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Industrial Applications of Bacterial Enzymes
Published in Pankaj Bhatt, Industrial Applications of Microbial Enzymes, 2023
Enzymes are used in different processes industrially, like in pharmaceuticals, detergents, baking products, leather, textiles, brewing, foods and juices, dairy, cosmetics, pulp and paper, and waste management. Here is a range of methods presenting how enzymes obtained from bacteria are used in different broad categories.
The Biosphere
Published in Stanley E. Manahan, Environmental Chemistry, 2022
Enzymes are biochemical catalysts that are very important in metabolism. Enzymes speed up metabolic reactions by as much as almost a billion-fold. In addition to making reactions go much more rapidly, enzymes are often highly specific in the reactions that they catalyze. The reason for the specificity of enzymes is that they have very specific structures that fit with the substances upon which they act.
Introduction
Published in Jean-Luc Wertz, Bénédicte Goffin, Starch in the Bioeconomy, 2020
Jean-Luc Wertz, Bénédicte Goffin
Starch must be broken down into glucose before the cells can use it, either as a source of energy or as building blocks for other molecules. This preliminary stage in the breakdown of starch is called digestion. The large polymeric molecules are broken down during digestion into glucose through the action of enzymes. After digestion, glucose enters the cytosol of the cell, where its gradual oxidation begins: glycolysis, the initial stage of glucose metabolism, does not involve molecular oxygen and produces a small amount of ATP and the three-carbon compound pyruvate. In aerobic cells, pyruvate formed in glycolysis is transported into the mitochondria, where it is oxidized by oxygen to carbon dioxide. Through chemiosmotic coupling, the oxidation of pyruvate in the mitochondria generates the bulk of the ATP produced during the conversion of glucose to carbon dioxide. The oxidation of pyruvate involves the citric acid cycle, in which acetyl CoA derived from pyruvate is modified to produce energy precursors in preparation for the next step, and the oxidative phosphorylation, in which ADP is transformed into ATP.
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.
Extremozymes used in textile industry
Published in The Journal of The Textile Institute, 2022
Priyanka Kakkar, Neeraj Wadhwa
Enzymes are widely used in the industrial processes by replacing various process including chemical reactions. But still most of the companies are unable to use these enzymes because of their inability to work under extreme conditions. The unique adaptations of extremozymes allow them to be used as a biocatalyst in industrial processes including unfavourable conditions. They give opportunities to improve enzyme technologies and to come up with highly attractive, sustainable, cost-effective, eco-friendly approach when compared to chemical catalysis (Sarmiento et al., 2015). Enzymes are used in various industries like food, pharmaceuticals, textile, detergent, beverages, paper, and leather. In textile industry, cellulase, xylanase, protease, lipase, amylase, pectinase, catalases are the important enzymes used in the finishing methods i.e. desizing, bioscouring, biostoning, biobleaching, biopolishing. Protein engineering and other technologies can be used to improve the extremozyme production and for heterologous expression of protein in mesophilic host (Cabrera & Blamey, 2018). Extremozymes are used in various industrial processes and by using protein engineering production yield of industrially important enzymes can be increased in a cost effective manner.
A contemporary review of enzymatic applications in the remediation of emerging estrogenic compounds
Published in Critical Reviews in Environmental Science and Technology, 2022
Jakub Zdarta, Luong N. Nguyen, Katarzyna Jankowska, Teofil Jesionowski, Long D. Nghiem
Numerous techniques have been developed to improve the stability, efficiency and reusability of enzymes. Enzyme immobilization has been established as the most promising and practically important to improve enzyme stability, efficiency, and reusability (Ba & Kumar, 2017). It is also considered as the most effective technique for practical application of immobilized biocatalysts. Enzyme immobilization techniques are principally based on the attachment of biomolecules, by way of adsorption and/or covalent interactions, to insoluble support materials. However, methods of enzyme immobilization by entrapment and encapsulation into the matrix structure have been also developed (Bilal et al., 2018b, Zdarta et al., 2018a, 2018b). One of the greatest advantages of the enzyme immobilization is stabilization of the biocatalysts structure that prevents enzyme against inactivation at harsh reaction conditions (Jesionowski et al., 2014). Immobilization may also reduce enzyme inactivation due to denaturation and inhibition, leading to the longer retention of high catalytic activity. Further, separation of the immobilized enzyme from the reaction mixture and retention in continuous processes are also improved (Arca-Ramos et al., 2016). Finally, the use of immobilized enzymes expands the range of possible bioreactor configurations for highly efficient biocatalytic processes (Mateo et al., 2007). The described advantages of immobilization enhance the utility and reusability of immobilized enzymes in the removal of estrogens.