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RISS 인기검색어
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- 저자 : 김태승 ( Nam Kee Rhee (검색결과 2 건)
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이남기,연석흠,김태승,Rhee, Nam-Kee,Youn, Suk-Heum,Kim, Tae-Seung 생화학분자생물학회 1993 한국생화학회지 Vol.26 No.6
다양한 Trichoderma species, 즉 효소 I(Meicelase from T. sp; Meiji Co., Japan), 효소 II(Meicelase TP60 from T. viride; Meiji Co., Japan), 효소 II1(cellulase from T. viride; A.B.M. Chemicals Ltd., England), and 효소 IV(cellulase from T. viride; Sigma Co., U.S.A.)의 cellulase를 사용하여 결정성 셀룰로오스인 Avicel PH-101의 가수분해과정을 속도론적으로 연구하였다. 가수분해반응은 초기가수분해과정(initial hydrolysis process)과 후기가수분해과정(later hydrolysis process)으로 구분되었다. 각 효소반응과정의 초기반응속도는 효소농도에 따른 Michaelis-Menten type의 속도식에 따라 진행됨을 알 수 있였다. 이 속도식으로부터 각 효소반응에 대한 최대반응속도 $(V_{max})$'와 half-saturated constant$(K_a)$값을 구하였다. 이들 결과로부터 초기반응과정의 반응속도가 비결정성 부분에 대한 각 효소의 반응성의 차이에 의존하는 반면, 후기반응과정은 기질의 결정성에 의존함을 알 수 있었다. 한편 큰 $K_a$값을 갖는 효소반응은 작은 흡착분배계수$(K_p)$의 값을 보여 주었다. 따라서 이러한 불균일계 반응에서 효소-기질착물의 농도와 흡착반응에서의 효소흡착량이 서로 비례하며, 결정성 셀룰로오스의 가수분해반응속도 역시 효소의 흡착세기에 의존함을 알았다. Various commercial cellulases from Trichoderma species such as enzyme I (Meicelase from T. sp; Meiji Co., Japan), enzyme II (Meicelase TP60 from T. viride; Co., Japan), enzyme III (cellulase from T. viride; A.B.M. Chemicals, England), and enzyme IV (cellulase from T. viride; Sigma Co., U.S.A.) were used for the enzymatic hydrolysis of microcrystalline celluose (Avicel PH-101). The hydrolysis process was divided into the initial and the later hydrolysis process. The results of these reactions were explained by kinetic equation of the Michaelis-Menten type with respect to enzyme concentration. From that equation, maximum velosity $(V_{max})$' and half-saturated constant $(K_a)$ were obtained for enzymes I-IV, respectively. For the initial process, the values of $V_{max}$' are 1.00, 0.91, 0.83, and 0.29, and $K_a$ values are 0.17, 0.12, 0.51, and 0.640, respectively. For the later process, the values of $V_{max}$' are 0.24, 0.23, 0.20, and 0.25, $K_a$ values are 0.15, 0.13, 0.17, and 1.10, respectively. All $V_{max}$' values for the later process showed similar values compared with that for the initial process. From this result, it could be suggested that the rate of the initial hydrolysis depends on each enzyme activity with the amorphous part of cellulose, but that of the later hydrolysis on the crystallinity of cellulose. And the smaller $K_a$ values show the larger adsorption partition coefficient $(K_p)$. In a view point of the adsorption of enzyme to substrate, it could be concluded that both the rate of hydrolysis and the extent of enzyme-substrate complex formation are proportional to the amount of enzyme adsorbed.
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이남기,연석흠,김태승 ( Nam Kee Rhee,Suk Heum Youn,Tae Seung Kim ) 생화학분자생물학회 1993 BMB Reports Vol.26 No.6
Various commercial cellulases from Trichoderma species such as enzyme I (Meicelase from T. sp; Meiji Co., Japan), enzyme II (Meicelase TP60 from T. viride; Co., Japan), enzyme III (cellulase from T. viride; A.B.M. Chemicals, England), and enzyme IV (cellulase from T. viride; Sigma Co., U.S.A.) were used for the enzymatic hydrolysis of microcrystalline celluose (Avicel PH-101). The hydrolysis process was divided into the initial and the later hydrolysis process. The results of these reactions were explained by kinetic equation of the Michaelis-Menten type with respect to enzyme concentration. From that equation, maximum velosity (V_(max)`) and half-saturated constant (K_a) were obtained for enzymes I-IV, respectively. For the initial process, the values of V_(max)` are 1.00, 0.91, 0.83, and 0.29, and K_a values are 0.17, 0.12, 0.51, and 0.640, respectively. For the later process, the values of V_(max)` are 0.24, 0.23, 0.20, and 0.25, K_a values are 0.15, 0.13, 0.17, and 1.10, respectively. All V_(max)` values for the later process showed similar values compared with that for the initial process. From this result, it could be suggested that the rate of the initial hydrolysis depends on each enzyme activity with the amorphous part of cellulose, but that of the later hydrolysis on the crystallinity of cellulose. And the smaller K_a values show the larger adsorption partition coefficient (K_p). In a view point of the adsorption of enzyme to substrate, it could be con-cluded that both the rate of hydrolysis and the extent of enzyme-substrate complex formation are proportional to the amount of enzyme adsorbed.
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