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KMID : 1007519940030010039
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Food Science and Biotechnology
1994 Volume.3 No. 1 p.39 ~ p.42
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Purification and Characterization of Aminopeptidase from Lactobacillus casei AHV 1055
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Jung, Heon Woong
Jang, Hae Dong/Lee, Hyong Joo
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Abstract
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An intracellular aminopeptidase was purified from Lactobacillus casei AHU by ammonium sulfate fractionation, Sephades G-100 gel filtration, DEAE-cellulose chromatography and rechromatography on DEAE-cellulose. The purified aminopeptidase was migrated as a single component in SDS-poly-acrylamide gel electrophoresis and consisted of a single polypeptide chain with a molecular weight of 63,000. The optimum pH and temperature of purified aminopeptidase were pH 7.0 and 40℃, respectively.
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