Serine protease

Improving production of extracellular proteases by random mutagenesis and biochemical characterization of a serine protease in Bacillus subtilis S1-4

X. C. Wang, Zhao, H. Y., Liu, G., Cheng, X. J., Feng, H., Wang, X. C., Zhao, H. Y., Liu, G., Cheng, X. J., and Feng, H., Improving production of extracellular proteases by random mutagenesis and biochemical characterization of a serine protease in Bacillus subtilis S1-4, vol. 15, p. -, 2016.

The feather is a valuable by-product with a huge annual yield produced by the poultry industry. Degradation of feathers by microorganisms is a prerequisite to utilize this insoluble protein resource. To improve the degrading efficiency of feathers, mutagenesis of the bacterium Bacillus subtilis S1-4 was performed. By combining ultraviolet irradiation and N-methyl-N’-nitro-N-nitrosoguanidine treatment for mutagenesis, a high protease-producing mutant (UMU4) of B.

Molecular cloning and characterization of a subtilisin-like protease from Arabidopsis thaliana

D. H. Li, Xi, H., Yu, X. B., and Cai, Y. P., Molecular cloning and characterization of a subtilisin-like protease from Arabidopsis thaliana, vol. 14, pp. 16535-16545, 2015.

The Arabidopsis thaliana genome encodes 56 subtilisin-like serine proteases (subtilases). In order to evaluate the protease activity of a previously uncharacterized subtilase, designated as AtSBT1.9, we cloned its full-length cDNA from A. thaliana seedlings. An AtSBT1.9 mature peptide coding sequence was inserted into the bacterial expression vector, pMAL-c2x, and the recombinant vector was transformed into Escherichia coli BL21 (DE3).

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