Articles with "endopeptidase stenotrophomonas" as a keyword



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Characterization and rational design for substrate specificity of a prolyl endopeptidase from Stenotrophomonas maltophilia.

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Published in 2020 at "Enzyme and microbial technology"

DOI: 10.1016/j.enzmictec.2020.109548

Abstract: A novel prolyl endopeptidase from Stenotrophomonas maltophilia, SmPEP, was discovered and characterized. The specific activity of the recombinant SmPEP expressed by Escherichia coli BL21 (DE3), was 68.3 U/mg at pH 8.0 and 37 °C. In order… read more here.

Keywords: prolyl endopeptidase; substrate; endopeptidase stenotrophomonas; substrate specificity ... See more keywords