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i. Neutral sphingomyelinase 2 converts sphingomyelin into ceramide and phosphocholine. Assume its Vmax is 35μMmin−1. When you provide 3×10−5M of sphingomyelin, you observe an initial velocity of 6.0μMmin−1. Calculate the KM for this reaction, rounding to 3 significant figures. Explain the changes in values of Vmax and KM, when 50μM of an uncompetitive inhibitor is added into the reaction mixture. ii. Table 1 illustrates the kinetic data for the esterification of valeric acid and pentanol to pentyl valerate by the enzyme Candida rugosa lipase in the absence of an inhibitor. The following supplementary data were obtained when the reaction occurred in the presence of p hydroxybenzoic acid, PBHA. lot an appropriate graph and relate whether PBHA is an inhibitor for this reaction. If so, propose the pe of inhibitor and give reasons. b) Define the term immobilized enzymes as described by the European Federation of Biotechnology. Explain the five (5) techniques to prepare immobilized enzymes. c) Briefly explain the four (4) benefits of the use of ion-exchange chromatography to purify a mixture of enzyme proteins.