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Essay / Studying the Effect of pH on Lipase Enzyme new sources of lipases with different catalytic characteristics is stimulated the isolation and selection of Bacillus subtilis. This study was designed to investigate the physicochemical parameters for optimized lipase production. Microbial lipases catalyze both the hydrolysis and synthesis of long-chain acylglycerols. They are currently being paid much attention with the rapid development of enzyme technology. Say no to plagiarism. Get a tailor-made essay on “Why violent video games should not be banned”? Get the original essay Characterization of these enzymes is of paramount importance to establish processing conditions for further application. To determine the optimal pH, we used sodium citrate buffer pH 3, 3.6 and 5.6 and sodium phosphate buffer pH 7.3 and 8. Changes in pH also alter the shape of an enzyme . Different enzymes work better at different pH values. The enzyme can continue to latch onto a substrate and continue its catalytic activity. If the pH is too high or too low, the shape of the enzyme can be changed. The most favorable pH value, at the point where the enzyme is most active, is known as the optimum pH. Extremely high or low pH values generally result in a complete loss of activity for most enzymes. pH is also a factor in enzyme stability. As with the activity for each enzyme, there is also a region of optimal pH stability.Keywords: Lipase, enzymes, Bacillus subtilis, optimal, pH.IntroductionLipases (triacylglycerol acyl hydrolases, EC 3.1.1.3) are a important group of enzymes mainly due to the large number of industrial applications. From an industrial point of view, lipase enzymes are considered very important due to their greater potential for large-scale production. Isolation of lipases by Bacillus subtills from different soil samples namely Ruchi Soya Oil Mill, Ghatabillod, Bajrang Soya Mill, Ghatabillod, Madhya Pradesh and dairy companies along with characterization of bacteria determines the maximum producer of lipase by qualitative and quantitative means, have been studied [1]. . Lipases are widely present in animals, plants and microorganisms, especially those derived from bacteria, and are more stable than others. Many microorganisms are known to be good producers of extracellular lipases [2]. Studies on the production of extracellular lipases with Bacillus have shown variations between different strains[3]. Lipases are widely present in bacteria, yeasts and fungi [4]. Bacterial lipases are commercially more important mainly due to the ease of their cultivation and optimization to obtain higher yield. Microbial lipases are in high demand due to their reaction specificity, stereospecificity and lower energy consumption than conventional methods [5]. Lipase with high enzymatic activity can replace the traditional catalyst in biodiesel processing, as this enzyme replaces chemicals in an otherwise energy-intensive process. [6].Lipase applications are also affected by temperature and pH stability. The enzyme is used as a catalyst for the production of different products used in industry..
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