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Amylases are widely distributed in various animals, plants, and microorganisms. The
enzyme is one of the best known protein which catalyzes the hydrolysis of starch to produce
glucose, maltose, and maltooligosaccharide. it has been used in textile industry, baking
industry, and so on. Today, it is used in development of new materials and low calorie
products. The objectives of this experiment are purification and analysis of cloned amylase
from Pseudomonas sp. to E. coli. The amylase expressed and purified from recombinant
Escherichia coli was immunoblotted to rabbit antiserum that was raised from an amylase, 50
kDa, purified from Pseudomonas sp. Thus, these two proteins were confirmed same enzyme.
The expressed protein showed amylase activity. The amylase purified from Escherichia coli
harboring the amylase gene showed same enzymatic action as extracellular amylase from
Pseudomonas sp. That is, the amylase produced maltose and maltotriose by starch hydrolysis.