期刊
BIORESOURCE TECHNOLOGY
卷 340, 期 -, 页码 -出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.biortech.2021.125591
关键词
Remazol Brilliant Blue R; Laccase; Decolourisation; Molecular docking; Box-Behnken design
资金
- Council of Scientific & Industrial Research (CSIR) , New Delhi [33/2018/MD-FFTFTC-ANB, MLP-10]
- CSIR-IITR [IITR/SCE/2021-2022/10]
The biodegradation of environmentally hazardous synthetic dyes by enzymes, particularly laccase derived from Arthrographis kalrae, has received significant attention in recent years. Through the Box-Behnken design approach, optimal dye decolourisation of Remazol Brilliant Blue R was achieved with a 97.18% efficiency. Fourier Transform Infrared Spectroscopy and UV-Visible Spectrophotometry confirmed the biodegradation process, while extra Precision Glide docking revealed a strong binding affinity between laccase and RBBR complex.
Biodegradation of environmentally hazardous synthetic dyes by enzymes has been achieved the highest interest in recent years. In this work, we optimized Remazol Brilliant Blue R (RBBR) dye biodegradation by Arthrographis kalrae derived laccase via the Box-Behnken design (BBD) approach of the surface response methodology (RSM). Optimization of dye decolourisation by one variable at a time (OVAT) approach resulted in optimal dye decolourisation at laccase dose (2 IU mL(-1)), pH (7.0), temperature (35 degrees C), incubation time (240 min), and initial dye concentration (100 mg L-1). The optimized process through BBD enhanced dye decolourisation (97.18%). Fourier Transform Infrared Spectroscopy and UV-Visible Spectrophotometry have proven biodegradation. In addition, in comparison to untreated samples, the laccase-treated dye sample showed relatively less phyto- and cytotoxic effect on Allium cepa L. Extra Precision Glide docking exhibited the binding affinity score of -5.355 kcal mol(- 1), between laccase-RBBR complex.
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