Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 24, Issue 21, Pages -Publisher
MDPI
DOI: 10.3390/ijms242115950
Keywords
B. subtilis; thermophilic serine protease; heterologous expression; detergent
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In this study, the extracellular expression of thermostable protease TTHA0724 was enhanced by developing a signal peptide library in the expression system of B. subtilis and optimizing signal peptides. The expression level of TTHA0724 in B. subtilis was 16.7 times higher compared to E. coli. TTHA0724 has great potential for industrial applications.
The thermostable protease TTHA0724 derived from Thermus thermophilus HB8 is an ideal industrial washing enzyme due to its thermophilic characteristics; although it can be expressed in Escherichia coli via pET-22b, high yields are difficult to achieve, leading to frequent autolysis of the host. This paper details the development of a signal peptide library in the expression system of B. subtilis and the optimization of signal peptides for enhanced extracellular expression of TTHA0724. When B. subtilis was used as the host and the optimized signal peptide was used, the expression level of TTHA0724 was 16.7 times higher compared with E. coli. B. subtilis as an expression host does not change the characteristics of TTHA0724. The potential application fields of TTHA0724 are studied. TTHA0724 can be used as a detergent additive at 60 degrees C, which can sterilize and eliminate mites while thoroughly cleaning protein stains. Soybean meal enzymatic hydrolysis with TTHA0724 at a high temperature produced a higher content of antioxidant peptides. These results indicate that TTHA0724 has great potential for industrial applications.
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