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자료유형
학술저널
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한국원예학회 HORTICULTURE ENVIRONMENT and BIOTECHNOLOGY HORTICULTURE ENVIRONMENT and BIOTECHNOLOGY Vol.48 No.6
발행연도
2007.12
수록면
349 - 353 (5page)

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Polyphenol oxidase (PPO) caused browning is a major cause of undesirable flavors and nutritional losses in peeled garlic. To screen for antibrowning compounds, PPO was purified from garlic extract by Sephadex G-100 column chromatography. The purified PPO revealed homogeneity of a single protein band on 12% SDS-PAGE. Its molecular weight was estimated to be 30 kDa by SDS-PAGE and confirmed by active staining. Its pH and temperature optima were pH 6.0 and 35℃, respectively. The PPO activity was a little inhibited by Na? and Fe?? ions, whereas the enzyme activity was increased by Ca??, Mn??, Zn??, and Hg?? ions. It was found by chemical modification reaction that serine residue is involved in active site of PPO.β-glucosidase inhibitor (β-GI) isolated from Bacillus lentimorbus B-6 was found to be an inhibitor for the PPO purified from garlic extract. The kinetic analysis showed that the inhibition of β-GI on the PPO is competitive and reversible. IC?? and the inhibition constant (K<SUB>I</SUB>) ofβ-GI against PPO were determined to be 0.85 mg/ml and 75μg/ml, respectively.

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Abstract
Introduction
Materials and Methods
Results and Discussion
Literature Cited

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