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New Insights into Feruloyl Esterase
Published in Jitendra Kumar Saini, Surender Singh, Lata Nain, Sustainable Microbial Technologies for Valorization of Agro-Industrial Wastes, 2023
Spectrophotometric methods are easy to perform and quantify the activity of feruloyl esterase. Destarched wheat bran is used as a substrate to produce feruloyl esterase by Fusarium oxysporum. The assay is done by using 100 mM MOPS buffer at pH-6 (Topakas et al., 2003). Esterase activity is detected using various substrates, such as p-NP and methyl ester. DMSO or isopropanol are used to dissolve the substrates. The release of p-nitrophenol is recorded at 420 nm in a UV spectrophotometer (Abokitse et al., 2010). Donnelly and Crawford (1988) used p-nitrophenyl butyrate to quantify the amount of extracellular enzyme by spectrophotometric method. Gopalan et al. (2016) used ethyl ferulate as a substrate for enzyme assay.
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
Esterases are enzymes that catalyze an ester group hydrolysis from a range of substrates to produce the esterified acid (Gopalan and Nampoothiri, 2016). They comprise both lipolytic enzymes, such as enzymes that use lipids as substrate, also called lipases, and non-lipolytic esterases, which are active on the substrates of the water-soluble ester. Regrettably, in scientific journals, the words “esterases” and “lipases” are sometimes used indiscriminately (Thierry et al., 2017). The three major criteria that differentiate between true lipases and nonlipolytic esterases are length, the physicochemical composition of the substrate, and enzyme kinetics of the hydrolyzed acyl ester chain (Wilkinson, 2004).
Carbamates
Published in Fina P. Kaloyanova, Mostafa A. El Batawi, Human Toxicology of Pesticides, 2019
Fina P. Kaloyanova, Mostafa A. El Batawi
Carbamates (except benzimidazol compounds) inhibit esterases. They produce carbamylation of acetylcholinesterase similar to the phosphorylation of AChE produced by organo-phosphorous compounds. Carbamates differ from OPs in the low stability of the carbamylated enzyme and the lack of the aging reaction.18 A consequence is the rapid recovery from acute poisoning. The zone of acute effect, determined by the ratio LD50:Lim ac, is much larger than that of OPs. The symptoms of intoxication develop quickly after exposure, long before the absorption of a dangerous dose, and thus prevent heavy intoxication. Recovery is very rapid, and cumulation of the effect is insignificant.
Allelopathic effect of Oocystis borgei culture on Microcystis aeruginosa
Published in Environmental Technology, 2022
Xiaoqian Wang, Yulei Zhang, Changling Li, Xianghu Huang, Feng Li, Xinyu Wang, Guanbao Li
During the e-culture experiment, the effects of filtrate on cell membrane integrity and esterase activity were analyzed using flow cytometry (FCM) (BDFAC Verse, USA) following previous studies [44,45]. The changes in esterase activity were measured by the fluorescence of fluorescein diacetate (FDA). A stock solution of FDA (10 mg mL−1, Sigma F-7378) dissolved in acetone was prepared and stored at −20°C before further use. Before each experiment, a working solution (0.5 mg mL−1) was prepared by adding acetone and kept in the dark. Cell staining was performed by treating 1 mL algal suspensions with 20 μL of FDA working solution and incubated for 20 min at 25°C. Esterase activity was measured from the flow cytometer (515–545 nm). According to Xiao [40,44] and Regel [46], frequency histograms of fluorescence data for cells were used to define esterase activity states. Three states were defined:a higher activity state, R1, corresponded to an esterase activity above the normal range, the normal state, R2, corresponded to the esterase within the normal range, a low activity state, R3, corresponded to the esterase of damaged cells.
Improved stability and catalytic activity of graphene oxide/chitosan hybrid beads loaded with porcine liver esterase
Published in Preparative Biochemistry and Biotechnology, 2018
Shruthi Sunderrajan, Lima Rose Miranda, Gautam Pennathur
The hydrolysis of esters is catalyzed by esterases with high enantioselectivity and regioselectivity at different temperatures, pH, and solvents.[1] This allows for large-scale, efficient, and cost-effective production of industrially important molecules in the food and perfume industries. Porcine liver esterase (PLE) is a commercially important enzyme with applications in food, beverage, and pharmaceutical industries.[2,3] It has been used for organic synthesis, especially in the resolution of secondary alcohols.[4]
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
Esterases are enzymes responsible for the catalysis of hydrolytic reactions in organophosphate pesticides. There are different types of esterases that facilitate the hydrolysis of amides, carboxylic esters, and phosphate esters and are known as amidases, carboxylesterases, and phosphatases, respectively. Acetylcholine esterase constitutes a prime enzyme system that is responsible for the degradation of malathion in mammals.51 Esterases are responsible for the hydrolysis of esters to their respective alcohols and acid components as follows: