China 
Africa 
Explore chapters and articles related to this topic
Metabolic Engineering of Yeast, Zymomonas mobilis, and Clostridium thermocellum to Increase Yield of Bioethanol
Published in Ayerim Y. Hernández Almanza, Nagamani Balagurusamy, Héctor Ruiz Leza, Cristóbal N. Aguilar, Bioethanol, 2023
S. Sánchez-Muñoz, M. J. Castro-Alonso, F. G. Barbosa, E. Mier-Alba, T. R. Balbino, D. Rubio-Ribeaux, I. O. Hernández-De Lira, J. C. Santos, C. N. Aguilar, S. S. Da Silva
Inhibitors derived from fermentation process due to the pre-processing of lignocellulosic material limits the metabolism of strains in terms of microbial growth and biofuel production [71]. These inhibitors can be categorized into three major types: (i) furan derivatives, (ii) short-chain aliphatic acids and (iii) phenolic compounds, as reviewed by Palmqvist and Hahn-Hägerdal [72]. Among these compounds, furan derivatives such as furfural and 5-hydroxymethylfurfural (HMF) are some of the most toxic substances since they induced serious damages to cellular metabolism. Furfural and HMF inhibits glycolytic and fermentative enzymes (pyruvate, acetaldehyde, and alcohol dehydrogenases (ADHs)) and cause breaks in double-stranded DNA [73]. Thus, furan derivates also generate reduction in concentration of intracellular ATP and NAD(P)H because the energy flux is redirected to pentose phosphate pathway (PPP) for repairing the induced damages [74, 75]. Moreover, furfural also affect mitochondria and vacuole membranes, as it induces the formation of intracellular ROS [76]. All the cellular damages mentioned above result in prolongation of lag phase of microbial growth and decrease specific growth rate, which lead to low yield of biofuel production [46]. In addition, furfural also increase the toxicity of acetic acid and phenolic compounds [77, 78].
Cardiovascular Disease and Oxidative Stress
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2019
Marco Fernandes, Alisha Patel, Holger Husi
MPO is a key molecular mediator in a vast array of clinical conditions, such as in cardiovascular, inflammatory, neurodegenerative, renal and immune-mediated diseases (Lazarevic-Pasti et al., 2015). MPO and its downstream pathways might be attractive targets for therapeutic intervention or even prophylaxis action of these ailments. Development of new efficient and specific inhibitors is undergoing using state-of-the-art virtual screening procedures (VSP), based on ligand-pharmacophore modelling (Soubhye et al., 2017). Oral administration of PF-1355, an MPO inhibitor, to a mice model of myocardial infarction (MI), decreased enzymatic MPO activity, likewise decreased the number of inflammatory cells and decreased left ventricular dilation (LVD). Extending the period of treatment lead to an improved outcome of both cardiac function and remodelling (Ali et al., 2016).
Biodegradation of Phenol
Published in Donald L. Wise, Debra J. Trantolo, Remediation of Hazardous Waste Contaminated Soils, 2018
C. Vipulanandan, S. Wang, S. Krishnan
The inhibition of bacterial growth is often due to the inhibition of enzyme systems. An enzyme inhibitor reduces the rate of an enzymatically catalyzed reaction by binding either with the free enzyme and/or with the enzyme-substrate complex. Three types of models are frequently used to explain cell growth inhibition: competitive, noncompetitive, and uncompetitive. Competitive inhibition occurs when a substrate competes with another substrate for a site on either the cell or the enzyme. Noncompetitive inhibition occurs when the inhibitor can combine with both the free cell or enzyme and the cell/enzyme–substrate complex. An uncompetitive inhibitor binds with the cell/enzyme-substrate complex, which cannot undergo further reaction to yield product. Uncompetitive inhibition is believed to be the most frequently responsible mechanism for cell growth inhibition.
Textile azo dyes discolouration using spent mushroom substrate: enzymatic degradation and adsorption mechanisms
Published in Environmental Technology, 2023
Juliana Barden Schallemberger, Nelson Libardi, Beatriz Lima Santos Klienchen Dalari, Mariane Bonatti Chaves, Maria Eliza Nagel Hassemer
In contrast, in the Linewaever-Burk linearisation (Figure 2B), the lines referring to NaCl concentrations and the absence of inhibitor intersect in the same area of the graph’s abscissa, however they intersect different areas of the ordinate, inferring a non-competitive inhibition. In this type of inhibition, the inhibitor binds to the enzyme at a different site from the active site, allowing normal binding of the substrate with the enzyme, however, complete inactivation of the enzyme occurs which prevents the conversion of the substrate into product. With the decrease in the amount of active enzymes in the medium as the inhibitor binds to the enzyme, the Vmax is reduced, while the Km is not affected as the inhibitor does not block the active enzyme site [70]. However, it was found that Km increased in the presence of NaCl. In contrast, Enaud et al. [71] found a competitive inhibition between ABTS and NaCl by representing Lineweaver–Burk, albeit a mixed inhibition according to the Cornish-Bowden model.
Cecropia pachystachya Trécul: identification, isolation of secondary metabolites, in silico study of toxicological evaluation and interaction with the enzymes 5-LOX and α-1-antitrypsin
Published in Journal of Toxicology and Environmental Health, Part A, 2022
Penina Sousa Mourão, Rafael de Oliveira Gomes, Clara Andrezza Crisóstomo Bezerra Costa, Orlando Francisco da Silva Moura, Herbert Gonzaga Sousa, George Roberto Lemos Martins Júnior, Danniel Cabral Leão Ferreira, Antônio Luiz Martins Maia Filho, Johnnatan Duarte de Freitas, Mahendra Rai, Francisco Das Chagas Alves Lima, Antonio Euzébio Gourlart Santana, Mariana Helena Chaves, Wellington Dos Santos Alves, Valdiléia Teixeira Uchôa
CYP2C9, CYP2C19, CYP2D6, and CYP3A4 are important enzymes in drug interactions and belong to the cytochrome P450 enzyme family, which is a family of monooxygenases involved in drug metabolism and responsible for metabolism of xenobiotics (Braz et al. 2018; Silva, da Silva, and Holanda 2020; Silvado 2008). Inhibition of these enzymes may trigger unwanted effects such as drug accumulation and or increased toxicity of the drug affected by the interaction, or reduced effectiveness (Braz et al. 2018). The last prediction analyzed here in PreADMET results is the similarity of bioactive compounds to a drug, which can be described by Lipinski´s Rule (also known as Lipinski´s Rule 5) which establishes molecular parameters to determine if molecules display reliable potential to become a new drug (Gomes and Leite 2021).
Production of cellulases by Thermomucor indicae-seudaticae: characterization of a thermophilic β-glucosidase
Published in Preparative Biochemistry and Biotechnology, 2019
Eduardo da Silva Martins, Eleni Gomes, Roberto da Silva, Rodolfo Bizarria Junior
Most microbial β-glucosidases are inhibited by glucose, which becomes a major limitation for the use of these enzymes in industrial processes.[12] High glucose concentrations may directly or indirectly interfere with the binding of the substrate to the activated site, reducing the reaction rate.[32] Inhibition of β-glucosidase produced by T. indicae-seudaticae was completely reversed when the substrate concentration increased but maintained the same glucose concentration. The present work demonstrated that the interaction of the enzyme with the inhibitor is competitive. Competitive inhibition may be reversed by increasing the substrate concentration, which does not occur in noncompetitive inhibition. In competitive inhibition, the inhibitor and the substrate compete for the active site of the enzyme. Thus, increased concentration favors enzyme binding to the substrate, which is reflected in the reversibility of enzymatic inhibition.[20]