Laccase Cross-Linked Ultraporous Aluminas for Sustainable Biodegradation of Remazol Brilliant Blue R

نویسندگان

چکیده

Over the past few decades, enzyme-based green and sustainable chemistry has attracted extensive research attention, which provides a promising alternative to conventional treatment methods of recalcitrant micropollutants. However, enzyme denaturation stability loss remain critical challenges for its potential applications in industrial wastewater treatment. In this study, laccase from Trametes versicolor (laccase T.) was cross-linked immobilized by ultraporous alumina (UPA) biodegradation Remazol Brilliant Blue R (RBBR). Through sequential use an aminosilane coupling agent (3-aminopropyl)triethoxysilane (APTES) bifunctional cross-linker glutaraldehyde (GA), synthesized biocatalysts showed better immobilization performances (about 4-fold physical adsorption). The GA concentration considerably affected T. cross-linking degree, while post-treatment protocol highest yield with lower activity recovery. Moreover, biocatalyst stabilities including pH stability, thermal storage reusability were also studied. Tolerance broader temperature ranges, good UPA(γ) biocatalysts, their continuous RBRR efficiency highlight potentials inorganic materials treatment, can broaden our understanding practical environmental fields.

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Purification and Characterization of Pleurotus florida Laccase (L1) involved in the Remazol Brilliant Blue R (RBBR) Decoloration

Pleurotus florida produces two extracellular laccase (L1 and L2) isoenzymes and the L1 isoenzyme is dominantly involved in the dye decoloration process. L1 isoenzyme was successfully purified to 6.4 fold with a yield of 36% and had a specific activity of 52.6 U mg of protein. The purified laccase was monomeric with an apparent molecular mass of ≈54 kDa. The optimum pH and temperature of the LI ...

متن کامل

Remazol Brilliant Blue R Dye Decolourization by Laccase Produced by Pleurotus Sajor-caju via Solid-State Fermentation

The application of synthetic dyes in various industries improved the aesthetic properties of the products, but the discharge of dye-containing effluent into water bodies leads to serious environmental problems. Till date, colour removal from effluent is still a challenge due to the absence of economically attractive treatments. In this study, decolourization of a synthetic dye – Remazol brillia...

متن کامل

Decolourisation of Remazol Brilliant Blue R via a novel Bjerkandera sp. strain.

A novel strain of Bjerkandera sp. (B33/3), with particularly high decolourisation activities upon Poly R-478 and Remazol Brilliant Blue R (RBBR) dyes, was isolated. The role of the ligninolytic extracellular enzymes produced by this strain on decolourisation of RBBR was studied in some depth. The basis of decolourisation is an enzyme-mediated process, in which the main enzyme responsible is a r...

متن کامل

Bio-bleaching of Remazol brilliant blue-19 by Stereum ostrea

Efficiency of white-rot fungi-Stereum ostrea (S. ostrea) as a test culture and Phanerochaete chrysosporium (P. chrysosporium) as a reference culture in colour removal from a textile dye, Remazol brilliant blue-19 (RBB-19) in medium was compared in this study. S. ostrea was more efficient than P. chrysosporium in decoloration process. Different parameters pH, temperature, sources of carbon and n...

متن کامل

Ligninolytic Enzymes Production and Remazol Brilliant Blue R Decolorization by Tropical Brazilian Basidiomycetes Fungi

Remazol Brilliant Blue R (RBBR) dye was used as substrate to evaluate ligninolytic activity in 125 basidiomycetous fungi isolated from tropical ecosystems. The extracellular RBBR decolorizing activity produced when selected fungi were grown in solid media and in soil contaminated with organochlorines was also evaluated. A total of 106 fungi decolorized the RBBR during the growth in malt extract...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Catalysts

سال: 2022

ISSN: ['2073-4344']

DOI: https://doi.org/10.3390/catal12070744