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      • Pleurotus ostreatus의 액체 종균 생산에 관한 연구

        강태수,천병익 江原大學校 産業技術硏究所 1988 産業技術硏究 Vol.8 No.-

        For the improvement of productivity of Pleurotus ostreatus, the production of liquid spawn was studied. The highest liquid spawn production was obtained after shaking culture for 4 days in the culture medium containing 5%(W/V) wheat flour, 0.2%(W/V) yeast extract, 0.1%(W/V)KNO3 0.05%(W/V)MgSO47H2O, 0.05%(W/V)KH2PO4. The optimum pH and temperature was 7.0 and 30℃. The period required to complete the mycelial growth after spawning were 28, 22, 10 and 9 days, respectively, when the 2%(V/V) of solid spawn and 2%(V/V), 5%(V/V) and 10%(V/V) of liquid spawn were inoculated. The days required from spawning to fruiting bodies were 38, 34, 28 and 27 days.

      • Zymomonas mobilis에 의한 알코올 발효 1. 발효 환경이 생육에 미치는 영향

        박무영,천병익 江原大學校 産業技術硏究所] 1983 産業技術硏究 Vol.3 No.-

        The effect of various environmental conditions on the growth kinetics of Zymomonas mobilis were studied and the kinetic parameters were evaluated. The value of ㎛ was 0.45hr?? and Ks was 0.23 g/L. Inhibition of growth at high glucose concentration was found to follow the threshold substrate inhibition. Threshold substrate concentration was 102 g/L and substrate inhibition constant was 196 g/L. The effects of yeast extract concentrations were found to follow the Monod equation. ㎛ value was 0.45 hr?? and Ks was 0.3 g/L at 20 g/L of glucose and 0.24 hr?? and 0.24 g/L respectively at 200 g/L of glucose. The optimum temperature was found to be 35℃ and the activation energy of growth was 7.7 Kcal/mole below 35℃ and -29 Kcal/mole above 35℃.

      • SCOPUSKCI등재

        컴퓨터 시뮬레이션에 의한 레토르트미반의 최적고온 살균조건

        이신영,천병익,이상규,Lee, Shin-Young,Chun, Byong-Ik,Lee, Sang-Kyu 한국식품과학회 1985 한국식품과학회지 Vol.17 No.3

        두께가 서로 다른(5${\sim}$24mm) 레토르트 미반에 대하여 여러온도(110-$150^{\circ}C$)에서 최적품질보유가 가능한 고온살균조건을 컴퓨터 simulation에 의하여 구하였다. 최적조건은 12D의 미생물학적 안전성을 유지할 때 최소의 c-값과 최대의 thiamine retention을 갖는 건에 의하여 선정하였다. 계산결과는 고온일수록 시료두께의 영향이 매우 중요함을 보이면서 미반고온살균의 우수한 음질보유는 두께 10mm이하에서 나타난다. Optimal quality retentions of cooked rice packed in retort pouch were simulated by computer using various thicknesses of retort pouch (5 to 24mm) and process temperatures (110 to $150^{\circ}C$). Optimal conditions were chosen by the minimal c-values and maximal thiamine retention when good bacteriological lethality (12D processing) was obtained. From the results of calculations, it were shown that the better quality retentions of high tharmal processing can be obtained below pouch thickness of l0mm and that the thickness of pouch is critical factor at higher processing temperature.

      • SCOPUSKCI등재

        보리전분 수용액계의 리올로지적 연구

        이신영,최준복,천병익,Lee, Shin-Young,Choi, Jun-Bok,Chun, Byong-Ik 한국식품과학회 1985 한국식품과학회지 Vol.17 No.3

        쌀보리와 겉보리전분의 희석 및 농후호화용액에 대한 리올로지적 성질을 여러 점도계를 사용하여 연구하였다. 희석전분액(0.05${\sim}$0.3%)의 점도특성은 Huggins식에 따르는 고유점도 및 해수에 의하여 설명할 수 있었으며, 농후전분용액(1${\sim}$5%)의 리올로지적 거동은 농도의 증가에 따라 시간의존성과 의가소성의 성질이 현저히 강해지는 특징을 나타내었다. 지수법칙을 적용하여 구한 점조도지수 값은 지수함수식에 따르는 농도 및 은도의존성을 나타내었다. 한편 이들 결과는 리올로지적 성질이 품종차이에 따라 크게 달라지는 경향을 보였다. 쌀보리전분은 겉보리전분보다 더 큰 고유점도값을 나타내었으며, 틱소트로픽성질이 더 강한 것으로 나타난다. 아울러 점조도지수 값의 농도 및 온도의존성도 더 높은 경향이었다. 그러나 보리전분은 다른 전분에 비하여 비교적 낮은 농도의존성과 높은 온도의존성을 갖는 특징을 보였다. The rheological studies on dilute and concentrate solutions of naked and covered barley starches were carried out with various viscosimeters. The rheology of dilute solutions (0.05-0.3%) were characterized by intrinsic viscosity and related parameter according to Huggins equation. Also, the rheology of the solutions of higher concentrations (1-5%) were characterized by time dependent characteristics and pseudoplastic behaviors. The values of consistency index according to the power equation were exponen tially dependent upon concentration and temperature. The results showed that the rheological properties could differ greatly due to difference in varieties. The naked barley starch exhibited higher intrinsic viscosity, more thixotropic behavior and more dependence of consistency index on concentration and temperature than the covered barley starch.

      • Studies on Ribulose-1, 5-Bisphosphate Carboxylase from Acetate Requiring Mutants of Chlamydomonas reinhardtii

        홍순주,김영명,이진하,천병익,Hong, Sun-Joo,Kim, Young-Myeong,Lee, Jin-Ha,Cheon, Byoung-Ik 생화학분자생물학회 1984 한국생화학회지 Vol.17 No.3

        Chlamydomonas reinhardtii에 N-methyl-N-nitroso-N-nitrosoguanidine을 처리하여 acetate 요구성 변이주, KX8215와 KX8261을 얻었고 여기에서 ribulose-1, 5-bisphosphate carboxylase를 분리하여 그 특성을 연구하였다. 2가 금속이온 $Mg^{2+}$, $Ni^{2+}$, $Co^{2+}$ 등은 효소 활성을 증가시켰고 할로겐족 음이온 $Cl^-$, $I^-$, $Br^-$ 등은 효소 활성을 저해하였으나 $Cu^{2+}$는 활성에 거의 영향을 주지 않았다. 또한 변이주 효소의 이온 영향, 최적 pH 그리고 효소 단백질의 함량 등은 야생종의 경우와 별 차이가 없었다. 변이주 효소의 최적온도는 $35^{\circ}C$로 야생종 효소의 $25^{\circ}C$ 보다 $10^{\circ}C$높았다. 중요한 점은 변이주 효소의 고유 활성도가 야생종 효소보다 현저하게 낮아진데 반해 변이주 효소의 Km(RuBP) 와 Km($Co_2$) 값은 야생종 효소보다 상당히 크게 나타난 것인데 이는 변이의 결과로 효소에 대한 RuBP와 $Co_2$의 친화력이 감소된 때문이라고 생각한다. 이상의 결과는 변이체 효소의 큰 subunit의 구조유전자에 변화가 일어났고 따라서 이 변이의 유전은 non-Mendelian이라는 추리를 가능케 한다. Ribulose-1, 5-bisphosphate carboxylase isolated from acetate requiring mutants, KX8215 and KX8261, of Chlamydomonas reinhardtii which were obtained by N-methyl-N-nitroso-N-nitrosoguanidine treatment have been characterized. Divalent metal cations, $Mg^{2+}$, $Ni^{2+}$, and $Co^{2+}$ appeared to enchance the enzyme activity whereas halogen anions, $Cl^-$, $I^-$, and $Br^-$ inhibited the enzyme activity. No difference between the mutant enzymes and that of the wild type has been detected in regards of ion effects, pH requirement, and the level of enzyme protein. Optimum temperature of the enzymes from both mutants were found to be higher at $35^{\circ}C$ than at $25^{\circ}C$ of the wild type enzyme. The specific activities of the mutant enzymes were remarkably lower than that of the wild type enzyme whereas Km (RuBP) and Km ($Co_2$) values of the former were significantly higher than those of the later, indicating that the affinities of the enzyme for RuBP and/or $Co_2$ are reduced as a result of the mutation. These results seem to support the previous indication that the lowered activities of the mutant enzymes would be due to the alteration in a structural gene for the large subunit in the enzymes and thus the inheritance of the mutation is non-Mendelian.

      • SCIESCOPUSKCI등재

        Chlamydomonas reinhardtii 변이체의 Ribulose - 1 , 5 - Bisphosphate carboxylase 에 관한 연구

        홍순주,김영명,이진하,천병익 ( Sun Joo Hong,Young Myeong Kim,Jin Ha Lee,Byoung Ik Cheon ) 생화학분자생물학회 1984 BMB Reports Vol.17 No.2

        Ribulose-1, 5-bisphosphate carboxylase isolated from acetate requiring mutants, KX8215 and KX8261, of Chlamydomonas reinhardtii which were obtained by N-methyl-N-nitrosoN-nitrosoguanidine treatment have been characterized. Divalent metal cations, Mg^(2+), Ni^(2+), and Co^(2+) appeared to enchance the enzyme activity whereas halogen anions, Cl^-, I^-, and Br inhibited the enzyme activity. No difference between the mutant enzymes and that of the wild type has been detected in regards of ion effects, pH requirement, and the level of enzyme protein. Optimum temperature of the enzymes from both mutants were found to be higher at 35℃ than at 25℃ of the wild type enzyme. The specific activities of the mutant enzymes were remarkably lower than that of the wild type enzyme whereas Km(RuBP) and Km (CO₂) values of the former were significantly higher than those of the later, indicating that the affinities of the enzyme for RuBP and/or CO₂ are reduced as a result of the mutation. These results seem to support the previous indication that the lowered activities of the mutant enzymes would be due to the alteration in a structural gene for the large subunit in the enzymes and thus the inheritance of the mutation is non-Mendelian.

      • SCOPUSKCI등재

        식물생약의 베타-갈락토시데이스 저해활성 검색

        한용남(Y. N. Han),이근억(K. E. Lee),최국지(K. C. Choi),천병익(B. I. Chun) 한국생약학회 1981 생약학회지 Vol.12 No.1

        세포표면이나 생체막에 존재하는 복합당질은, 각종 면역현상, 염증, 세포융합, 보체결합, 암화, 암전이, 바이러스 감염 등의 여러 현상에 중요한 역할을 하고 있으며, 이러한 복합당질을 가수분해하는 효소가 동물의 뇌, 간의 리소즘, 마크로파지, 세균 등에서 분리되어 그 성상이 알려지고 있다. 이러한 당 가수분해 효소의 저해제에 관한 연구를 목적으로, 본 연구에서는 우선 β-galactosidase를 선정하여 생약 150여종을 대상으로 저해 활성을 검색하였다.

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