Purification and some properties of the extracellular protease ofBacillus pumilus

Fabián, J.

doi:10.1007/bf02873080

Cited by 4 publications

(3 citation statements)

References 26 publications

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“…With the exception of the alanyl tripeptidyl peptidase-like activity, the activities reported in Tables 1 and 2 were serine-or chymotrypsinlike serine-class proteolytic activities. Such extracellular proteinases have been observed previously in the genus Bacillus (Gupta et al, 2002;Kato et al, 1992;Leshchinskaya et al, 1997;Priest, 1985), including B. pumilus (Aoyama et al, 2000;Fabian, 1970;Kumar, 2002;Miyaji et al, 2006;Tran-Chau & Urbanek, 1974).…”

Section: Detection and Characterization Of Extracellular Proteolytic supporting

confidence: 70%

Extracellular proteolytic activities expressed by Bacillus pumilus isolated from endodontic and periodontal lesions

Johnson

Shaw

Nelson

et al. 2008

Journal of Medical Microbiology

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The purpose of the present study was to identify 12 Bacillus isolates that had been obtained from root canals of teeth requiring endodontic therapy and from periodontal pockets in severe marginal periodontitis, and to determine whether these isolates exhibited extracellular proteolytic activity and, using in vitro assays, whether any such activity could degrade substrates that would be pathophysiologically relevant with regard to the production of endodontic and periodontal lesions. Biochemical and carbohydrate fermentation patterns were used in the identification of all strains, which was confirmed by determination of the16S rRNA gene sequence for strain BJ0055. Screening for production of extracellular proteolytic activity by all strains was done with a general proteinase substrate. All isolates were identified as representing Bacillus pumilus and all exhibited extracellular proteolytic activity. The putative pathophysiological relevance of extracellular proteinase production in strain BJ0055 was assessed using fluorophore-labelled elastin and collagen and several chromogenic peptides. Probable classes of proteinases acting on each substrate were investigated using class-specific inhibitors. Activity-pH profiles were determined in buffers at different pH values. Extracellular activities that were caseinolytic, elastinolytic, collagenolytic, glutamyl endopeptidase-like, and alanyl tripeptidyl peptidase-like were observed. No trypsin-like activities were detected. Serine-and chymotrypsin-like serine proteinase activities were detected, with activity observed at neutral and alkaline, but not acidic, pH. B. pumilus strains isolated from endodontic and periodontal lesions exhibited extracellular activities that degrade elastin, collagen and other substrates. These activities may be virulence factors that contribute to tissue damage in apical periodontitis and severe marginal periodontitis.

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Section: Detection and Characterization Of Extracellular Proteolytic supporting

confidence: 70%

Extracellular proteolytic activities expressed by Bacillus pumilus isolated from endodontic and periodontal lesions

Johnson

Shaw

Nelson

et al. 2008

Journal of Medical Microbiology

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“…clavatus on Nigerian poultry feeds vis-a-vis the potential health risks posed to farm animals is discussed.Microbial degradation of agricultural produce during storage is due to the ability of the implicated microbes to produce a wide range of extracellular enzymes including proteases. Several such enzymes from various saprophytes have been extracted and purified (ARIMA and IWASAKI 1968, FABIAN 1970, BASAVESWARA RAO et al 1981.A search through the available literature showed lack of information on the proteases of Aspergillus cluvatus, a known toxigenic and tumorigenic fungus. Although previous workers (FORGACS et al 1954, GLINSUKON et al 1974, FLANNIGAN et al 1984) have expressed concern about the potential health risks posed to consumers by the presence of this organism on various agricultural produce, few studies have been made of the physiology and biochemistry of A .…”

mentioning

confidence: 99%

“…Microbial degradation of agricultural produce during storage is due to the ability of the implicated microbes to produce a wide range of extracellular enzymes including proteases. Several such enzymes from various saprophytes have been extracted and purified (ARIMA and IWASAKI 1968, FABIAN 1970, BASAVESWARA RAO et al 1981.…”

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confidence: 99%

The purification and activities of an alkaline protease of Aspergillus clavatus from Nigerian poultry feeds

Ogundero

Osunlaja

1986

J. Basic Microbiol.

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Optimal growth and extracellular protease production by Aspergillus clavatus Des. was recorded at 30 degrees C and between days 5 and 7 of the 8-day incubation period. Purification of this enzyme was achieved by a combination of ultrafiltration, alcoholic precipitation and fractionation on DEAE-cellulose and Sephadex-G.200. A single peak of an alkaline protease was subsequently obtained with a 9-fold increase in specific activity and a final recovery value of 26.2%. The enzyme had optimal activity at 37 degrees C and a pH of 7.8. The enzyme did not degrade leucine amide, hippurylphenylalanine and hippurylarginine indicating lack of exo-protease activity. However, endo-protease activity led to a rapid hydrolysis of gelatin with optimal activity at 40 degrees C and pH 7.8. The high incidence of A. clavatus on Nigerian poultry feeds vis-a-vis the potential health risks posed to farm animals is discussed.

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Isolation, partial purification, and some properties of protease I from a thermophilic mold Thermoascus aurantiacus var. levisporus

1984

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Purification and some properties of the extracellular protease ofBacillus pumilus

Cited by 4 publications

References 26 publications

Extracellular proteolytic activities expressed by Bacillus pumilus isolated from endodontic and periodontal lesions

Extracellular proteolytic activities expressed by Bacillus pumilus isolated from endodontic and periodontal lesions

The purification and activities of an alkaline protease of Aspergillus clavatus from Nigerian poultry feeds

Isolation, partial purification, and some properties of protease I from a thermophilic mold Thermoascus aurantiacus var. levisporus

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