Isolation and characterization of a subtilisin-like proteinase of Bacillus intermedius secreted by the Bacillus subtilis recombinant strain AJ73 at different growth stages

Abstract

Two subtilisin-like serine proteinases of Bacillus intermedius secreted by the Bacillus subtilis recombinant strain AJ73 (pCS9) on the 28th and 48th h of culture growth (early and late proteinase, respectively) have been isolated by ion-exchange chromatography on CM-cellulose and by FPLC. Molecular weights of both proteinases were determined. The N-terminal sequences of the recombinant protein and mature proteinases of the original strain were compared. Kinetic parameters and substrate specificities of the early and late proteinase were analyzed. Physicochemical properties of the enzymes were studied.

Cloning, expression and characterization of the serine protease gene fromChaetomium thermophilum

“…Many subtilisin-like peptidases were previously reported to be produced by different organisms (Jorda et al 2000;Arnorsdottir et al 2002;Kluskens et al 2002;Jean et al 2003;Poole et al 2003;Kim et al 2006;Mikhailova et al 2007). But most of them are not stable when treated at a high temperature or a wide range of pH, and their optimum reaction temperature is relatively lower, e.g.…”

Effects ofBacillusSerine Proteases on the Bacterial Biofilms

“…B. pumilus 3-19 was found to be an important source of proteases such as subtilisin-like protease (AprBp) and glutamyl endopeptidase (GseBp) [ 30 , 39 ]. Subtilisin-like protease, a 27 kDa extracellular protease, was purified from B. subtilis AJ73 recombinant strain carrying pCS9 plasmid with a gene encoding AprBp of B. pumilus 3-19 [ 40 ]. Glutamyl endopeptidase, a 23 kDa extracellular protease, was purified from B. subtilis JB 20-36 recombinant strain carrying Δ58.21 plasmid with a gene encoding GseBp of B. pumilus 3-19 [ 41 ].…”