• Journal of Microbiology and Biotechnology
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• 제31권3호
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• pp.464-474
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• 2021

Bacterial cytochrome P450 (CYP) enzymes are responsible for the hydroxylation of diverse endogenous substances with a heme molecule used as a cofactor. This study characterized two CYP154C3 proteins from Streptomyces sp. W2061 (CYP154C3-1) and Streptomyces sp. KCCM40643 (CYP154C3-2). The enzymatic activity assays of both CYPs conducted using heterologous redox partners' putidaredoxin and putidaredoxin reductase showed substrate flexibility with different steroids and exhibited interesting product formation patterns. The enzymatic characterization revealed good activity over a pH range of 7.0 to 7.8 and the optimal temperature range for activity was 30 to 37℃. The major product was the C16-hydroxylated product and the kinetic profiles and patterns of the generated hydroxylated products differed between the two enzymes. Both enzymes showed a higher affinity toward progesterone, with CYP154C3-1 demonstrating slightly higher activity than CYP154C3-2 for most of the substrates. Oxidizing agents (diacetoxyiodo) benzene (PIDA) and hydrogen peroxide (H2O2) were also utilized to actively support the redox reactions, with optimum conversion achieved at concentrations of 3 mM and 65 mM, respectively. The oxidizing agents affected the product distribution, influencing the type and selectivity of the CYP-catalyzed reaction. Additionally, CYP154C3s also catalyzed the C-C bond cleavage of steroids. Therefore, CYP154C3s may be a good candidate for the production of modified steroids for various biological uses.

• 공업화학
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• 제27권6호
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• pp.659-663
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• 2016

알켄 또는 알킨의 산화 반응이 루테늄 지르코니아 불균일 촉매에 의해 매우 선택적이며 효율적으로 전환되었다. 절단반응을 통해, C-C 이중 결합은 알데히드 관능기로, 삼중 결합은 다이케톤 또는 카르복시산으로 전환되었는데, 다양한 기질들이 $30^{\circ}C$에서 $PhI(OAc)_2$ 산화제와 dichloromethane 및 물(각각 5 mL와 0.5 mL)의 혼합 용매 조건에서 반응이 수행되었다. 사용된 촉매 $Ru(OH)_x/ZrO_2$는 이 절단 반응에 대해 기존의 다른 루테늄 기반 불균일 또는 균일 촉매들보다 더 좋은 활성과 선택성을 보였다. 반응이 진행되는 동안, 제조된 촉매의 기계적인 물성은 안정적이었고, 금속의 침출은 전혀 보이지 않았다. 불포화된 탄화수소들의 산화적 절단에 대해, 합성된 촉매는 여러 번 재사용해도 그 촉매의 성능을 그대로 유지하였다.