Studies on Bacterial Protease

TSURU, Daisuke; Kira, Heizo; YAMAMOTO, Tekehiko; Fukumoto, Juichiro

doi:10.1271/bbb1961.31.330

Cited by 12 publications

(2 citation statements)

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“…The molecular mass of the trypsin-like protease was found to be 21 kDa. which is close to that reported for that of S. griseus, 22.8 kDa [46]. It is much higher than that reported for S. (radiae (16.5 kDa) [47] and S. moderatus Table 3 Effect of metal ions on the activity of the metalloprotease and trypsin-like enzyme Enzyrne (0.…”

Section: Effect Of Metal Ions On Activitysupporting

confidence: 74%

Extracellular proteases from Streptomyces spp. G₁₅₇: purification and characterization

Sampath

Subramanian

Chandrakasan

1997

Biotech and App Biochem

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While investigating about 250 strains of actinomycete isolated from tannery soil, Streptomyces spp. G157 exhibited the highest potency for the production of extracellular proteases. After preliminary fractionation by differential precipitation with (NH4)2SO4 the purification was carried out on a Sephadex G‐100 gel‐filtration column. Two proteolytically active fractions, fractions 1 and 2, were obtained. The two fractions were further purified on a DEAE‐cellulose ion‐exchange column. Upon characterization, fraction 1 was found to be a metal‐chelator‐sensitive protease and fraction 2 a trypsin‐like protease. The metal‐chelator‐sensitive protease was found to have a pH optimum over the range 7.0Ő8.0, a temperature optimum between 45 and 55 ° C and molecular mass of 36 kDa. The trypsin‐like protease was found to have a pH optimum between 8.4 and 8.6, a temperature optimum of 37 ° C and molecular mass of 21 kDa.

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Section: Effect Of Metal Ions On Activitysupporting

confidence: 74%

Extracellular proteases from Streptomyces spp. G₁₅₇: purification and characterization

Sampath

Subramanian

Chandrakasan

1997

Biotech and App Biochem

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“…Examples are proteases produced by Slreptomyces j?adiael7 B. lichemformis, 24 3. and B. s~b t i l i s .~~.~~ I n some cases the accompanying protein \\as shov n t o be a neutral protease. No accompanying protease has been observed after column chromatography or after moving boundary or sedimentation analysis of the three subtilisins;2t3 1fi, 19 further investigations into the homogeneity by disc electrophoresis have not been reported nor has separation been a c h i e~e d .~* -~~ I n this paper methods are described for the characterization of proteolytic preparations or of proteolytic activities in fermentation broth, allowing direct comparison with reference preparations. Evidence is presented for the multiplirity of the subtilisins and of other alkaline proteases, which show-characteristic patterns of activity.…”

Section: Introductionmentioning

confidence: 92%

Proteolytic components of alkaline proteases of Bacillus strains. Zymograms and electrophoretic isolation

Zuidweg¹,

Bos²,

Welzen³

1972

Biotech & Bioengineering

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SummaryCharacterization of proteolytic activity in preparations or fermentation broth is accomplished by methods based on a combination of disc electrophoresis and visualization of the activity. The methods permit a direct comparison with reference preparations. All alkaline proteases studied, including the three subtilisins, were found to consist of several proteolytic components. The zymograms of the subtilisin type preparations show an irregular pattern. At least 14 different components may be observed, belonging to 6 types of mobility pattern, 3 of which could be assigned to the subtilisins. None of the components belongs to the group of metalloproteases. A quite regular pattern is shown by the zymogram of protease preparations produced by the alkalophilic Bacillus strains.A few of the components of the subtilisin preparations lllaxatase and protease A were isolated by preparative disc electrophoresis and by electrofocusing, allowing a further characterization. Special attention was directed to the determination of properties specific for the application of subtilisins as additives in household detergents. Thermostability in sodium tripolyphosphat,e solution was found to range from about 10% for one of the minor components to 80% for the main component of Maxatase. Three types of curves representing the effect of pH on the activity were observed. The curve of the main component of Maxatase shows a characteristic shape with a maximum at pH 10.3; with other components lower pH optima were observed. Isoelectric points of the components were found to range from pH 7 to 10.

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Proteases of the genus Bacillus. II. Alkaline proteases

Keay

Moser

Wildi

1970

Biotech & Bioengineering

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snmmaryThe alkaline proteases of B. subtilis NRRL B3411, B. pumilis, and B. lichenijormis have been isolated by fractionation followed by ion exchange chromatography and their homogeneity demonstrated. General enzyme properties of the B. subtilis NRRL B3411 alkaline protease have been studied and attempts made to differentiate a group of alkaline protesses. It is clear that the alkaline proteases known as Subtilisins or Subtilopeptidases are not exclusive to B. subtilis but are common to many BaciUi and therefore the generic name Bacillopeptidases has been proposed. It is clear too that on the basis of the effect of pH on activity, amino acid composition, esterase activity, and immunological crossreactions the Bacillopeptidsses can be divided into two groups or types: ( a ) Bacillopeptidase A (Subtilisin A or Subtilopeptidase A) which includes Subtiliiin Carlsberg, B. lichaifonnis, and B. pumilis alkaline proteases; (b) Bacillopeptidase B (Subtiliiin B or Subtilopeptidase B) which includes B subtilis NRRL B3411, Subtilisin Novo, Subtilisin BPN' (Nagarse), alkaline protease Daiwa Kasei, and (probably) B. subtilis oar. amylosacchariticus. At present, no further differentiation is possible and whether or not the enzymes within group A or B are identical remains an open question.Methods for examination of crude enzyme mixtures or fermentation beers are described and from the examination of a number of crude enzymes and fermentation beers it appears that organisms producing Bacillopeptidase A do not produce neutral protease or amylase, while organisms producing Bacillopeptidase B produce a neutral protease and amylase as well. 213

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Studies on Bacterial Protease

Cited by 12 publications

References 0 publications

Extracellular proteases from Streptomyces spp. G₁₅₇: purification and characterization

Extracellular proteases from Streptomyces spp. G₁₅₇: purification and characterization

Proteolytic components of alkaline proteases of Bacillus strains. Zymograms and electrophoretic isolation

Proteases of the genus Bacillus. II. Alkaline proteases

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Studies on Bacterial Protease

Cited by 12 publications

References 0 publications

Extracellular proteases from Streptomyces spp. G157: purification and characterization

Extracellular proteases from Streptomyces spp. G157: purification and characterization

Proteolytic components of alkaline proteases of Bacillus strains. Zymograms and electrophoretic isolation

Proteases of the genus Bacillus. II. Alkaline proteases

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Product

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Extracellular proteases from Streptomyces spp. G₁₅₇: purification and characterization

Extracellular proteases from Streptomyces spp. G₁₅₇: purification and characterization