Bacterial extracellular protease activities in field soils under different fertilizer managements

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Abstract:

The major extracellular endopeptidase from Bacillus subtilis PF212 (isolated from paddy field soil) and B. subtilis CF80 (isolated from upland field soil) belongs to the group of serine proteases produced by Bacillus spp. known as subtilisins (optimum pH 7.0, optimum temperature 60°C, and molecular mass 28 kDa). The NH2-terminal amino acid sequence (20 amino acids) of the endopeptidase from (i) strain CF80 was identical with that of subtilisin BPN' and (ii) strain PF212 was identical with that of subtilisin Amylosacchariticus. The properties (i.e., effect of inhibitors) of these endopeptidases were similar to those of the overall soil endopeptidase and soil endopeptidases extracted from paddy field soil. From the numbers of B. subtilis we isolated from paddy fields and found to produce a subtilisin-like serine protease, it seemed possible to consider that subtilisin was one of the soil endopeptidases in paddy field soils. The major extracellular endopeptidase from Serratia marcescens (strains 4-12-132, 4-12-131, and 4-60-110) isolated from upland field soils applied with animal slurry is a serratial metalloprotease (optimum pH 9.5, optimum temperature 40°C, and molecular mass 50 kDa). The NH2-terminal amino acid sequence (20 amino acids) of the endopeptidase from strain 4-12-132 was identical with that of serratial metalloprotease, and partial DNA sequence of the endopeptidase gene of S. marcescens 4-12-132 had high homology with that of the serratial metalloprotease gene. The properties (i.e., effect of inhibitors) of this endopeptidase were similar to those of the overall soil endopeptidase in upland fields applied with animal slurry. Thus, it was possible to consider that serratial metalloprotease was one of the soil endopeptidases in upland fields applied with animal slurry.Key words: subtilisin, serratial metalloprotease, soil endopeptidase, proteolytic bacteria.

L'endopeptidase extracellulaire majeure de Bacillus subtilis (PF212) isolée du sol de rizières, et de B. subtilis (CF80) isolée du sol de champs non submergés, appartient aux subtilisines produites par Bacillus spp. (protéase à sérine, pH optimal de 7,0, température optimale de 60 °C et poids moléculaire de 28 kDa). La séquence des 20 acides aminés amino-terminaux a démontré que les résidus de l'endopeptidase de CF80 étaient identiques à ceux de la subtilisine BPN', et que les résidus de PF212 étaient identiques à ceux de la subtilisine Amylosacchariticus. Leurs propriétés (effets des inhibiteurs) étaient semblables à ceux des endopeptidases totales du sol de champs non cultivés et des endopeptidases extraites du sol des rizières. Puisque qu'un bon nombre de B. subtilis produisant des protéases à sérine de types semblables ont été isolés des rizières, il est concevable que la subtilisine était l'une des endopeptidases retrouvée dans le sol des rizières. L'endopeptidase extracellulaire majeure de Serratia marcescens (4-12-132, 4-12-131 et 4-60-110) isolée du sol de champs non submergés épandus avec du lisier appartient aux métalloprotéases serratiales (pH optimal de 9,5, température optimale de 40 °C et poids moléculaire de 50 kDa). La séquence amino-terminale (20 acides aminés) de l'endopeptidase de 4-12-132 était identique à celle d'une métalloprotéase serratiale, et la séquence partielle d'ADN du gènes de l'endopeptidase de S. marcescens (4-12-132) était fortement homologue à celle du gène de la métalloprotéase serratiale. Puisque leurs propriétés (effets des inhibiteurs) étaient semblables à celles des endopeptidases du sol de champs non submergés épandus avec du lisier, il est concevable que la métalloprotéase serratiale était l'une des endopeptidases du sol de champs non submergés épandus avec du lisier.Mots clés : subtilisine, métalloprotéase serratiale, endopeptidases du sol, bactéries protéolytiques.[Traduit par la Rédaction]

Document Type: Research Article

Publication date: May 1, 2003

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  • Published since 1954, this monthly journal contains new research in the field of microbiology including applied microbiology and biotechnology; microbial structure and function; fungi and other eucaryotic protists; infection and immunity; microbial ecology; physiology, metabolism and enzymology; and virology, genetics, and molecular biology. It also publishes review articles and notes on an occasional basis, contributed by recognized scientists worldwide.
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