Extraction and Application of Laccases from Shimeji Mushrooms (Pleurotus ostreatus) Residues in Decolourisation of Reactive Dyes and a Comparative Study Using Commercial Laccase from Aspergillus oryzae
نویسندگان
چکیده
Oxidases are able to degrade organic pollutants; however, high costs associated with biocatalysts production still hinder their use in environmental biocatalysis. Our study compared the action of a commercial laccase from Aspergillus oryzae and a rich extract from Pleurotus ostreatus cultivation residues in decolourisation of reactive dyes: Drimaren Blue X-3LR (DMBLR), Drimaren Blue X-BLN (DMBBLN), Drimaren Rubinol X-3LR (DMR), and Drimaren Blue C-R (RBBR). The colour removal was evaluated by considering dye concentration, reaction time, absence or presence of the mediator ABTS (2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), and the source of laccase. The presence of ABTS was essential for decolourisation of DMR (80-90%, 1 h) and RBBR (80-90%, 24 h) with both laccases. The use of ABTS was not necessary in reactions containing DMBLR (85-97%, 1 h) and DMBBLN (63-84%, 24 h). The decolourisation of DMBBLN by commercial laccase showed levels near 60% while the crude extract presented 80% in 24 h.
منابع مشابه
Efficient Recovery of Lignocellulolytic Enzymes of Spent Mushroom Compost from Oyster Mushrooms, Pleurotus spp., and Potential Use in Dye Decolorization
This study was conducted in order to perform efficient extraction of lignocellulolytic enzymes amylase (EC 3.2.1.1), cellulase (EC 3.2.1.4), laccase (EC 1.10.3.2), and xylanase (EC 3.2.1.8) from spent mushroom compost (SMC) of Pleurotus ostreatus, P. eryngii, and P. cornucopiae. Optimal enzyme recovery was achieved when SMCs were extracted with 50 mM sodium citrate (pH 4.5) buffer at 4℃ for 2 h...
متن کاملImmobilization of a Pleurotus ostreatus Laccase Mixture on Perlite and Its Application to Dye Decolourisation
In the present study, a crude laccase preparation from Pleurotus ostreatus was successfully immobilized on perlite, a cheap porous silica material, and tested for Remazol Brilliant Blue R (RBBR) decolourisation in a fluidized bed recycle reactor. Results showed that RBBR decolourisation is mainly due to enzyme action despite the occurrence of dye adsorption-related enzyme inhibition. Fine tunin...
متن کاملImprovement of Catalytic Efficiency, Thermo-stability and Dye Decolorization Capability of Pleurotus ostreatus IBL-02 laccase by Hydrophobic Sol Gel Entrapment
UNLABELLED BACKGROUND In serious consideration of the worldwide environmental issues associated with the extensive use of the textile dyes and effluents generated thereof, the scientists across the world are in search for potential treatment technologies for their treatment. In such scenario the ligninolytic enzymes provide a potential alternative because they are cost effective, eco-friendl...
متن کاملFactorial design for optimization of laccase production from Pleurotus ostreatus IMI 395545 and laccase mediated synthetic dye decolorization
In the present study, Plackett–Burman design (PBD) followed by response surface methodology (RSM) was used to optimize the culture medium composition for laccase production from Pleurotus ostreatus IMI 395545. Influence of carbon, nitrogen (sources) and inducer were evaluated by Plackett–Burman design. The factors that induce positive effect on enzyme production were further optimized using cen...
متن کاملThe white-rot fungus Pleurotus ostreatus secretes laccase isozymes with different substrate specificities.
Four laccase isozymes (LCC1, LCC2, LCC3 and LCC4) synthesized by Pleurotus ostreatus strain V-184 were purified and characterized. LCC1 and LCC2 have molecular masses of about 60 and 65 kDa and exhibited the same pI value (3.0). Their N termini were sequenced, revealing the same amino acid sequence and homology with laccases from other microorganisms. Laccases LCC3 and LCC4 were characterized b...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
دوره 2010 شماره
صفحات -
تاریخ انتشار 2010