To Study the Effect of pH on Lipase
Journal Title: International Journal of Research and Review - Year 2018, Vol 5, Issue 8
Abstract
Bacteriallipases are commercially more important mainly because of the ease of their cultivation and optimization to obtain higher yield. The industrial demand of new sources of lipases with different catalytic characteristics stimulated the isolation and selection of Bacillus subtilis. This study was designed to investigate physicochemical parameters for optimized lipase production. Microbial lipases catalyze both the hydrolysis and synthesis of long-chain acylglycerols. They are currently given much attention with the rapid development of enzyme technology. The characterization of these enzymes of paramount importance to establish the process conditions for subsequent application. To determine the optimum pH, we used the sodium citrate buffer pH 3, 3.6and 5.6 and sodium phosphate buffer at pH 7.3 and 8.Change in pH also alters an enzyme’s shape. Different enzymes work best at different pH values. The enzyme can continue locking with a substrate and continue its catalysts activity. If the pH is too high or too low it can change the shape of the enzyme. The most favourable pH value the point where the enzyme is most active is known as the optimum pH. Extremely high or low pH values generally result in complete loss of activity for most enzymes pH is also a factor in the stability of enzymes. As with activity for each enzyme, there is also a region of pH optimal stability.
Authors and Affiliations
Praveena Gupta
Keywords
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