• 제목/요약/키워드: Bacillus pumilus H10-1

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Bacillus pumilus IJ-1의 생물계면활성제 생산을 위한 배양 특성 (Characteristics of Culture Conditions for the Production of Biosurfactant by Bacillus pumilus IJ-1)

  • 박은진;김지연
    • Journal of Applied Biological Chemistry
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    • 제58권1호
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    • pp.81-88
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    • 2015
  • Bacillus pumilus IJ-1의 생물계면활성제 생산을 위한 배지 조성의 특성을 조사하기 위하여 다양한 탄소원, 질소원 및 무기염이 미치는 영향을 검토하였다. 그 결과 B. pumilus IJ-1은 0.5%(w/v) tryptone을 첨가하여 배양하였을 때 가장 많은 생물계면활성제를 생산하였다. B. pumilus IJ-1은 0-10% (w/v)의 NaCl 농도와 pH 5-10, $20-45^{\circ}C$의 환경에서 생장이 가능하였다. 그리고 생물계면활성제 생산은 pH 9.0의 초기 배지에서 $20^{\circ}C$, 72시간 동안 배양했을 때 최대였으며, 이러한 배양 조건 하에서 얻어진 배양액의 표면장력은 27.0 dyne/cm이었다.

흰 코뿔소 배설물로부터 분리한 Bacillus pumilus H10-1의 Xylanase 활성 (Xylanase Activity of Bacillus pumilus H10-1 Isolated from Ceratotherium simum Feces)

  • 윤영미;안기홍;김중곤;안승현;차영록;양정우;유경단;문윤호;안종웅;구본철;최인후
    • KSBB Journal
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    • 제29권5호
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    • pp.316-322
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    • 2014
  • Xylanase have been used to convert the polymetric xylan into fermentable sugars from the production of ethanol and xylitol from plant biomass. The aim of this study was to isolate and identify xylanolytic bacterium from herbivore feces and was to used the xylanase for enzymatic hydrolysis of biomass. Xylanolytic strains were isolated from 59 different feces of herbivores from Seoul Grand Park located in Gwacheon Gyeonggi-do. The xylanolytic strains were selected by congo red staining and DNS method. Total 67 strains isolated from the herbivores feces were tested for xylanase activity. Among the strains, H10-1, which has the highest xylanase activity, was isolated from feces of Ceratotherium simum. The H10-1 strain was identified as Bacillus pumilus based on its morphological/biochemical characteristics and partial 16S rDNA gene sequences. Culture conditions of B. pumilus H10-1 such as initial medium pH, incubation temperature and incubation time were optimized for maximum xylanase production. And also xylanase produced by B. pumilus H10-1 was applied for the saccharification of Miscanthus sacchariflorus cv. 'Geodae 1', which was pretreated with 1.5M NaOH. The optimized culture conditions of B. pumilus H10-1 were pH 9, $30^{\circ}C$ incubation temperature, and 7 day incubation time, respectively. This xylanase activity under the optimized conditions was $20.4{\pm}3.3IU$. The crude xylanase produced by B. pumilus H10-1 was used for the saccharification of xylan derived from pretreated 'Geodae 1'. The saccharification conditions were $50^{\circ}C$, 200 rpm, and 5 days. Saccharification efficiency of pretreated 'Geodae 1' by B. pumilus H10-1 was 8.2%.

Isolation and Biochemical Characterization of Bacillus pumilus Lipases from the Antarctic

  • Arifin, Arild Ranlym;Kim, Soon-Ja;Yim, Joung Han;Suwanto, Antonius;Kim, Hyung Kwoun
    • Journal of Microbiology and Biotechnology
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    • 제23권5호
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    • pp.661-667
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    • 2013
  • Lipase-producing bacterial strains were isolated from Antarctic soil samples using the tricaprylin agar plate method. Seven strains with relatively strong lipase activities were selected. All of them turned out to be Bacillus pumilus strains by the 16S rRNA gene sequence analysis. Their corresponding lipase genes were cloned, sequenced, and compared. Finally, three different Bacillus pumilus lipases (BPL1, BPL2, and BPL3) were chosen. Their amino acid sequence identities were in the range of 92-98% with the previous Bacillus pumilus lipases. Their optimum temperatures and pHs were measured to be $40^{\circ}C$ and pH 9. Lipase BPL1 and lipase BPL2 were stable up to $30^{\circ}C$, whereas lipase BPL3 was stable up to $20^{\circ}C$. Lipase BPL2 was stable within a pH range of 6-10, whereas lipase BPL1 and lipase BPL3 were stable within a pH range of 5-11, showing strong alkaline tolerance. All these lipases exhibited high hydrolytic activity toward p-nitrophenyl caprylate ($C_8$). In addition, lipase BPL1 showed high hydrolytic activity toward tributyrin, whereas lipase BPL2 and lipase BPL3 hydrolyzed tricaprylin and castor oil preferentially. These results demonstrated that the three Antarctic Bacillus lipases were alkaliphilic and had a substrate preference toward short- and medium-chain triglycerides. These Antarctic Bacillus lipases might be used in detergent and food industries.

Assessment and Optimization of Xylanase Production Using Mono-Culture and Co-Cultures of Bacillus subtilis and Bacillus pumilus

  • Chitranshu Pandey;Neeraj Gupta
    • 한국미생물·생명공학회지
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    • 제51권1호
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    • pp.59-68
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    • 2023
  • Xylanase is an industrially relevant enzyme used for the production of xylobiose and xylose. Various methods are used to enhance the microbial yield of xylanase. In the present study, co-culturing of Bacillus subtilis and Bacillus pumilus were investigated using submerged fermentation for xylanase production, which was markedly increased when sal, sagwan, newspaper, wheat bran, and xylan were used as single carbon sources. Maximum xylanase production was reported after 5 days of incubation in optimized media at pH 7.0 and 37℃, resulting in 2.69 ± 0.25 µmol/min by coculture. The 1:1 ratio of sal and sagwan in optimized production media was shown to be suitable for xylanase synthesis in submerged fermentation (SMF). In comparison to mono-culture using B. pumilus and B. subtilis, co-culturing resulted in an overall 3.8-fold and 2.15-fold increase in xylanase production, respectively.

Xylanase를 생산하는 내열성 Bacillus속 균주의 분리와 효소생산 조건 (isolation of Xylanase-producing Thermo-tolerant Bacillus sp. and Its Enzyme Production)

  • 박영서;강미영;장학길;박귀근;강종백;이정기;오태광
    • 한국미생물·생명공학회지
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    • 제27권5호
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    • pp.370-377
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    • 1999
  • Thermo-tolerant bacterium producing the xylanase was isolated from soil and identified as Bacillus pumilus. This strain, named Bacillus pumilus TX703, was able to grow ad produce xylanase at the culture temperature of 5$0^{\circ}C$. The maximum xylanase production was obtained when 1%(w/v) birchwood xylan and 1% (w/v) soytone were used as carbon source and nitrogen source, respectively. The biosynthesis of xylanase was under the catabolite repression induced by glucose in the culture medium, and it was completely inhibited in the presence of 0.2% (w/v) glucose. The maximum activity of xylanase was observed from pH8.0 to 9.0 and from 50 to 6$0^{\circ}C$ and the enzyme was highly heat-stable, whose activity remained was over 50% at 8$0^{\circ}C$, and was quite stable from pH5.0 to 10.0.

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대두 열수 침출액을 이용한 청국장 발효균주 Bacillus pumilus JB-1의 배양 최적화 (Optimization of Culture Conditions of Bacillus pumilus JB-1 for Chungkook-jang Fermentation in Soybean Boiling-Waste Liquor Medium)

  • 권하영;류희영;권정숙;이상한;손호용
    • 한국미생물·생명공학회지
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    • 제35권4호
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    • pp.304-309
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    • 2007
  • 생 대두는 설사, 체중감소 등의 농도 의존적 독성을 나타내므로, 가열처리 및 발효과정이 필요하며, 이 과정 중에 대두 열수 침출액이 부산물로 발생한다. 본 연구에서는, 현재 대부분이 폐기되고 있는 대두 열수 침출액을 저 이취, 면역증강 활성이 강력한 청국장 발효균주 Bacillus pumilus JB-1의 대량생산을 위한 배지로 사용하고자, 대두 열수 침출액의 성분을 검토하고 이에 따른 최적 배양조건을 검토하였다. 대두 열수 침출액은 88% 수분함량, 9.5%총당, 1.6% 조단백, 0.3% 조지질, 0.1% 조섬유와 2.1%의 회분을 포함하였으며, total polyphenol, total flavonoids 및 유리아미노산 함량은 각각 생 대두의 55%, 76%,및 30%수준을 나타내어 영양적으로 매우 우수함을 확인하였다. 검토된 B. pumilus JB-1 균주 최적배양조건은 1/10 희석한 침출액에 pH 무조정, 무가당, $(NH_4)_2SO_4$ 0.1% 첨가한 후, 균주를 0.5% 접종하여 $37^{\circ}C$, 120 rpm 교반조건에서 48시간 배양이었다. 최종적으로 5리터 Jar fermentor를 이용한 대량발효에서 효율적인 청국장 스타터 균주생산 및 대두 열수 침출액의 기능성소재 이용 가능성을 확인하였다.

Purification and Characterization of a Fibrinolytic Enzyme from Bacillus pumilus 2.g Isolated from Gembus, an Indonesian Fermented Food

  • Afifah, Diana Nur;Sulchan, Muhammad;Syah, Dahrul;Yanti, Yanti;Suhartono, Maggy Thenawidjaja;Kim, Jeong Hwan
    • Preventive Nutrition and Food Science
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    • 제19권3호
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    • pp.213-219
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    • 2014
  • Bacillus pumilus 2.g isolated from gembus, an Indonesian fermented soybean cake, secretes several proteases that have strong fibrinolytic activities. A fibrinolytic enzyme with an apparent molecular weight of 20 kDa was purified from the culture supernatant of B. pumilus 2.g by sequential application of ammonium sulfate precipitation, ion-exchange chromatography, and hydrophobic chromatography. The partially purified enzyme was stable between pH 5 and pH 9 and temperature of less than $60^{\circ}C$. Fibrinolytic activity was increased by 5 mM $MgCl_2$ and 5 mM $CaCl_2$ but inhibited by 1 mM phenylmethylsulfonyl fluoride (PMSF), 1 mM sodium dodecyl sulfate (SDS), and 1 mM ethylenediaminetetraacetic acid (EDTA). The partially purified enzyme quickly degraded the ${\alpha}$ and ${\beta}$ chains of fibrinogen but was unable to degrade the ${\gamma}$ chain.

Expression and Biochemical Characterization of Cold-Adapted Lipases from Antarctic Bacillus pumilus Strains

  • Litantra, Ribka;Lobionda, Stefani;Yim, Joung Han;Kim, Hyung Kwoun
    • Journal of Microbiology and Biotechnology
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    • 제23권9호
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    • pp.1221-1228
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    • 2013
  • Two lipase genes (bpl1 and bpl3) from Antarctic Bacillus pumilus strains were expressed in Bacillus subtilis. Both recombinant lipases BPL1 and BPL2 were secreted to the culture medium and their activities reached 3.5 U/ml and 5.0 U/ml, respectively. Their molecular masses apparent using SDS-PAGE were 23 kDa for BPL1 and 19 kDa for BPL3. Both lipases were purified to homogeneity using ammonium sulfate precipitation and HiTrap SP FF column and Superose 12 column chromatographies. The final specific activities were estimated to be 328 U/mg for BPL1 and 310 U/mg for BPL3. Both lipases displayed an optimum temperature of $35^{\circ}C$, similar to other mesophilic enzymes. However, they maintained as much as 70% and 80% of the maximum activities at $10^{\circ}C$. Accordingly, their calculated activation energy at a temperature range of $10-35^{\circ}C$ was 5.32 kcal/mol for BPL1 and 4.26 kcal/mol for BPL3, typical of cold-adapted enzymes. The optimum pH of BPL1 and BPL3 was 8.5 and 8.0, respectively, and they were quite stable at pH 7.0-11.0, showing their strong alkaline tolerance. Both lipases had a preference toward medium chain length ($C_6-C_{10}$) fatty acid substrates. These results indicate the potential for the two Antarctic B. pumilus lipases as catalysts in bioorganic synthesis, food, and detergent industries.

Intergeneric protoplast fusion between Bacillus pumilus and Cellulomonas fimi

  • Kim, D.M.;Lee, K.H.
    • 한국미생물생명공학회:학술대회논문집
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    • 한국미생물생명공학회 1986년도 추계학술대회
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    • pp.528.1-528
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    • 1986
  • Cellulose utilising hybrids between Cellulomonas fimi and Bacillus pumilus were isolated after PEG mediated protoplast fusion. 33% (w/v) PEG #6, 000 and 50mM $Ca^{++}$were optimum concentration. The intergeneric fusion frequency was 3.2$\times$10$^{-7}$ xtracellular CMCase and $\beta$-glucosidase activities were detected from one hydrid unlike only CMCase was detected from Cellulomonas fimi.

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Purification and Characterization of Manganese-Dependent Alkaline Serine Protease from Bacillus pumilus TMS55

  • Ibrahim, Kalibulla Syed;Muniyandi, Jeyaraj;Pandian, Shunmugiah Karutha
    • Journal of Microbiology and Biotechnology
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    • 제21권1호
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    • pp.20-27
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    • 2011
  • The purification and characterization of a $Mn^{2+}$-dependent alkaline serine protease produced by Bacillus pumilus TMS55 were investigated. The enzyme was purified in three steps: concentrating the crude enzyme using ammonium sulfate precipitation, followed by gel filtration and cation-exchange chromatography. The purified protease had a molecular mass of approximately 35 kDa, was highly active over a broad pH range of 7.0 to 12.0, and remained stable over a pH range of 7.5 to 11.5. The optimum temperature for the enzyme activity was found to be $60^{\circ}C$. PMSF and AEBSF (1 mM) significantly inhibited the protease activity, indicating that the protease is a serine protease. $Mn^{2+}$ ions enhanced the activity and stability of the enzyme. In addition, the purified protease remained stable with oxidants ($H_2O_2$, 2%) and organic solvents (25%), such as benzene, hexane, and toluene. Therefore, these characteristics of the protease and its dehairing ability indicate its potential for a wide range of commercial applications.