Open AccessProteolytic enzymes from recombinant Streptomyces lividans TK24
Author(s) -
Aretz Werner,
Koller Klaus P.,
Riess Günther
Publication year - 1989
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1989.tb03592.x
Subject(s) - proteases , recombinant dna , enzyme , biochemistry , streptomycetaceae , biology , streptomyces , chymotrypsin , actinomycetales , microbiology and biotechnology , chemistry , bacteria , trypsin , genetics , gene
Different proteases from the culture fluids of recombinant Streptomyces lividans strains were isolated. Several individual proteases were separated and characterized. A chymotrypsin‐chylike activity (CLA) was identified that specifically degrades a fusion protein between the α‐amylase inhibitor from S. tendae (Tendamistat, HOE467) and proinsulin from the monkey Macaca fascicularis . The effective chemical inhibition of the degrading enzyme is demonstrated.