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Extremophilic Microbes and their Extremozymes for Industry and Allied Sectors
Published in Ajar Nath Yadav, Ali Asghar Rastegari, Neelam Yadav, Microbiomes of Extreme Environments, 2021
Hiran Kanti Santra, Debdulal Banerjee
Other than OP degradation these extremozymes could be exploited for the elimination of undesired microorganisms from water purifying plants by using lactonases immobilized on membrane filters (Ng et al. 2011). This trait of these enzymes was achieved due to their ability to interfere with bacterial quorum sensing property by the Sso Pox lactonase activity on acylhomoserine lactones. Another report includes the use of mutant Sso Pox (W263F) as a detoxification tool. The enzyme was dissolved in several buffered aqueous solvents (like 30% ethanol, 30% or 50% methanol and 0.1% sodium-dodecyl-sulfate) to evaluate its catalytic activity under stressing denaturing conditions. One such example includes the toxin extraction from contaminated soils (Merone et al. 2010; Hiblot et al. 2012a). The results were compared with those obtained with bd PTE from B. diminuta. It was revealed that W263F outperforms bd PTE in most of the tested situations. After a 15 minute treatment at room temperature 99.5% of paraoxon was hydrolized in 30% methanol and ethanol and 0.1% sodium-dodecyl-sulfate (Merone et al. 2010). PLL enzymes have proved to be successful for OP detoxification. It is a fact that p-nitrophenol produced by paraoxon and parathion hydrolysis is toxic in nature but lesser toxicity is reported than the original OP and there are soil bacteria that are able to degrade p-nitrophenol by utilizing it as carbon source (Munnecke 1979) offers complete removal of these xenobiotics from nature (Spain and Gibson 1991).
The Pentose Phosphates Pathway—Glucogenesis
Published in Jean-Louis Burgot, Thermodynamics in Bioenergetics, 2019
The enzyme catalyzing the reaction is the glucose-6-phosphate dehydrogenase. The lactone is hydrolyzed to the acid-6-phosphogluconate under the action of a specific lactonase (Figure 101): Structure of 6-phosphogluconate acid.Then, the 6-phosphogluconate acid undergoes oxidation and decarboxylation. The keto-pentose ribulose-5-phosphate is formed under the action of the enzyme 6-phosphogluconate dehydrogenase. It is interesting to notice that, then, there is formation of a second molecule of NADPH (Figure 102): 6-phosphogluconateacid→6-phosphogluconatedehydrogenaseD-ribulose-5-phosphateFormation of ribulose-5-phosphate.
Natural enzymes used to convert feedstock to substrate
Published in Ruben Michael Ceballos, Bioethanol and Natural Resources, 2017
Lactonase (EC 3.1.1.17), also called d-glucono-1,5-lactone lactonohydrolase, aldonolactonase, or gluconolactonase, catalyzes the hydrolysis of different types of hexose-1,5-lactones to their corresponding aldonic acids (Brodie and Lipmann, 1955; Beeson et al., 2011). Lactonase is found in commercial preparations of enzymes (e.g., Novozyme 188) from Trichoderma reesei and Aspergillus niger (Bruchmann et al., 1987). As a side effect, lactonase can facilitate cellulolysis as it removes lactones, which also inhibit cellulases (Bruchmann et al., 1987; Rouyi et al., 2014).
Production of highly soluble native human paraoxonase 2 with potential anti-biofilm property
Published in Preparative Biochemistry & Biotechnology, 2023
Fauzia Parween, Priyamedha Yadav, Kalyani Singh, Rinkoo Devi Gupta
HuPON2 has been characterized as a highly promiscuous enzyme in vitro and non-enzymatic functions as an antioxidant in vivo.[11,12] The role of HuPON2 as an anti-biofilm agent in gram-negative bacteria is known owing to its lactonase activity for the hydrolysis of Acyl-HSL.[6] However, the primary QS molecules in Mycobacteria is poorly explored.[13,14] Hence in this study, we aim to further extend the anti-biofilm property of HuPON2 due to its promiscuous nature. Herein, we studied the biofilm inhibition in Mycobacterium smegmatis (M. smeg.), which is a model organism to study Mycobacteria in general, due to its nonpathogenic nature and a short generation time.[15]