Open AccessOccurrence of a metalloprotease (thermolysin) inhibitor among Brevibacillus species and purification of such inhibitor from Brevibacillus reuszeri IFO 15719 T
Author(s) -
KOBAYASHI Takeshi,
NAKAGAWA Naoji,
IMADA Chiaki,
HAMADASATO Naoko,
WATANABE Etsuo
Publication year - 2004
Publication title -
fisheries science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.412
H-Index - 64
eISSN - 1444-2906
pISSN - 0919-9268
DOI - 10.1111/j.1444-2906.2003.00804.x
Subject(s) - thermolysin , microbiology and biotechnology , strain (injury) , biology , biochemistry , chemistry , enzyme , trypsin , anatomy
ABSTRACT: The extracellular production of a thermolysin inhibitor by 534 wild‐type strains isolated from marine sediments and related‐type strains was examined. The inhibition of thermolysin activity by strain T‐177 was observed on a casein agar medium. According to our detailed taxonomic study, strain T‐177 is related to Brevibacillus laterosporus . Further screening for a thermolysin inhibitor was performed using strain T‐177 and nine other taxonomically related Brevibacillus type strains, and the ability to produce the inhibitor was observed in five strains. Among these strains, B. reuszeri IFO 15719 T exhibited the highest thermolysin inhibitory activity in broth media, and thus was used for the purification and characterization of the inhibitor. Chromatographic analyses suggested that this substance is a monomeric protein with a molecular mass of 60 kDa.