The storage stability of Bacillus subtilis spore displaying cysteine protease of Clonorchis sinensis and its effect on improving the gut microbiota of mice

2021 ◽  
Vol 105 (6) ◽  
pp. 2513-2526
Author(s):  
Zeli Tang ◽  
Zhanshuai Wu ◽  
Hengchang Sun ◽  
Lu Zhao ◽  
Mei Shang ◽  
...  
Catalysts ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 606
Author(s):  
Silu Sheng ◽  
Edgardo T. Farinas

Enzymes displayed on the Bacillus subtilis spore coat have several features that are useful for biocatalysis. The enzyme is preimmobilized on an inert surface of the spore coat, which is due to the natural sporulation process. As a result, protein stability can be increased, and they are resistant to environmental changes. Next, they would not lyse under extreme conditions, such as in organic solvents. Furthermore, they can be easily removed from the reaction solution and reused. The laboratory evolved CotA laccase variant T480A-CotA was used to oxidize the following phenolic substrates: (+)-catechin, (−)-epicatechin, and sinapic acid. The kinetic parameters were determined and T480A-CotA had a greater Vmax/Km than wt-CotA for all substrates. The Vmax/Km for T480A-CotA was 4.1, 5.6, and 1.4-fold greater than wt-CotA for (+)-catechin, (−)-epicatechin, and sinapic acid, respectively. The activity of wt-CotA and T480A-CotA was measured at different concentrations from 0–70% in organic solvents (dimethyl sulfoxide, ethanol, methanol, and acetonitrile). The Vmax for T480A-CotA was observed to be greater than the wt-CotA in all organic solvents. Finally, the T480A-CotA was recycled 7 times over a 23-h period and up to 60% activity for (+)-catechin remained. The product yield was up to 3.1-fold greater than the wild-type.


1984 ◽  
Vol 25 (2) ◽  
pp. 99-105_1 ◽  
Author(s):  
Michio HAMAMOTO ◽  
Shigetoshi YAMAGUCHI ◽  
Yoshiteru ASAI ◽  
Kousou SHIMODA

2011 ◽  
Vol 62 (5) ◽  
pp. 1368-1373 ◽  
Author(s):  
Guohui Li ◽  
Qi Tang ◽  
Huiqing Chen ◽  
Qin Yao ◽  
Degang Ning ◽  
...  

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