Factors Affecting the Inactivation of Naringinase Immobilized on Chitin during Debittering of Fruit Juice
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概要
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Naringinase from Aspergillus niger was immobilized on chitin with glutaradehyde and sodium borohydride. The immobilized enzyme was inactivated when it was used for the debittering of natural grapefruit juice or a simulated juice, so a series of inhibition studies were performed. Citric acid inhibited native naringinase only at pH 3,but not at pH 4.5. However, it inhibited the immobilized naringinase at both pH 3 and 4.5. Glucose, fructose, and rhamnose were all inhibitors for both native and immobilized naringinases at pH 3 and 4.5. The Lineweaver-Burk plots for the inhibition studies of glucose and fructose showed that these sugars were non-competitive inhibitors. This might explain the inactivation of the immobilized enzyme during the debittering of grapefruit juice or a simulated juice.
- 公益社団法人日本生物工学会の論文
- 1984-06-25
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