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KMID : 0379119830110030109
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Korean Journal of Mycology
1983 Volume.11 No. 3 p.109 ~ p.114
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Studies on the β-Galactosidase Activity of Whole Cell Aspergillus phoenicis
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Abstract
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β-Galactosidase activity of Aspergillus phoenicis was studied using ONPG and lactose as substrate. It increased monotonically during the exponential growth phase and dropped rapidly at the beginning of the stationary one. It exhibited high tolerable temperature and acidic optimal pH which provides certain advantages from the industrial view point. Enzyme of β-galactosidase had more subsrate affinity for ONPG than for lactose and its apparent maximum activity was also higher with the former as substrate. Activity of this enzyme depended upon the conditions of immobilization. Optimum crosslinking reaction was occurred at pH 7.2 and 0.35 vol. % of glutaraldehyde concentration.
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