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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제24권 제4호
- 발행연도
- 2014.1
- 수록면
- 545 - 555 (11page)
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초록· 키워드
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It has been previously demonstrated that laccases exhibit great potential for use in severalindustrial and environmental applications. In this paper, two laccase isoenzyme genes, lccBand lccC, were cloned and expressed in Pichia pastoris GS115. The sequence analysis indicatedthat the lccB and lccC genes consisted of 1,563 and 1,584 bp, and their open reading framesencoded 520 and 527 amino acids, respectively. They had 72.7% degree of identity innucleotides and 86.7% in amino acids. The expression levels of LccB and LccC were up to32,479 and 34,231 U/l, respectively. The recombinant laccases were purified by ultrafiltrationand (NH4)2SO4 precipitation, showing a single band on SDS-PAGE, which had a molecularmass of 58 kDa. The optimal pH and temperature for LccB were 2.0 and 55oC with 2,2'-azinobis-[3-ethylbenzthiazolinesulfonic acid (ABTS) as a substrate, whereas LccC exhibited optimalpH and temperature at 3.0 and 60oC. The apparent kinetic parameters of LccB were 0.43 mMfor ABTS with a Vmax value of 51.28 U/mg, and the Km and Vmax values for LccC were 0.29 mMand 62.89 U/mg. The recombinant laccases were able to decolorize five types of dyes. AcidViolet 43 (100 g/ml) was completely decolorized by LccB or LccC (2 U/ml), and thedecolorization of Reactive Blue KN-R (100 g/ml) was 91.6% by LccC (2 U/ml). Thus, the studycharacterizes useful laccase isoenzymes from T. versicolor that have the capability of beingincorporated into the treatment of similar azo and anthraquinone dyes from dyeing industries.
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참고문헌 (23)
참고문헌 신청
Baldrian P. / 2006 / Fungal laccases - occurrence and properties / FEMS Microbiol. Rev 30 : 215 ~ 242
Bourbonnais R / 1995 / Lignin oxidation by laccase isozymes from Trametes versicolor and role of the mediator 2,2’-azinobis(3-ethylbenzthiazoline-6-sulfonate) in kraft ligni
Bradford M. / 1976 / A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding / Anal. Biochem 72 :
Cabana H / 2009 / Immobilization of laccase from the white rot fungus Coriolopsis polyzona and use of the immobilized biocatalyst for the continuous elimination of endocrine
Camarero S / 2005 / Lignin-derived compounds as efficient laccase mediators for decolorization of different types of recalcitrant dyes / Appl. Environ. Microbiol 71 : 1775 ~
Bourbonnais R / 1995 / Lignin oxidation by laccase isozymes from Trametes versicolor and role of the mediator 2,2’-azinobis(3-ethylbenzthiazoline-6-sulfonate) in kraft ligni
Bradford M. / 1976 / A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding / Anal. Biochem 72 :
Cabana H / 2009 / Immobilization of laccase from the white rot fungus Coriolopsis polyzona and use of the immobilized biocatalyst for the continuous elimination of endocrine
Camarero S / 2005 / Lignin-derived compounds as efficient laccase mediators for decolorization of different types of recalcitrant dyes / Appl. Environ. Microbiol 71 : 1775 ~
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