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• W2051265686 abstract "Bacillus amyloliquefaciens CH51은 분자량 27 kDa 크기의 subtilisin 타입의 혈전용해능을 지니는 단백질분해효소인 AprE51을 생산하였다. 이전연구에서 더 우수한 혈전용해 활성을 갖는 AprE51-6이 세포외 돌연변이법으로 생산되었으며, 본 연구에서는 이 개선된 효소인 AprE51-6의 열안정성을 증진시킬 목적으로 B. subtilis subtilisin E의 아미노산과의 상동성 분석을 통하여 두 아미노산인 Gly-166과 Asn-218이 치환되었다. 그 결과 G166R과 N218S 돌연변이체는 혈전용해능을 보이는 용해능 배지에서 원 효소보다 각각 1.8배와 4.5배 높은 혈전용해능을 보였다. 정제된 두 돌연변이효소인 AprE51-7과 AprE51-8는 원효소인 AprE51-6에 비하여 1.9 그리고 2.5배 높은 <TEX>$k_{cat}$</TEX>값을 나타내었고, 2.1과 1.9배 낮은 기질친화력을 나타내는 <TEX>$K_m$</TEX>값을 보여주었다. 특히 AprE51-8는 나토키나아제에 비하여 알칼리 pH 영역에서 높은활성을 유지하였고, <TEX>$60^{circ}C$</TEX>에서 더 우수한 열안정성을 보여주었다. 열안정성의 정도를 나타내는 척도인 반감기 값에서도 AprE51-7과 AprE51-8는 <TEX>$50^{circ}C$</TEX>에서 21.5분과 27.3분으로 기존의 AprE51보다 2배 그리고 2.6배 더 긴 반감기를 보였다. AprE51 from Bacillus amyloliquefaciens CH51 is a 27 kDa subtilisin-like protease with fibrinolytic activity. AprE51-6 showing increased catalytic activity was produced previously. To enhance the thermostability of AprE51-6, 2 residues, Gly-166 and Asn-218 based on B. subtilis subtilisin E were mutated by site-directed mutagenesis. The results of the mutational analysis showed that substitution of arginine for Gly-166 (AprE51-7) increased the fibrinolytic activity 1.8-fold. An N218S mutant (AprE51-8) also increased the fibrinolytic activity up to 4.5-fold in a fibrin plate assay. Purified AprE51-7 and AprE51-8 mutants had a 1.9- and a 2.5-fold higher <TEX>$k_{cat}$</TEX>, respectively, and a 2.1-1.9-fold lower <TEX>$K_m$</TEX>, respectively. This resulted in a 3.8- and a 4.7-fold increase in catalytic efficiency (<TEX>$k_{cat}/K_m$</TEX>), respectively, relative to that of wild-type AprE51. AprE51-8 had a broader pH range than AprE51-6 and nattokinase, especially at an alkaline pH value. In addition, AprE51-8 showed higher thermostability than AprE51-6 at <TEX>$60^{circ}C$</TEX>. The half-lives of AprE51-7 and AprE51-8 at <TEX>$50^{circ}C$</TEX> were 21.5 and 27.3 min, respectively, which are 2.0 and 2.6 times longer, respectively, than that of the wild-type AprE51." @default.
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• W2051265686 date "2013-01-30" @default.
• W2051265686 modified "2023-10-16" @default.
• W2051265686 title "Enhancement of the Thermostability of a Fibrinolytic Enzyme from Bacillus amyloliquefaciens CH51" @default.
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• W2051265686 doi "https://doi.org/10.5352/jls.2013.23.1.15" @default.
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