• Nuclear Engineering and Technology
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• v.51 no.8
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• pp.1978-1982
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• 2019

The paper presents the electrical performance measurements of a prototype nuclear battery and two types of betavoltaic cells. The electrical performance was assessed by measuring current-voltage properties (I-V) and determining the short-circuit current and the open-circuit voltage. With ⁶³Ni as an irradiation source, the open-circuit voltage and the short-circuit current were determined as 1 V and 64 nA, respectively. The prototype consisted of 10 betavoltaic cells that were prepared using radioactive ⁶³Ni. Electroplating of the radioactive ⁶³Ni on an ohmic contact (Ti-Ni) was carried out at a current density of 20 mA/㎠. Two types of betavoltaic cells were studied: with an external ⁶³Ni source and a ⁶³Ni-covered source. Under irradiation of the ⁶³Ni source with an activity of 10 mCi, the open-circuit voltage V_oc of the fabricated cells reached 151 mV and 109 mV; the short-circuit current density J_sc was measured to be 72.9 nA/cm2 and 64.6 nA/㎠, respectively. The betavoltaic cells had the fill factor of 55% and 50%, respectively.

• Monthly Duck's Village
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• s.74
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• pp.63-63
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• 2009

• Monthly Duck's Village
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• s.183
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• pp.63-63
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• 2018

• Monthly Duck's Village
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• s.57
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• pp.63-63
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• 2008

• Nuclear industry
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• v.5 no.3 s.25
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• pp.63-63
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• 1985

• Mycobiology
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• v.29 no.1
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• pp.63-63
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• 2001

• Proceedings of the Korean Society of Plant Pathology Conference
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• 1999.10a
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• pp.63.2-63
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• 1999

• 한국전기화학회:학술대회논문집
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• 2004.04a
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• pp.63-63
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• 2004

• Kyungpook Mathematical Journal
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• v.63 no.1
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• pp.11-13
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• 2023

We give a new proof for the full form of Hilbert's Nullstellensatz based on on integral extension and Noether's Normalization Lemma.

• Journal of Microbiology and Biotechnology
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• v.21 no.11
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• pp.1116-1122
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• 2011

In this study, site-directed mutagenesis was performed on the ${\beta}$-agarase AgaA gene from Zobellia galactanivorans to improve its catalytic activity and thermostability. The activities of three mutant enzymes, S63K, C253I, and S63K-C253I, were 126% (1,757.78 U/mg), 2.4% (33.47 U/mg), and 0.57% (8.01 U/mg), respectively, relative to the wild-type ${\beta}$-agarase AgaA (1,392.61 U/mg) at $40^{\circ}C$. The stability of the mutant S63K enzyme was 125% of the wild-type up to $45^{\circ}C$, where agar is in a sol state. The mutant S63K enzyme produced 166%, 257%, and 220% more neoagarohexaose, and 230%, 427%, and 350% more neoagarotetraose than the wild-type in sol, gel, and nonmelted powder agar, respectively, at $45^{\circ}C$ over 24 h. The mutant S63K enzyme produced 50% more neoagarooligosaccharides from agar than the wild-type ${\beta}$-agarase AgaA from agarose under the same conditions. Thus, mutant S63K ${\beta}$-agarase AgaA may be useful for the production of functional neoagarooligosaccharides.