Acetylcholinesterase biosensors for electrochemical detection of neurotoxic pesticides and acetylcholine neurotransmitter: A literature review.

Neurotoxic pesticides are a group of chemicals that pose a severe threat to both human health and the environment. These molecules are also known to accumulate in the food chain and persist in the environment, which can lead to long-term exposure and adverse effects on non-target organisms. The detrimental effects of these pesticides on neurotransmitter levels and function can lead to a range of neurological and behavioral symptoms, which are closely associated with neurodegenerative diseases. Hence, the accurate and reliable detection of these neurotoxic pesticides and associated neurotransmitters is essential for clinical applications, such as diagnosis and treatment. Over the past few decades, acetylcholinesterase (AchE) biosensors have emerged as a sensitive and reliable tool for the electrochemical detection of neurotoxic pesticides and acetylcholine. These biosensors can be tailored to utilize the high specificity and sensitivity of AchE, enabling the detection of these chemicals. Additionally, enzyme immobilization and the incorporation of nanoparticles have further improved the detection capabilities of these biosensors. AchE biosensors have shown tremendous potential in various fields, including environmental monitoring, clinical diagnosis, and pesticide residue analysis. This review summarizes the advancements in AchE biosensors for electrochemical detection of neurotoxic pesticides and acetylcholine over the past two decades.

Efficient decolorization and detoxification of triarylmethane and azo dyes by porous-cross-linked enzyme aggregates of Pleurotus ostreatus laccase.

In this preset study, porous-cross-linked enzyme aggregates (CLEAs) of Pleurotus ostreatus laccase were utilized for the spontaneous decolorization and detoxification of triarylmethane and azo dyes, reactive blue 2 (RB) and malachite green (MG). The specific surface area and pore radius of the porous-CLEAs are 136.3 m2/g and 19.47 Ao, and the higher specific surface indicated greater biocatalytic efficiency, as increased mass transfer and dye interaction with the CLEAs laccase. CLEAs laccase decolorized 500 ppm of MG and RB with 98.12-58.33% efficiency after 120 min, at pH 5.0 and 50°C, without a mediator. Furthermore, the biotransformation of the MG and RB with immobilized laccase was confirmed with the help of UV-visible spectroscopy, high-performance liquid chromatography, and Fourier transform infrared spectroscopy. The reusability potential of CLEAs was assessed in batch mode for 10 cycles of dye decolorization. The decolorization activities for the immobilized laccase were 89% and 12% at the 6th cycle for MG and RB, respectively. This immobilized enzyme could effectively remove dyes from aqueous solution, and demonstrated significant detoxification in experimental plants (Triticum aestivum and Phaseolus mungo) and plant growth-promoting rhizobacteria (Azospirillum brasilense, Bacillus megaterium, Rhizobium leguminosarum, Bacillus subtilis, and Pseudomonas fluorescens). In conclusion, porous CLEAs laccase could be useful as a potential bioremediation tool for the detoxification and decolorization of dyeing wastewater in future.

Amino-functionalised mesoporous silica microspheres for immobilisation of Candida antarctica lipase B - application towards greener production of 2,5-furandicarboxylic acid.

In the present study, amino-functionalised mesoporous silica microspheres were utilised as support for the covalent immobilisation of Candida antarctica lipase B (CaLB) for the subsequent production of 2,5-furandicarboxylic acid (FDCA) from 2,5-diformylfuran (DFF). Under the optimised operating conditions of pH 6.5, particle/enzyme ratio of 1.25:1.0 and glutaraldehyde concentration of 4 mM, a maximum CaLB immobilisation yield of 82.4% on silica microspheres was obtained in 12.25 h. The immobilised CaLB was used for the synthesis of alkyl esters, which were utilised along with hydrogen peroxide for FDCA synthesis. The biocatalytic conversion of 30 mM DFF dictated a 77-79% FDCA in 48 h at 30°C; where the turnover number and turnover frequency of immobilised CaLB were 6220.73 mol mol-1 and 129.59 h-1, respectively, for ethyl acetate, against 6297.65 mol mol-1 and 131.2 h-1, respectively, for ethyl butyrate. Upon examining the operational stability, the immobilised CaLB exhibited high stability till five cycles of FDCA production.

Recent developments in the use of tyrosinase and laccase in environmental applications.

Our current global environmental challenges include the reduction of harmful chemicals and their derivatives. Bioremediation has been a key strategy to control the massive presence of chemicals in the environment. Enzymes including the phenoloxidases, laccases and tyrosinases, are increasingly being investigated as "green products" in the removal of many chemical contaminants in waters and soils. Both phenoloxidases are widespread in nature and attractive biocatalysts due to their ability to use readily available molecular oxygen as sole cofactor for their catalytic elimination of a large number of chemicals. Taking advantage of their catalytic potentials, remarkable advances have been made in the engineering of laccases to produce suitable biocatalysts in environmental applications. Studies about novel strategies of laccase immobilization and insolubilization for the treatment of chemical contaminants were provided. Likewise, tyrosinases are gaining increasing interest in environmental applications due to their catalytic similarities with laccases although they remain far less investigated to date. This disparity was addressed in this review along with the molecular features and catalytic mechanism of tyrosinases relevant in environmental applications. A perspective on the future use of laccases and tyrosinases in bioremediation was discussed.