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Purification and Characterization of Laccase Enzyme from Locally Isolated Aspergillus flavus Strain

Purification and Characterization of Laccase Enzyme from Locally Isolated Aspergillus flavus Strain

Syeda Rubab Zaidi* and Safdar Ali Mirza

Government College University, Lahore, Punjab 54000, Pakistan

 
Corresponding Author: Syeda Zaidi
rubabzaidi2009@yahoo.com

ABSTRACT

Laccases belong to family oxidoreductase are widely present in nature and possess broad range of substrates. Vast application of these enzymes demands their production in a large quantity. In this study production and optimization of laccase enzyme production from locally isolated and screened potential fungal strain of Aspergillus flavus was monitored. During this study culture medium and different parameters such as incubation period and inoculum size were optimized and inducers were employed for enhanced production of laccase. Partial purification was accomplished through Ammonium-Sulphate precipitation and for further purification gel filtration and anion exchange methods were used along with protein estimation. The purified fraction was then subjected to enzymatic characterization to find its thermal stability, effect of pH and selected chemical compounds. Other significant experimental findings were; optimum incubation period was 7 days, inoculum size was 3 discs of 0.5 cm, CuSO4 as inducer improved production, laccase activity of crude extract i.e. 10.89U/ml increased to 15.07U/ml with purification of the enzyme, the purified samples of enzyme was significantly greater protein concentration than crude sample so, the optimum pH was 5.0 for laccase activity and the enzymatic extract was thermostable up to 60oC for 1 hour with guaiacol as substrate. The biological production of enzyme have an ecofriendly impact in current scenario. 
 
Novelty Statement | The study is novel in suggesting ecofriendly impact of production of laccase enzyme from locally isolated Aspergillus flavus strain.
 

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Pakistan Journal of Zoology

October

Vol. 54, Iss. 5, Pages 2003-2500

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