04-12-2014, 07:26 AM
microbial enzymes and their applications ppt
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microbial enzymes and their applications ppt
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microbial enzymes and their applications ppt
17-03-2017, 04:49 PM
Enzymes are considered as a potential biocatalyst for a large number of reactions. In particular, microbial enzymes have wide uses in industries and medicine. Microbial enzymes are also more active and stable than plant and animal enzymes. In addition, microorganisms represent an alternative source of enzymes because they can be grown in large quantities in a short time by fermentation and because of their biochemical diversity and susceptibility to gene manipulation. Industries are looking for new microbial strains in order to produce different enzymes to meet current enzyme requirements. This special issue covers ten articles, including three review articles, highlighting the importance and applications of valuable microbial enzymes from a biotechnological and industrial point of view.
M. Dinarvand et al. In their work they optimized the conditions for the overproduction of intracellular inulinase and invertase of the fungus Aspergillus niger ATCC 20611. Optimization is one of the most important criteria in the development of any new microbial process. Response surface analysis is one of the vital tools for determining optimum process conditions. This type of design of a limited set of variables is advantageous compared to the conventional method. The response surface methodology was used for this optimization and achieved the increase up to 16 times. This study would be very useful for potential application in fermentation industries.
In this review, N. Gurung et al. They have made an attempt to highlight the importance of different enzymes with a special focus on amylase and lipase. Enzymes generally increase reaction rates several times more than normal chemical reactions. Lipases play an important role in the food, detergent, chemical and pharmaceutical industries. In the past, microbial lipases have gained significant attention in industries because of their substrate specificity and their stability under varying conditions. Amylase is an enzyme that catalyzes the decomposition of starch into sugars, abundant in the process of animal and human digestion. The main advantage of microbial amylases is that it is economical and easy to handle. At present, much attention is paid to the rapid development of microbial enzyme technology, and these enzymes are relatively more stable than enzymes derived from plants and animals.
P. Mukherjee and P. Roy in their article have purified and characterized the hydrocarbon dioxygenase enzyme of Stenotrophomonas maltophilia PM102, which has a broad substrate specificity. It was found that the presence of copper induces the activity of the enzyme to be 10.3 times greater, and NADH induces the increase of 14.96 times. The copper-enhanced monooxygenase activity and the Fourier Transform Infrared (FT-IR) characterization of biotransformation products from trichlorethylene satisfy the production of industrial and medically important chemicals and make bioremediation more attractive by improving the development of This technology.
C. Huynen et al. In their review article they discuss the importance of protein scaffolding to develop hybrid enzymes. The article discusses the use of class A beta-lactamases as versatile scaffolds for designing hybrid enzymes referred to as beta-lactamase hybrid proteins (BHPs), in which an external polypeptide, peptide, protein or fragment thereof is inserted into several suitable positions. The document further highlights how BHPs can be specifically designed to be developed as bifunctional proteins to produce and characterize otherwise difficult to express proteins, to determine the epitope of specific antibodies, to generate antibodies against non-immunogenic epitopes and to understand the structure / function relationship of Proteins. Hybrid proteins can be applied to produce difficult-to-express peptides / proteins / protein fragments, to map epitopes, to display antigens, and to study protein structure / function relationships. Among other applications, BHP could be a major player in biosensors and in affinity chromatography, drug detection and drug selection.
P. Manivasagan et al. In their paper they focus on the purification and characterization of the protease of Streptomyces sp. MAB18. The authors have optimized the conditions for protease overproduction using surface response methodology. They have also determined the molecular mass of the purified enzyme and the great activity and stability of the enzyme at different pH and temperatures. In addition, the authors confirmed that the protease has an antioxidant capacity. In industries, the protease derived from poultry residues will be useful as a protein or as an antioxidant.
The paper entitled "Trichoderma fungus glucosidases: an efficient cellulose machinery in biotechnological applications" is a detailed review of glucosidases that are members of the cellulose enzyme complex described by P. Tiwari et al. The authors focus especially on the glycosidases of the fungus Trichoderma, used mainly for the saccharification of the cellulosic biomass for the production of biofuels. They describe the family of enzymes, their classification, structural parameters, properties and studies in the levels of genomics and proteomics. In addition, by avoiding the low production of enzymes with hypersecretoric strains, they give an idea of the use of these strains for renewable energy sources as the production of bioethanol. They implicate the importance of fungal glucosidases that could be successful for the production of biofuels to meet the need in energy crisis.
A. Khoramnia et al. In his article discusses the application of yeast enzymes for the modification of medium chain fatty acids (MCFAs) for industrial purposes and antibacterial applications. The article focuses on the conceptualization, design and testing of the enzyme produced from a Malay strain of Geotrichum candidum. With the modification in the processing of fatty acids using a naturally derived enzyme, free lauric acid rich MCFAs can be obtained which can become a source of antibacterial use for Gram-positive () and Gram-negative () bacteria that are difficult microbes Because some of their strains become resistant to drugs. They also describe that the higher lipolysis by the specific enzyme strain is associated with the higher moisture content in the reaction environment in the hydrolysis of coconut oil.
M. A. Hassan et al. In his paper he discusses the isolation of Bacillus amyloliquefaciencs and B. subtilis from the soil and the production and characterization of keratinolytic protease. These bacteria were able to degrade the wool completely in 5 days and also produced the highest enzymatic activity. Characterization studies confirmed that the enzyme is stable over a wide range of pH and temperatures. In addition, they confirmed that keratinolytic proteases from isolated bacteria are stable in various organic solvents.
In this review article, S. C. B. Gopinath et al. They put different strategies to characterize the fungal lipases by their role in the industry and the medicine. The advantage of fungal lipases is conferred with their extracellular nature of production, thus reducing the complexities and high cost of operation compared to other bacterial enzymes. The authors provide several illustrations to show how lipolysis can be used and put strategies for the characterization of fungal lipases that are capable of degrading the fatty substances from different sources in order to highlight other applications. This review would contribute to the isolation and characterization of lipase from various fungal sources and the application of lipase to the medical and dairy industry and the degradation of the fatty substance from oil spills.
A. Knob et al. In their paper they focus on xylans and discuss the purification and characterization of a xylanase produced using the spent grain of the brewery as a substrate in their paper. This study is the first report since the characterization of xylanase was carried out by the use of such agroindustrial residues. In addition, the researchers also determined the molecular mass of purified xylanase, enzymatic activity and stability in various ranges of pH and temperature, optimum conditions of enzymatic production and the effect of some metal ions and inhibitors on xylanase activity. The authors concluded that the use of spent grain from the brewery for the production of xylanase not only decreased the amount of this waste, but also reduced the cost of producing xylanase as desired in biotechnological processes.
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