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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제25권 제9호
- 발행연도
- 2015.1
- 수록면
- 1,433 - 1,441 (9page)
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초록· 키워드
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Pollution resulting from the discharge of textile dyes into water systems has become a major global concern. Because peroxidases are known for their ability to decolorize and detoxify textile dyes, the peroxidase activity of Vitreoscilla hemoglobin (VHb) has recently been studied. It is found that VHb and variants of this enzyme show great promise for enzymatic decolorization of dyes and may play a role in achieving their successful removal from industrial wastewater. The level of VHb peroxidase activity correlates with two amino acid residues present within the conserved distal pocket, at positions 53 and 54. In this work, sitedirected mutagenesis of these residues was performed and resulted in improved VHb peroxidase activity. The double mutant, Q53H/P54C, shows the highest dye decolorization and removal efficiency, with 70% removal efficiency within 5 min. UV spectral studies of Q53H/P54C reveals a more compact structure and an altered porphyrin environment (λSoret = 413 nm) relative to that of wild-type VHb (λSoret = 406), and differential scanning calorimetry data indicate that the VHb variant protein structure is more stable. In addition, circular dichroism spectroscopic studies indicate that this variant’s increased protein structural stability is due to an increase in helical structure, as deduced from the melting temperature, which is higher than 90°C. Therefore, the VHb variant Q53H/P54C shows promise as an excellent peroxidase, with excellent dye decolorization activity and a more stable structure than wild-type VHb under high-temperature conditions.
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참고문헌 (22)
참고문헌 신청
Andersson CI / 2003 / Enhanced ribosome and tRNA contents in Escherichia coli expressing a truncated Vitreoscilla hemoglobin mutant analyzed by flow field-flow fractionation
Bhunia A / 2001 / Horseradish peroxidase catalyzed degradation of industrially important dyes / Biotechnol. Bioeng 72 : 562 ~ 567
Bolognesi M / 1999 / Anticooperative ligand binding properties of recombinant ferric Vitreoscilla homodimeric hemoglobin: a thermodynamic, kinetic and Xray crystallographic s
Cenens J / 1988 / Visible spectroscopy of methylene blue on hectorite, laponite B, and barasym in aqueous suspension / Clays Clay Miner 36 : 214 ~ 224
Chivukula M / 1995 / Lignin peroxidase-catalyzed oxidation of sulfonated azo dyes generates novel sulfophenyl hydroperoxides / Biochemistry 34 : 7765 ~ 7772
Bhunia A / 2001 / Horseradish peroxidase catalyzed degradation of industrially important dyes / Biotechnol. Bioeng 72 : 562 ~ 567
Bolognesi M / 1999 / Anticooperative ligand binding properties of recombinant ferric Vitreoscilla homodimeric hemoglobin: a thermodynamic, kinetic and Xray crystallographic s
Cenens J / 1988 / Visible spectroscopy of methylene blue on hectorite, laponite B, and barasym in aqueous suspension / Clays Clay Miner 36 : 214 ~ 224
Chivukula M / 1995 / Lignin peroxidase-catalyzed oxidation of sulfonated azo dyes generates novel sulfophenyl hydroperoxides / Biochemistry 34 : 7765 ~ 7772
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