Abstract
It was found that a submerged culture ofMycobacterium phlei degrades simple esters (ethylacetate and ethylbutyrate) as well as synthetic lipids (triacetine and tributyrine). The effect of pH on the rate of degradation of tributyrine was investigated and the maximum activity of esterases found within a wide range of pH. The activity of esterases was followed during growth of a submerged culture ofMycobacterium phlei. Esterases were not released into the cultivation medium during growth or even during the early stationary phase. Only a low steady activity of esterases could be demonstrated in a filtrate of the cultivation liquid. The total activity of esterases reached its maximum after a 6–11 day incubation. The specific activity of esterases reached a maximum on the 6th day of incubation; its value decreased to about one half and did not change substantially on prolonged incubation. Changes in the specific activity of esterases were found to be time-related with changes of pH and a decrease of the specific activity was associated with a release of macromolecular compounds into the incubation medium. Esterases as well as other macromolecular compounds were isolated from the filtrate of the cultivation medium ofMycobacterium phlei. The isolated preparation contained 60–72% total activity of esterases present in the filtrate of the cultivation liquid.
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References
Andrejew A., Germez-Rieux Ch., Tacquet A.: Activité lipasique des bacilles tuberculeux et desMycobactéries atypiques.Ann. Inst. Pasteur (Paris) 99, 68 (1960).
Andrejew A., Tacquet A.: Activité lipasique des Mycobactéries. II. Influence du milieu et de l'age de la culture. Essais de differentes substrats et inhibiteurs.Zbl. Bakt., I. Abt. 194, 536 (1964).
Andrejew A., Tacquet A.: Differents types d'activité lipasique chez les Mycobactéries.Ann. Inst. Pasteur (Paris) 108, 652 (1965).
Bergmann F., Rimon S., Segal R.: Effect of pH on the activity of eel esterase towards different substrates.Biochem. J. 68, 493 (1958).
Cattaneo G.: Lipase activity ofMycobacterium ranae.Arch. Sci. Med. 100, 34 (1955); C.A.49, 14895ef (1955).
Cohen S., Kushnick J. B., Purdy C. V.: Observations on mycobacterial esterases with series of synthetic substrates.J. Bacteriol. 66, 266 (1953).
Cohen S., Purdy C. V., Kushnick J. B.: Inhibition of mycobacterial esterases by Polymyxin B.Antibiotics & Chemotherapy 4, 18 (1954).
Davis B. D., Dubos R. J.: Interaction of serum albumin, free and esterified oleic acid and lipase in relation to cultivation of the tubercle bacillus.Arch. Biochem. 11, 201 (1964).
Davis B. D., Dubos R. J.: The binding of fatty acids by serum albumin, a protective growth factor in bacteriological media.J. Exp. Med. 86, 215 (1947).
Davis B. D., Dubos R. J.: The inhibitory effect of lipase on bacterial growth in media containing fatty acid esters.J. Bacteriol. 55, 11 (1948).
Edson N. L.: The intermediary metabolism in the mycobacteria.Bacteriol. Rev. 15, 147 (1952).
Hauduroy P., Bel F., Hovanessian A.: Techniques permettant de faire un diagnostic précis deMycobacterium kansasii (Hauduroy).Ann. Inst. Pasteur (Paris) 111, 84 (1966).
Hubáček J., Málek I.: Some biological and biochemical properties of acid-fast and non-acid-fast strains ofMycobacterium phlei. (In Czech).Čs. mikrobiologie 3, 32 (1958).
Jezeski J. J., Halvorson H. O., Macy H.: The action of microorganisms on fats. I. Oxygen uptake by bacteria in the presence of lipid substrates.J. Bacteriol. 59, 645 (1950).
Laboureur P., Labrousse M.: Lipase de Rhizopus arrhizus. Obtention, purification et propriétés de la lipase deRhizopus arrhizus varDelamar.Bull. Soc. Chim. Biol. 48, 747 (1966).
Meyer J., Malgras J., Schär R.: The specifity of tributyrin as a substrate for esterases and for lipasesBull. assoc. diplomes microbiol. fac. pharm. Nancy 52, 10 (1953); C.A.49, 8390g (1955).
Monod F., Jacob F.: General conclusions: teleonomic mechanisms in cellular metabolism, growth, and differentiation.Cold Spring Harbor Symp. 26, 389 (1961).
Moyed H. S., Umbarger H. A.: Regulation of biosynthetic pathways.Physiol. Rev. 42, 444 (1962).
Myers D. K., Tol J. W., deJonge M. H. T.: Studies on aliesterases. 5. Substrate specifity of esterases of some saprophytic mycobacteria.Biochem. J. 65, 223 (1957).
Pattyn S. R.: A study of some strains ofMycobacterium xenopei.Zbl. Bakt., I. Abt. 201, 246 (1966).
San Clemente C. L., Vadehra D. V.: Instrumental assay of microbial lipase at constant pH.Appl. Microbiol. 15, 110 (1967).
Sartory A., Meyer J.: Technique d'isolement et de characterisation d'une lipase des bacilles acidoalcoolo-resistants.Bull. Acad. Natl. Med. 131, 243 (1947).
Scarpa B.: Caratteristiche biologiche di micobatteri anomali.Bollettino I.S.M. 42, 11 (1963).
Tison F., Tacquet A., Roos P., Devulder B.: Test qualitatif simple d'etude de l'activité lipasique des mycobactéries.Ann. Inst. Pasteur (Paris) 110, 784 (1966).
Viallier J., Cayré R. M., Lanery R.: Essais de “transformation” concernant les Mycobactéries.Compt. rend. Soc. Biol. 160, 1473 (1966).
Wayne L. C.: Differentiation of mycobacteria by their effect on Tween 80.Am. Rev. Resp. Dis. 86, 579 (1962).
Wayne L. C., Doubek J. R., Russell R. L.: Classification and identification of Mycobacteria. I. Test employing Tween 80 as substrate.Am. Rev. Resp. Dis. 90, 588 (1964).
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Procházka, P., Nohýnek, M., Šroglová, A. et al. Esterases in mycobacteria. Folia Microbiol 17, 17–27 (1972). https://doi.org/10.1007/BF02872249
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DOI: https://doi.org/10.1007/BF02872249