Production of fungal laccase and its immobilization and stability

Nam Seok Cho, Hee Yeon Cho, Soo Jeong Shin, Yun Jeong Choi, Andrzej Leonowicz, Shoji Ohga

研究成果: ジャーナルへの寄稿記事

18 引用 (Scopus)

抄録

The extracellular laccase of white-rot fungus, Cerrena unicolor, was purified from culture by Sephadex G-25 and ion-exchange chromatography on DEAE-Toyopearl column and immobilized on various supports. Purified laccase showed two times higher activity after desalting process and 3.7 to 13.4 times activity after DEAE chromatography. During immobilizing process, 93.8% protein and 100% of laccase activity were coupled to the supports. Following immobilization, the optimal pH (5.5) for immobilized laccase was slightly shifted wide pH values (from 5.0 to 6.0) in the case of some supports, and decreased more gradually in alkaline region. Both free and immobilized laccases showed the highest activity at 60°C, however, the immobilized enzyme was more resistant to the wide range of temperature (50-80°C). Even at the 9 °C, treated glass beads and Supp-1 maintained almost 80% activity. After 10 days of storage at 4°C, the immobilized laccases retained 95-100% of its initial activity. It was also more stable during storage at 4°C. While, after the same storage time only 34% the initial activity was retained by the free enzyme. Immobilized laccase on glass supports was retained 85-90% activity over 20 days storage, while free enzyme almost zero activity. The immobilized laccases which are more stable and temperature resistant than free enzyme, seem to be more useful.

元の言語英語
ページ(範囲)13-18
ページ数6
ジャーナルJournal of the Faculty of Agriculture, Kyushu University
53
発行部数1
出版物ステータス出版済み - 2 2008

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Laccase
laccase
Immobilization
Glass
glass
Enzymes
enzymes
Immobilized Enzymes
immobilized enzymes
white-rot fungi
Temperature
Ion Exchange Chromatography
ion exchange chromatography
Chromatography
storage time
chromatography
temperature
Fungi

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Agronomy and Crop Science

これを引用

Cho, N. S., Cho, H. Y., Shin, S. J., Choi, Y. J., Leonowicz, A., & Ohga, S. (2008). Production of fungal laccase and its immobilization and stability. Journal of the Faculty of Agriculture, Kyushu University, 53(1), 13-18.

Production of fungal laccase and its immobilization and stability. / Cho, Nam Seok; Cho, Hee Yeon; Shin, Soo Jeong; Choi, Yun Jeong; Leonowicz, Andrzej; Ohga, Shoji.

:: Journal of the Faculty of Agriculture, Kyushu University, 巻 53, 番号 1, 02.2008, p. 13-18.

研究成果: ジャーナルへの寄稿記事

Cho, NS, Cho, HY, Shin, SJ, Choi, YJ, Leonowicz, A & Ohga, S 2008, 'Production of fungal laccase and its immobilization and stability', Journal of the Faculty of Agriculture, Kyushu University, 巻. 53, 番号 1, pp. 13-18.
Cho, Nam Seok ; Cho, Hee Yeon ; Shin, Soo Jeong ; Choi, Yun Jeong ; Leonowicz, Andrzej ; Ohga, Shoji. / Production of fungal laccase and its immobilization and stability. :: Journal of the Faculty of Agriculture, Kyushu University. 2008 ; 巻 53, 番号 1. pp. 13-18.
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abstract = "The extracellular laccase of white-rot fungus, Cerrena unicolor, was purified from culture by Sephadex G-25 and ion-exchange chromatography on DEAE-Toyopearl column and immobilized on various supports. Purified laccase showed two times higher activity after desalting process and 3.7 to 13.4 times activity after DEAE chromatography. During immobilizing process, 93.8{\%} protein and 100{\%} of laccase activity were coupled to the supports. Following immobilization, the optimal pH (5.5) for immobilized laccase was slightly shifted wide pH values (from 5.0 to 6.0) in the case of some supports, and decreased more gradually in alkaline region. Both free and immobilized laccases showed the highest activity at 60°C, however, the immobilized enzyme was more resistant to the wide range of temperature (50-80°C). Even at the 9 °C, treated glass beads and Supp-1 maintained almost 80{\%} activity. After 10 days of storage at 4°C, the immobilized laccases retained 95-100{\%} of its initial activity. It was also more stable during storage at 4°C. While, after the same storage time only 34{\%} the initial activity was retained by the free enzyme. Immobilized laccase on glass supports was retained 85-90{\%} activity over 20 days storage, while free enzyme almost zero activity. The immobilized laccases which are more stable and temperature resistant than free enzyme, seem to be more useful.",
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