurium TV 119 균주들에 대해서 항균력을 보여주었다.

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Bacillus subtilis와 Lactobacillus bulgaricus에 의한 청국장 단백질의 용해성, 점성, 보수성 및 보유성 (Solubility, Viscosity, Water Holding Capacity, and Oil Holding Capacity of Soybean Proteins by Bacillus subtilis and/or Lactobacillus bulgaricus)

  • 이진우
    • 한국지역사회생활과학회지
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    • 제18권3호
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    • pp.399-406
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    • 2007
  • Soybean seeds were fermented by Bacillus subtilis and/or Lactobacillus bulgaricus to improve solubility, viscosity, water holding capacity and oil holding capacity of soybean proteins in Chongkukjang. The maximum colony forming unit and protease activity of B. subtilis or L bulgaricus were observed after 60 hours of fermentation, and those of the mixed fermentation by two microorganisms were steadily increased during the fermentation periods. Solubilities of soybean proteins by B. subtilis or L bulgaricus were steadily increased before the values were considerably increased to 60 hours of fermentation, whereas water holding capacities of the proteins were decreased by B. subtilis or L. bulgaricus and those of the mixed fermentation were decreased progressively. Viscosities of soybean proteins by B. subtilis and/or L. bulgaricus were decreased progressively during the fermentation. Viscosities of soybean proteins by B. subtilis and/or L. bulgaricus were decreased progressively during the fermentation. Oil holding capacities of soybeans by B. subtilis or L. bulgaricus were maximum at 20 or 80 hours of fermentation and those of the mixed fermentation were decreased after 10 hours of the fermentation.

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Volatile Components of Korean Soybean Paste Produced by Bacillus subtilis PM3

  • JONG-KYU KIM;JI, WON-DAE;SUNG-HO YANG;MYEONG-RAK CHOI
    • Journal of Microbiology and Biotechnology
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    • 제5권3호
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    • pp.143-148
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    • 1995
  • A strain producing soybean paste flavor was isolated from traditional Korean soybean paste. The isolate was identified as Bacillus subtilis PM3. The neutral fraction representing the traditional soybean paste aroma was obtained from the whole volatile components produced by B. subtilis PM3 in cooked soybean. Each separated peak from the neutral fraction of gas chromatogram was identified by gas chromatography-mass spectrometry (GC/MS) and Kovat's retention index, and the aromas of each peak were investigated by a sniffing test with the exercise panel. The twenty-nine components, including six character impact compounds and twelve components of flavors of Korean soybean paste, were confirmed. Some regions of gas chromatogram represented the soybean paste odor. It has been confirmed that traditional Korean soybean paste can be manufactured with the strain B. subtilis PM3.

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Molecular Cloning and Sequencing of Cell Wall Hydrolase Gene of an Alkalophilic Bacillus subtilis BL-29

  • Kim, Tae-Ho;Hong, Soon-Duck
    • Journal of Microbiology and Biotechnology
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    • 제7권4호
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    • pp.223-228
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    • 1997
  • A DNA fragment containing the gene for cell wall hydrolase of alkalophilic Bacillus subtilis BL-29 was cloned into E. coli JM109 using pUC18 as a vector. A recombinant plasmid, designated pCWL45B, was contained in the fragment originating from the alkalophilic B. subtilis BL-29 chromosomal DNA by Southern hybridization analysis. The nucleotide sequence of a 1.6-kb HindIII fragment containing a cell wall hydrolase-encoding gene was determined. The nucleotide sequence revealed an open reading frame (ORF) of 900 bp with a concensus ribosome-binding site located 6 nucleotide upstream from the ATG start codon. The primary amino acid sequence deduced from the nucleotide sequence revealed a putative protein of 299 amino acid residues with an M.W. of 33, 206. Based on comparison of the amino acid sequence of the ORF with amino acid sequences in the GenBank data, it showed significant homology to the sequence of cell wall amidase of the PBSX bacteriophage of B. subtilis.

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Conserved Virulence Factors of Pseudomonas aeruginosa are Required for Killing Bacillus subtilis

  • Park Shin-Young;Heo Yun-Jeong;Choi Young-Seok;Deziel Eric;Cho You-Hee
    • Journal of Microbiology
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    • 제43권5호
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    • pp.443-450
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    • 2005
  • The multi-host pathogen, Pseudomonas aeruginosa, possesses an extraordinary versatility which makes it capable of surviving the adverse conditions provided by environmental, host, and, presumably, competing microbial factors in its natural habitats. Here, we investigated the P. aeruginosa-Bacillus subtilis interaction in laboratory conditions and found that some P. aeruginosa strains can outcompete B. subtilis in mixed planktonic cultures. This is accompanied by the loss of B. subtilis viability. The bactericidal activity of P. aeruginosa is measured on B. subtilis plate cultures. The bactericidal activity is attenuated in pqsA, mvfR, lasR, pilB, gacA, dsbA, rpoS, and phnAB mutants. These results suggest that P. aeruginosa utilizes a subset of conserved virulence pathways in order to survive the conditions provided by its bacterial neighbors.

Poly-γ-Glutamic Acid 고생성 Bacillus spp. 균주의 분리 및 발효특성 (Isolation and Characterization of Bacillus spp. with High-Level Productivity of Poly-γ-Glutamic Acid)

  • 심상협;박홍진;오현화;정도연;송근섭;김영수
    • 한국식품영양과학회지
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    • 제46권9호
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    • pp.1114-1121
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    • 2017
  • 전통장류로부터 식품 유해요소를 생성하지 않는 Bacillus 균주를 분리하여 세포외효소 활성(amylase, protease, cellulase, xylanase)을 측정한 후, 단백질 분해 활성이 우수한 14개 균주와 비교균주 1균주를 선발하였다. 선발된 균주에 대해 16S rRNA 유전자를 이용한 균주 동정을 실시한 결과, B. amyloliquefaciens 10종, B. methylotrophicus 1종, B. velezensis 1종, B. subtilis 3종이 분리 동정되었다. 그중 B. subtilis JBG17019, B. amyloliquefaciens JBD17076, B. amyloliquefaciens JBD17109 균주에서 식중독미생물에 대한 증식 억제능이 확인되었다. Glutamic acid 대사와 관련한 발효특성을 확인하기 위하여 선발된 Bacillus 균주에 대해 glutamate, glutamine 및 ${\gamma}$-PGA 생성능을 측정하였다. 발효특성과 ${\gamma}$-PGA 생성능에 대한 다변량 요인분석을 주성분(PCA) 추출법으로 분석한 결과, PC1(효소 활성(amylase, cellulase, xylanase), PC2(${\gamma}$-PGA 생성능) 및 PC3(protease, glutamate 및 glutamine)의 3가지 주성분이 분류되었다. 주성분(PC)의 추출에 따라 B. amyloliquefaciens JBD17076 및 B. subtilis JBG17019 균주는 우수한 효소 활성 및 ${\gamma}$-PGA 생성을 하는 것으로 평가되었다.

Tetrameric β를 이용한 고초균 포자에서의 미생물 표면 발현 모체 선별 (Screening of Bacterial Surface Display Anchoring Motif Using Tetrameric β-galactosidase in Bacillus subtilis Spore)

  • 김준형;반재구;김병기
    • KSBB Journal
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    • 제26권3호
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    • pp.199-205
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    • 2011
  • Using tetrameric ${\beta}$-galactosidase as a model protein, anchoring motives were screened in Bacillus subtilis spore display system. Eleven spore coat proteins were selected considering their expression levels and the location in the spore coat layer. After chromosomal single-copy homologous integration in the amyE site of Bacillus subtilis chromosome, cotE and cotG were chosen as possible spore surface anchoring motives with their higher whole cell ${\beta}$-galactosidase activity. PAGE and Wester blot of extracted fraction of outer layer of purified spore, which express CotE-LacZ or CotG-LacZ fusion verified the existence of exact size of fusion protein and its location in outer coat layer of purified spore. ${\beta}$-galactosidase activity of spore with CotE-LacZ or CotG-LacZ fusion reached its highest value around 16~20 h of culture time in terms of whole cell and purified spore. After intensive spore purification with lysozyme treatment and renografin treatment, spore of BJH135, which expresses CotE-LacZ, retained only 1~2% of its whole cell ${\beta}$-galactosidase activity. Whereas spore of BJH136, which has cotG-lacZ cassette in the chromosome, retained 10~15% of its whole cell ${\beta}$-galactosidase activity, proving minor perturbation of CotG-LacZ, when incorporated in the spore coat layer of Bacillus subtilis compared to CotE-LacZ. Usage of Bacillus subtilis WB700, of which 7 proteases are knocked-out and thereby resulting in 99.7% decrease in protease activity of the host, did not prevent the proteolytic degradation of spore surface expressed CotG-LacZ fusion protein.