• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1977.10a
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• pp.198.1-198
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• 1977

Aspergillus nidulans가 생산하는 naringinase를 acrylamide gel을 이용한 entrapping moth길에 의하여 고정화하여 그 고정화 효소의 물리, 화학적인 성질에 대하여 검토한 결과 다음과 같았다. 1) Acrylamide의 농도는 10% 일때 enzyme activity가 가장 좋았다. 2) Immobilized enzyme의 최적온도는 $50^{\circ}C로서$ 유리효소의 경우보다 $10^{\circ}C정도$ 증가 하였고 최적 pH는 유리효소의 경우와 마찬가지로 pH 40이었다.(중략)

• Food Science and Preservation
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• v.11 no.1
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• pp.38-41
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• 2004

To obtain basic data for utilizing Yuzu(Citrus junos) as row materials to industrial products, enzyme treatments conditions for removing bitter substances was investigated. The amount of nuringin and hesperidin weve 61.94 and 9.98 mg％ in Yuzu juice. When 3％ Amorepacific enzyme and Japanese naringinase were treated with the juice for 120 minutes, naringin and hesperidin were decreased to 6.85 and 1.11 mg％ ; 8.43 and 0.06 mg％, respectively. The changes in Hunter color value of the juice were negligible by enzyme treatments. However, the redness was increased and lightness was decreased by the enzymes. When Yuzu-juice was treated with the enzymes, sensory scores were increased. The optimum amount of Amorepacific for reducing bitter taste was determined to 3％.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1976.10a
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• pp.190.4-190
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• 1976

Naringinase 생산 균주로 분리 선정된 Asp. niger S-1은 동시에 Hesperidinase도 강력히 생산함이 확인 되었으며 이 균의 효소학적 특성을 요약하여 1. 최적 반응 온도는 $60^{\circ}C이며$ $80^{\circ}C에서$ 30분 열처리 하여도 65%을 활성을 가지며 pH 5.0부위에서 최적반응과 안정성을 보였으며 Mg(이온)은 반응을 활성화 하였다. 2. Aceton을 60% 처리하여 조효소를 11배 정제하였으며 35%가 회수되었고 유안 0.4-0.6 포화로 48배 정제되었으며 13%가 회수되었다.

• Microbiology and Biotechnology Letters
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• v.4 no.4
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• pp.131-137
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• 1976

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$^{\circ}C$, 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$^{\circ}C$ for 30min at pH value 4.0., 70％ at 70$^{\circ}C$ and 65％ at 80$^{\circ}C$. Most stable pH of this enzyme was showed 5.0 after treatment for 24hr at 4$^{\circ}C$ (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 13f6 of the original enzyme activity with 48-fold increase in specific activity and enzyme has been purified 25 fold with a yield 19％ by 0.6-5.8 saturation. (6) Hesperidinase formation was noticeably increased by addition of small amount of orange-peel extraction on the wheat bran medium.