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Scope and Application of Bionanotechnology for the Bioremediation of Emerging Contaminants Generated as Industrial Waste Products
Published in Naveen Dwivedi, Shubha Dwivedi, Bionanotechnology Towards Sustainable Management of Environmental Pollution, 2023
Md Shahid Alam, Surabhi Rode, Harry Kaur, Sapna Lonare, Deena Nath Gupta
Carboxylesterase (CbE) hydrolyses carboxyl esters and degrades various insecticides such as organophosphates, pyrethroids, and carbamates. The combination of nanotechnology and the enzymatic approach is well established due to its recyclable and robust characteristics. Diao et al. (2013) immobilized insect (Spodoptera litura) CbE on mesoporous silica nanoparticles (SBA-15 and MCM-41) (Diao et al., 2013). Taking advantage of mesoporous material, the enzyme was immobilized to enhance its insecticide degrading property. The SBA-15 immobilized enzyme degraded 60% of Malathion (organophosphate) and 50% of Diethofencarb (carbamate) in the initial two hours of exposure. The enzyme exhibited its activity even in organic solvents and a denaturing agent such as urea. Based on the stability, catalytic efficiency, and lower loading time, SBA-15 is a preferable platform over MCM-41. The larger pores of SBA-14 rendered more significant immobilization potential and thus ensured a higher rate of insecticide degradation.
Application of Polymer Drugs to Medical Devices and Preparative Medicine
Published in Severian Dumitriu, Valentin Popa, Polymeric Biomaterials, 2020
M.R. Aguilar, L. García-Fernández, M.L. López-Donaire, F. Parra, L. Rojo, G. Rodríguez, M.M. Fernández, J. San Román
On the other hand, research is also focused on the enzymatic degradation of the linker bond. In this sense, poly(oleyl 2-acetamido-2-deoxy-α-d-glucopyranoside methacrylate-co-N-vinyl pyrrolidone) was developed as an active glycopolymer for brain tumor where the drug delivery occurs via ester hydrolysis by the presence of carboxylesterase enzyme (Lopez Donaire et al., 2009).
Esterases and Their Industrial Applications
Published in Pankaj Bhatt, Industrial Applications of Microbial Enzymes, 2023
Hamza Rafeeq, Asim Hussain, Ayesha Safdar, Sumaira Shabbir, Muhammad Bilal, Farooq Sher, Marcelo Franco, Hafiz M. N. Iqbal
In 1978, a new classification scheme was introduced by the NC-IUBMB (Walker and Mackness, 1983). Carboxylesterases (EC 3.1.1.1) or carboxylic ester hydrolases, also known as aliesterases, are most commonly found on open chains of organic molecules (i.e., aliphatic molecules), in comparison with arylesterases (EC 3.1.1.2), also referred to as paraoxonases, Est-A hydrolyases, or aryl ester hydrolyses that are primarily active in treating aromatic compounds and capable of hydrolysis. However, EC 3.1.1.1 enzymes may also hydrolyze compounds of aryl ester, while EC 3.1.1.2 may hydrolyze open-chain esters of carboxylic esters but are not their preferred substrate.
A comprehensive review on enzymatic degradation of the organophosphate pesticide malathion in the environment
Published in Journal of Environmental Science and Health, Part C, 2019
Smita S. Kumar, Pooja Ghosh, Sandeep K. Malyan, Jyoti Sharma, Vivek Kumar
Carboxylesterase is a group of nonspecific enzymes widely distributed in nature and have been isolated and purified from vertebrates and plants. Carboxylesterases catalyze the conversion of carboxylic acid ester groups to their respective acid anions and alcohols. Owing to this capability, they are efficiently used for the remediation of carbamates, organochlorine pesticides, organophosphates, and pyrethroid contaminated wastewater. It belongs to the a/b-hydrolase family of enzymes and includes cholinesterases, epoxide hydrolases, and phosphotriesterases. Carboxylesterases inhibited by organophosphates are known as β-esterases and those not inhibited are hydrolyzing esters. Most of the microbial species capable of degrading and metabolizing malathion as a sole carbon and energy source have been observed to produce different variations of carboxylesterase enzyme.
Biological activities and gene expression of detoxifying enzymes in Tribolium castaneum induced by Moutan cortex essential oil
Published in Journal of Toxicology and Environmental Health, Part A, 2022
Xin Li, Yanjun Xu, Jing Liu, Xiaoxue Yu, Wenjuan Zhang, Chunxue You
Carboxylesterase (CarE), glutathione S-transferase (GST), and cytochrome P450 (CYP450) are three major detoxification enzymes involved in metabolizing the xenobiotic compounds in insects (Gao et al. 2020; Pajaro-Castro, Caballero-Gallardo, and Olivero-Verbel 2017; Wang et al. 2020b). GST plays a critical role in detoxification of exogenous and endogenous toxic substances in insects by catalyzing conjugation reactions of electrophilic compounds with endogenous glutathione (GSH) (Francis, Vanhaelen, and Haubruge 2005; Li et al. 2013). Carboxylesterase (CarE) constitutes a superfamily of metabolic enzymes that hydrolyze carboxylic esters and plays an important role in xenobiotic detoxification (Gong et al. 2016). CYPs not only play vital roles in the metabolism of endogenous compounds, including steroids, fatty acids, and hormones, but also are well known for their ability to oxidatively metabolize various plant allelochemicals such as terpenoids, furanocoumarins, flavonoids, alkaloids, lignans, and pyrethrins (Li, Schuler, and Berenbaum 2007; Wang et al. 2020a). An important aspect of elucidating underlying mechanisms of insecticidal actions is determining the changes in detoxifying enzymes in insects after exposure to the insecticides (Zhou et al. 2016). For instance, the up-regulated genes in Spodoptera frugiperda encoding detoxifying enzymes including CYP450, GST, and CarE may be involved in azadirachtin degradation (Shu et al. 2021). The up-regulated GSTs and CYP450s function cooperatively and participate in the metabolism of terpinen-4-ol in Sitophilus zeamais (Huang et al. 2018). However, the underlying mechanism of insecticidal actions of Moutan cortex essential oil against T. castaneum was not investigated. In this investigation, roles of the three most important detoxification enzymes in the response of T. castaneum to Moutan cortex essential oil were examined, which might contribute to understanding the underlying insecticidal mechanisms of action.