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KMID : 0366119760040040131
Korean Journal of Applied Microbiology & Bioengineering
1976 Volume.4 No. 4 p.131 ~ p.137
Studies on the Hesperidinase of Aspergillus niger S-1

Abstract
Aspergillus niger S-1 was proved to be a good hesperidinase producer which have been selected for naringinase utilization. Enzyme of this strain had good characteristics and purified relative high degree with good recovery by ammonium sulfate or aceton treatment. Results obtained were summarized as follows
(1) The enzyme was most active at 60¡É, when the reaction was performed in the pH 4.0 for 30min. Optimum pH for enzyme activity was 5.0 and activity was retained 78% at pH value 3.5.
(2) Hesperidinase activity retained 95% of its full activity after treatment at 60¡É for 30min at pH value 4.0., 70% at 70¡É and 65% at 80¡É. Most stable pH of this enzyme was showed 5.0 after treatment for 24hr at 4¡É
(3) Only Magnesium ion activated enzyme reaction, while other metallic ions, Cu^(++), Mn^(++), pb^(++), Mo^(++), Ag^(++), Hg^(++) inhibited.
(4) Eleven fold purification with 35% recovery was obtained in the case of 60% aceton treatment and 10-fold purification with 5.6% recovery was showed with 40% aceton comparing to the crude extract Enzyme.
(5) Crude enzyme precipitated with 0.4-0.6 saturated ammonium sulfate contained 13% of the original enzyme activity with 48-fold increase in specific activity and enzyme has been purified 25 fold with a yield-19% by 0.6-0.8 saturation.
(6) Hesperidinase formation was noticeably increased by addition of small amount of orange-peel extraction on the wheat bran medium.
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