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Updated: Jan 23, 2026

Chromatographic Purification of Highly Active Yeast Ribosomes
Published on: October 24, 2011
Comparison of downstream processing methods in purification of highly active laccase
Anna Antecka1, Michał Blatkiewicz2, Tomasz Boruta2
1Faculty of Process and Environmental Engineering, Lodz University of Technology, ul. Wolczanska 213, 90-924, Lodz, Poland. anna.antecka@p.lodz.pl.
Researchers optimized fungal laccase production and purification using integrated bioreactor systems. Aqueous two-phase extraction (ATPE) proved highly effective for concentrating laccase, achieving high specific activity and isoform separation.
Area of Science:
- Enzyme Technology
- Biochemical Engineering
- Mycology
Background:
- Laccases are enzymes known for degrading phenolic and lignin compounds.
- Research interest in laccases has grown due to their potential applications.
- Efficient production and purification methods are crucial for laccase utilization.
Purpose of the Study:
- To maximize laccase activity from Cerrena unicolor.
- To evaluate and compare ultrafiltration, ATPE, and foam fractionation for laccase purification.
- To develop an integrated system for fungal laccase production and purification.
Main Methods:
- Repeated fed-batch cultivation of Cerrena unicolor in a bioreactor with integrated filtration.
- Purification using ultrafiltration, aqueous two-phase extraction (ATPE), and foam fractionation (FF).
- Assessment of recovery yield and purification fold for each method.
Main Results:
- Achieved high laccase specific activity (204.1 U/mg) in the fermentation broth.
- ATPE demonstrated a high recovery yield (97.4%) compared to ultrafiltration (73.7%) and FF (24.9%).
- A two-step purification yielded two laccase isoforms with high specific activities (2349 and 3374 U/mg).
Conclusions:
- An integrated system for fungal laccase production, concentration, and separation was proposed.
- ATPE is an effective method for fungal laccase concentration and purification.
- Optimized downstream processing significantly enhances laccase specific activity and enables isoform separation.
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