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678,193 result(s) for "Enzymes"
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Enzymes : a very short introduction
\"Enzymes are the astonishing, tiny molecular machines that make life possible. Each one of these small proteins speeds up a single chemical reaction inside a living organism many millionfold. Working together, teams of enzymes carry out all the processes that collectively we recognise as life, from making DNA to digesting food. This Very Short Introduction explains the why and the how of speeding up these reactions - catalysis - before going on to reveal how we have evolved these catalysts of such extraordinary power and exquisite selectivity. Paul Engel shows how X-ray crystallography has revealed the complex molecular shapes that allow enzymes to function at an extraordinarily sophisticated level. He also examines medical aspects of enzymes, both in the way faulty enzymes cause disease and in the way enzymes can be used for diagnosis and therapy. Finally, he looks at the many varied ways in which individual enzymes, taken out of their biological context, are used nowadays as tools - in washing powders, food production, waste treatment, and chemical synthesis.\"--Amazon.ca
Statistical Optimization of alpha-Amylase Production from Novel Local Isolated Bacillus spp. NRC1 and Its Textile Applications
By employing Plackett-Burman design (PBD) to investigate the qualitative interactions between eleven parameters [potato shell weight, incubation time, glucose, lactose, baker's yeast, peptone, (NH.sub.4).sub.2SO.sub.4, CuSO.sub.4, FeSO.sub.4, CaCl.sub.2, KCl], and central composite design (CCD), the production of [alpha]-amylase by a local bacterial isolate Bacillus spp. NRC1 using agro-industrial wastes was improved. Using a variety of waste materials, including corn cobs (CC), onion peels (OP), rice straw (RS), potato shells (PS), Molokhia stem (MS), okra suppression (OS), lemon peels (LP), and pea peels (PP), Bacillus spp. NRC1 was tested in the production of amylase. Out of the eight agro-industrial wastes tried, the highest amylase yield (6.99 U/ml) was reached using potato peels. The statistical optimization of enzyme production was carried out using PBD followed by CCD design, causing 2.06-fold and 1.51-fold increase, respectively. The overall increase was 3.11-fold. In PBD design, potato peels, peptone and (NH.sub.4).sub.2SO.sub.4 were positive factors for amylase production. The crude enzyme was tested for its ability to desize cotton fabric and subsequently studying its effect on fabric dyeability. The produced amylase proved its potentials in textile industry.
Cape Gooseberry —Selected Aspects
Vacuum-Assisted Sorbent Extraction (VASE) is a novel extraction technique that uses vacuum to facilitate the transfer of volatile compounds from the matrix to the sorbent. This technique was explored for extraction of volatiles from cape gooseberry fruit, for both qualitative and quantitative analyses. Selected extraction parameters were tested: sample size, extraction temperature and time, influence of tissue disintegration on release of volatiles, and also addition of Ag[sup.+1] ions in the form of AgNO[sub.3] to stop enzymatic formation of volatile compounds. For selected conditions (10 g sample, extraction for 30 min. at 40 °C of volatiles from blended fruit) quantitative aspects were explored. Twenty-two compounds of cape gooseberry were tested. The method was characterized with a very good linearity in a range of 10–5000 µg/kg and good reproducibility. The experiments proved the usefulness of VASE in both volatile profiling and quantitative analyses of cape gooseberry and in prospective other fruit.
Nitazoxanide Inhibits the Bifunctional Enzyme GlG6PD::6PGL of IGiardia lamblia/I: Biochemical and In Silico Characterization of a New Druggable Target
Giardiasis, which is caused by Giardia lamblia infection, is a relevant cause of morbidity and mortality worldwide. Because no vaccines are currently available to treat giardiasis, chemotherapeutic drugs are the main options for controlling infection. Evidence has shown that the nitro drug nitazoxanide (NTZ) is a commonly prescribed treatment for giardiasis; however, the mechanisms underlying NTZ’s antigiardial activity are not well-understood. Herein, we identified the glucose-6-phosphate::6-phosphogluconate dehydrogenase (GlG6PD::6PGL) fused enzyme as a nitazoxanide target, as NTZ behaves as a GlG6PD::6PGL catalytic inhibitor. Furthermore, fluorescence assays suggest alterations in the stability of GlG6PD::6PGL protein, whereas the results indicate a loss of catalytic activity due to conformational and folding changes. Molecular docking and dynamic simulation studies suggest a model of NTZ binding on the active site of the G6PD domain and near the structural NADP[sup.+] binding site. The findings of this study provide a novel mechanistic basis and strategy for the antigiardial activity of the NTZ drug.