Download Abstract format policy Abstract title: Times New Roman, 12 font

Abstract format policy
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Abstract title: Times New Roman, 12 font & Bold, centered, initial letter of each word should
be capitalized.
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Author name: Times New Roman, 11 font & Bold, centered (Please underline the name of
presenting author and mark the corresponding author with an asterisk *).
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Affiliation: Times New Roman, 11 font, centered.
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Abstract text: Times New Roman 11, single-spaced type.
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Keywords: Times New Roman 11, two or three keyword.
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References (optional): Times New Roman 11, less than three references. Call out references in
the text with number in bracket (e.g. [1]).
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Please note that abstracts should be submitted in English, in Word format.
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Abstract text should be up to 500 words (including title and reference).
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All text (title, reference, body of abstract, authors) and images should not exceed 1 page.
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All abstracts should be submitted online through the conference website.
[Abstract Example]
Overexpression and Biochemical Characterization of DagA from
Streptomyces coelicolor A3(2)
Uyangaa Temuujin1, Won-Jae Chi1, Yong-Keun Chang2 and Soon-Kwang Hong1*
(Please underline the name of presenting author)
1
Division of Bioscience and Bioinformatics, Myongji University, Yongin, Gyeonggi-do 449728, South Korea ([email protected])
2
Department of Chemical and Biomolecular Engineering, Korea Advanced Institute of Science
and Technology, 373-1, Kusong-dong, Yusung-gu, Taejon 305-701, South Korea
The DagA product of Streptomyces coelicolor is an agarase with a primary translation product
(35 kDa) of 309 amino acids, including a 30-amino acid signal peptide. Although dagA
expression in Streptomyces lividans under the control of its own set of promoters was previously
reported, its enzymatic properties have never been elucidated. To develop an improved
expression system for dagA, three types of strong promoters for the Streptomyces host were
linked to dagA, and their efficiencies in DagA production were compared in S. lividans TK24.
All of the transformants with dagA grew at improved rates and produced larger amounts of DagA
in the modified R2YE medium containing 0.5% agar as the sole carbon source. Of the three
transformants, the S. lividans TK24/pUWL201-DagA (ermE promoter) produced the highest
agarose activity (A540=4.24), and even the S. lividans TK24/ pHSEV1-DagA (tipA promoter) and
S. lividans TK24/ pWHM3-DagA (sprT promoter) produced higher agarose activity (A540=0.24
and 0.12, respectively) than the control (A540=0.01) in the modified R2YE medium. The mature
form of DagA protein (32 kDa) was successfully purified by one-step affinity column
chromatography by using agarose beads with excellent yield. The purified DagA was found to
exhibit maximal agarase activity at 40°C and pH 7.0. The K m, Vmax, and Kcat values for agarose
were 2.18 mg/ml (approximately 1.82×10−5 M), 39.06 U/mg of protein, and 9.5×103/s,
respectively. Thin layer chromatography (TLC) analysis, matrix-assisted laser
desorption/ionization-time-of-flight (MALDI-TOF) mass spectrometry, and Fourier transform
nuclear magnetic resonance (FT-NMR) spectrometry of the hydrolyzed products of agarose by
DagA revealed that DagA is an endo-type β-agarase that degrades agarose into neoagarotetraose
and neoagarohexaose.
Keywords: Streptomyces coelicolor . DagA . β-Agarase
References (optional)
[1] Bibb MJ, Jones GH, Joseph R, Buttner MJ, Ward JM (1987) The agarase gene (dagA) of
Streptomyces coelicolor A3(2): affinity purification and characterization of the cloned gene
product. J Gen Microbiol 133:2089–2096
[2] Buttner MJ, Fearnley JM, Bibb MJ (1987) The agarase gene (dagA) of Streptomyces
coelicolor A3(2): nucleotide sequence and transcriptional analysis. Mol Gen Genet 209:101–
109