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KMID : 0617219910020010043
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Duksung Bulletin Phamaceutical Sciences
1991 Volume.2 No. 1 p.43 ~ p.58
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Studies on Purification and Characterzation of Chitinolytic Enzymes from Allium fistulosum L
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Abstract
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Chitin is major component of the outer shell of crustaceans(shrimp and crab) is the second most plentiful natural polymer next to cellulose. Its chemical structure is β-(1->4) linked poly N-acetyl-D-glucosamine. Recently, chitin derivatives and its oligosaccharides have the potential as the new drug (antitumor, antithrombotic, and antiatheroclerotic). The complete enzymatic hydrolysis of chitin to free N-acetyl-D-glucosamine is performed by chitinolytic system including β-N-acetylglucosaminidase (GlcNAcase) as well as chitinase.
It was found that the green onion(Allium fistulosum L.) showed both enzymatic activities. The purpose of the research was to purify and chracterize two kinds of enzyme above from the green onion. Protein fraction precipitated from ammonium sulfate was passed through the convention column chromatographic steps (gel-filtration and ion-exchange chromatography) and partially purified.
The specific activity of GlcNAcase was 8.60 units/mg and the purification was increased to 14-fold. The total recovery was correspondent to 6 ％. The specific activity of chitinase was 1.74 units/mg. The optimum pH of GlcNAcase was 5.0 and its optimum temperature was in the range of 50-55℃. The pH stability was 7.0 and temperature stability was 30℃. The maximum activity of chitinase was shown in 0.05M citrate buffer (pH 5.0). A partially purified chitinolytic enzyme from the 10og of green onion could make 38mg of N-acetylglucosamine in hydrolyzing 700mg of colloidal chitin.
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