Abstract
Purified preparations of enzymes are requisite for their application as well as decoding their basic characteristics and mechanisms. The chapter presents the purification protocols employed to purify a range of industrially useful enzymes mainly sourced from extremophiles (solvent-tolerant and halophilic microbes). Single-step Phenyl Sepharose 6 Fast Flow hydrophobic interaction chromatography for extremophilic enzymes and affinity precipitation by alginate for carbohydrate-active enzymes were adopted by us. A single-step purification protocol is economical, and better enzyme recovery is obtained. Pseudomonas aeruginosa PseA, our laboratory isolate, turned out to be a versatile solvent-tolerant microbe. Three potential enzymes, protease, lipase, and aminopeptidase, were produced, purified, and characterized from it and was potentiated for use in nonaqueous enzymology. Proteases, lipase, and amylase from halophiles were also purified and characterized. Halophilic enzymes are industrially desirable as, in addition to salt-stability other polyextremophilic properties are found in these enzymes. The experiences gained by purifying these enzymes will come in handy for developing successful purification procedures for other proteins.
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