A new organic solvent tolerant protease from Bacillus pumilus 115b

Abstract

Five out of the nine benzene-toulene-ethylbenzene-xylene (BTEX) tolerant bacteria that demonstrated high protease activity on skim milk agar were isolated. Among them, isolate 115b identified as Bacillus pumilus exhibited the highest protease production. The protease produced was stable in 25% (v/v) benzene and toluene and it was activated 1.7 and 2.5- fold by n-dodecane and n-tetradecane, respectively. The gene encoding the organic solvent tolerant protease was cloned and its nucleotide sequence determined. Sequence analysis revealed an open reading frame (ORF) of 1,149 bp that encoded a polypeptide of 383 amino acid residues. The polypeptide composed of 29 residues of signal peptide, a propeptide of 79 residues and a mature protein of 275 amino acids with a calculated molecular mass of 27,846 Da. This is the only report available to date on organic solvent tolerant protease from B. pumilus.

Salt stress represses production of extracellular proteases in Bacillus pumilus

“…The proteases from B. pumilus are classified into the serine protease family S8 and comprise an independent group named endopeptidase Q (Rawlings et al, 2010). Endopeptidase Q exhibits some unique catalysis properties, such as resistance to various detergents and surfactants, oxidative and thio reagents, and some organic solvents (Rahman et al, 2007;Feng et al, 2013). In addition, endopeptidase Q exhibits good thermostability (Wan et al, 2009).…”

Draft Genome Sequence of Bacillus pumilus BA06, a Producer of Alkaline Serine Protease with Leather-Dehairing Function

“…Representative subtilisins from Bacillus subtilis and the related species have been extensively studied for many years (3,13). Recently, alkaline serine proteases from various strains of Bacillus pumilus were characterized with unique biochemical characteristics, such as higher thermostability and catalytic efficiency (6,9,10,12,16). B. pumilus BA06, isolated from the proteinaceous soil, is able secrete a major alkaline serine protease that shows good potential in leather dehairing (8,17).…”

Single amino acid mutation alters thermostability of the alkaline protease from <italic>Bacillus pumilus</italic>: thermodynamics and temperature dependence

“…Great efforts have been made on screening and isolating new enzymes [3,4]. Up to now, various alkaline proteases have been purified and characterized from different strains of B. pumilus [5][6][7][8]. These proteases belong to subtilisin according to the sequence alignment and are classified as endopeptidase Q in the MEROPS database [9].…”