• 제목/요약/키워드: Microbial Biotechnology

검색결과 2,188건 처리시간 0.39초

Lipase-catalyzed production of biodiesel

  • Sohn, Jung-Hoon;Kim, So-Young;Lee, Eung-Suek;Choi, Eui-Sung
    • 한국생물공학회:학술대회논문집
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    • 한국생물공학회 2003년도 생물공학의 동향(XIII)
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    • pp.127-128
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    • 2003

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방선균 분리주가 생산하는 Phospholipase C 저해물질인 MT-2617-2B의 분리 및 특성 (Isolation and Characterization of MT2617-2B, a Phospholipase C Inhibitor Produced by an Actinomycetes Isolate)

  • 고학룡;이현선;오원근;안순철;김보연;강대욱;민태익;안종석
    • 한국미생물·생명공학회지
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    • 제24권1호
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    • pp.19-26
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    • 1996

  • A phospholipase C (PLC) inhibitor (MT267-2B) was isolated from the culture broth of actinomycetes isolate MT2617-2 by the extraction with n-butanol and column chromatographic techniques. The molecular weight of the inhibitor was 1057, by the spectroscopic analyses of IR, $^{13}C$-and $^{1}H$-NMR and ESI-MS. The chemical structure of MT2617-2B was found to be a macrolide compound consisted of a hemiketal ring, polyhydroxyl and polymethyl groups, which had a malonate and guanidine group as its side chain. MT2617-2B produced its two isomers having the same molecular weight by standing in methanol solution at room temperature. Therefore, MT2617-2B was identified as copiamycin and niphithricin A, macrolide antibiotics. The values of $IC_{50}$ against PLC-${\gamma}$1 and PLC-${\beta}$1 were 25 and 50${\mu}$g/ml, respectively. MT2617-2B had antimicrobial activities against Staphylococcus aureus and Candida albicans, but not against Escherichia coli.

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Two pHZ1358 Derivative Vectors for Efficient Gene Knockout in Streptomyces

  • He, Yunlong;Wang, Zhijun;Bai, Linquan;Liang, Jingdan;Zhou, Xiufen;Deng, Zixin
    • Journal of Microbiology and Biotechnology
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    • 제20권4호
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    • pp.678-682
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    • 2010

  • The deletion of sti from the Streptomyces plasmid pIJ101 made its derivative pHZ1358 an efficient vector for gene disruption and replacement. Here, pHZ1358 was further optimized by the construction of a derivative plasmid pJTU1278, in which a cassette carrying multiple cloning sites and a lacZ selection marker were introduced for convenient plasmid construction in E. coli. In addition, the oriT region of pJTU1278 was also deleted, generating a vector (pJTU1289) that can be used specifically for PCR-targeting. The efficient usage of these vectors was demonstrated by the deletion of the gene involved in avermectin biosynthesis in S. avermitilis.

  • https://doi.org/10.4014/jmb.0910.10031 인용 PDF KSCI

Discovery of D-Stereospecific Dipeptidase from Thermophilic Bacillus sp. BCS-l and Its Application for Synthesis of D-Amino Acid-Containing Peptide

  • Baek, Dae-Heoun;Kwon, Seok-Joon;Park, Jin-Seo;Lee, Seung-Goo;Mheen, Tae-Ick;Sung, Moon-Hee
    • Journal of Microbiology and Biotechnology
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    • 제9권5호
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    • pp.646-649
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    • 1999

  • A thermophilic bacterium producing D-stereospecific dipeptidase was isolated from Korean soil samples. The enzyme hydrolyzed the peptide bond between D-alanyl-D-alanine (D-Ala-D-Ala). The isolated bacterial strain was rod shaped, gram-positive, motile, and formed an endospore. Morphological and physiological characteristics suggested this microorganism a thermophilic Bacillus species, and was named as Bacillus sp. BCS-l. The production of D-stereospecific dipeptidase was growth-associated and optimal at $55^{\circ}C$. The enzyme was applied for the synthesis of D-amino acid-containing peptide, N-benzyloxycarbonyl-L-aspartyl-D-alanine benzyl ester (Z-L-Asp-D-AlaOBzl), as a model reaction. A thermodynamically controlled synthesis of Z-L-Asp-D-AlaOBzl was achieved in an organic solvent.

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