Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 273-277 |
| Seitenumfang | 5 |
| Fachzeitschrift | Enzyme and microbial technology |
| Jahrgang | 40 |
| Ausgabenummer | 2 |
| Publikationsstatus | Veröffentlicht - 28 Apr. 2006 |
Abstract
A laccase (E.C. 1.10.3.2) from Trametes spec. was isolated from aqueous media using foam fractionation. The pH value, superficial velocity, foaming period, and temperature were varied to optimise the transport of the active enzyme into the foam phase. Several detergents were added in varying concentrations to form and stabilize the foam, and the cationic detergent cetyltrimethylammonium bromide (CTAB) proved to be the most appropriate. From water as a model system, maximum recovery rates of 94% of laccase activity were achieved at pH 6.0 in 6 min. For separation of the enzyme from protein rich culture media, the operation conditions had to be adjusted. At pH 5.4, 89% of laccase activity was transported into the foam phase after 15 min. The method established was successfully applied to the isolation of an active laccase isoenzyme from submerged cultures of the basidiomycete Pleurotus sapidus.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biotechnologie
- Chemische Verfahrenstechnik (insg.)
- Bioengineering
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biochemie
- Immunologie und Mikrobiologie (insg.)
- Angewandte Mikrobiologie und Biotechnologie
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in: Enzyme and microbial technology, Jahrgang 40, Nr. 2, 28.04.2006, S. 273-277.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Laccase isolation by foam fractionation
T2 - New prospects of an old process
AU - Linke, Diana
AU - Zorn, Holger
AU - Gerken, Birte
AU - Parlar, Harun
AU - Berger, Ralf G.
N1 - Funding information: Financial support by the AIF (project # 121 ZN) through the Forschungskreis der Ernährungsindustrie e.V., Bonn, is gratefully acknowledged. The project is part of the joint initiative “Biologisch aktive Naturstoffe, Chemische Diversität” at the University of Hannover.
PY - 2006/4/28
Y1 - 2006/4/28
N2 - A laccase (E.C. 1.10.3.2) from Trametes spec. was isolated from aqueous media using foam fractionation. The pH value, superficial velocity, foaming period, and temperature were varied to optimise the transport of the active enzyme into the foam phase. Several detergents were added in varying concentrations to form and stabilize the foam, and the cationic detergent cetyltrimethylammonium bromide (CTAB) proved to be the most appropriate. From water as a model system, maximum recovery rates of 94% of laccase activity were achieved at pH 6.0 in 6 min. For separation of the enzyme from protein rich culture media, the operation conditions had to be adjusted. At pH 5.4, 89% of laccase activity was transported into the foam phase after 15 min. The method established was successfully applied to the isolation of an active laccase isoenzyme from submerged cultures of the basidiomycete Pleurotus sapidus.
AB - A laccase (E.C. 1.10.3.2) from Trametes spec. was isolated from aqueous media using foam fractionation. The pH value, superficial velocity, foaming period, and temperature were varied to optimise the transport of the active enzyme into the foam phase. Several detergents were added in varying concentrations to form and stabilize the foam, and the cationic detergent cetyltrimethylammonium bromide (CTAB) proved to be the most appropriate. From water as a model system, maximum recovery rates of 94% of laccase activity were achieved at pH 6.0 in 6 min. For separation of the enzyme from protein rich culture media, the operation conditions had to be adjusted. At pH 5.4, 89% of laccase activity was transported into the foam phase after 15 min. The method established was successfully applied to the isolation of an active laccase isoenzyme from submerged cultures of the basidiomycete Pleurotus sapidus.
KW - Basidiomycete
KW - Downstream process
KW - Foam fractionation
KW - Laccase
UR - http://www.scopus.com/inward/record.url?scp=33751176846&partnerID=8YFLogxK
U2 - 10.1016/j.enzmictec.2006.04.010
DO - 10.1016/j.enzmictec.2006.04.010
M3 - Article
AN - SCOPUS:33751176846
VL - 40
SP - 273
EP - 277
JO - Enzyme and microbial technology
JF - Enzyme and microbial technology
SN - 0141-0229
IS - 2
ER -