PRODUCTION OF ELASTASE AND PROTEINASE BY PSEUDOMONAS AERUGINOSA

Abstract

Morihara, Kazuyuki (Shionogi Research Laboratory, Osaka, Japan). Production of elastase and proteinase by Pseudomonas aeruginosa . J. Bacteriol. 88: 745–757. 1964.—Some strains of Pseudomonas aeruginosa produced elastase, but the others did not. The elastase-positive strains produced two proteinases (fractions II and III), and the elastase-negative strains produced one proteinase (fraction III). Moreover, one proteinase (fraction I) was produced by both elastase-positive and elastase-negative strains, but the activity was small and negligible. The three proteinases were separated by column chromatography on diethylaminoethyl-cellulose, and elastolytic activity corresponded to fraction II. The effect of components of the medium was slight for production of fraction II; fraction III was produced only in synthetic medium containing Ca ion and not in natural medium. The optimal pH of fractions I, II, and III for casein was 6.5, 8.0, and 10.0, respectively; that of fraction II for elastin was 7.5 to 8.0. The other characters of the three proteinases also differed. Both the proteolytic and the elastolytic activities of fraction II showed a similar behavior for various treatments, except the inhibition test by NaCl and serum. Fraction III proteinases from various strains were identical in their enzymatic or other characters, showing that various strains were related regardless of the difference of their elastolytic activity. The reason that the elastolytic activity of P. aeruginosa differed according to the origin of the strain is discussed on the basis of a taxonomic study; results indicate that the ability to produce elastolytic activity (fraction II) may be a dissociative character of the species.

The Pseudomonas aeruginosa flagellum confers resistance to pulmonary surfactant protein‐A by impacting the production of exoproteases through quorum‐sensing

“…The production of many P. aeruginosa exoproteases is tightly regulated by QS, an intercellular signalling process (Juhas et al, 2005), as well as by the availability of cations Zn 2+ and Ca 2+ . In fact, the expression and processing of the predominant QS-regulated P. aeruginosa protease, elastase, is dependent on the presence of Zn 2+ and Ca 2+ (Morihara, 1964;Olson and Ohman, 1992;Sarkisova et al, 2005). As a metalloprotease, elastase requires Zn 2+ for its catalytic activity, which is stabilized by Ca 2+ (Morihara, 1964;Thayer et al, 1991).…”

“…In fact, the expression and processing of the predominant QS-regulated P. aeruginosa protease, elastase, is dependent on the presence of Zn 2+ and Ca 2+ (Morihara, 1964;Olson and Ohman, 1992;Sarkisova et al, 2005). As a metalloprotease, elastase requires Zn 2+ for its catalytic activity, which is stabilized by Ca 2+ (Morihara, 1964;Thayer et al, 1991). These analyses were subsequently confirmed by Sarkisova et al (2005), who showed that Zn 2+ and Ca 2+ drastically induced the production of exoproteases in P. aeruginosa biofilms that formed under in vitro conditions.…”

Regulation of toxA and regA by the Escherichia coli fur gene and identification of a Fur homologue in Pseudomonas aeruginosa PA103 and PA01

“…Most strains of P. aeruginosa produce three different proteases (Morihara, 1964). Strain PA103 was originally selected as being protease-deficient (Liu, 1968).…”

A COMPARISON OF DIFFERENT METHODS FOR DETERMINING ELASTASE ACTIVITY OF PSEUDOMONAS AERUGINOSA STRAINS FROM MINK

“…Growth was monitored by measuring culture turbidity. Previous investigations have shown that alkaline protease is not produced in the medium used in this study (13,22).…”