Extracellular proteases of Halobacillus blutaparonensis strain M9, a new moderately halophilic bacterium

Santos, Anderson Fragoso dos; Valle, Rogério; Pacheco, C.A.; Alvarez, Vanessa Marques; Seldin, Lucy; Santos, André Luis Souza dos

doi:10.1590/s1517-83822014005000015

Cited by 18 publications

(6 citation statements)

References 27 publications

(40 reference statements)

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“…In fact, there are very few studies reporting proteases from Halobacillus species. The available data showed a protease molecular weight range of 30–80 KDa .…”

Section: Resultsmentioning

confidence: 99%

“…By referring to the few reports characterizing proteases from Halobacillus species, there is wide difference concerning the optimum salt and salt range/concentration for production. As example, Santos et al , found that strain Halobacillus blutaparonensis M9 secreted protease activity at NaCl concentrations ranging from 50 to 100 g/L with an optimum level at 25 g/L NaCl while Karbalaei‐Heidari et al reported maximum protease production from Halobacillus karajensis MA‐2 using the NaNO 3 as salt at a concentration of 127.5 g/L. In addition, in Halobacillus sp.…”

Section: Discussionmentioning

confidence: 99%

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Characterization of thermo-solvent stable protease fromHalobacillussp. CJ4 isolated from Chott Eldjerid hypersaline lake in Tunisia

Daoud

Jlidi

Hmani

et al. 2016

J. Basic Microbiol.

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About 110 newly isolated halophilic and halotolerant bacteria were screened for protease production. A moderately halophilic strain (CJ4), isolated from Chott Eldjerid Hypersaline lake in Tunisia, showed the highest activity on agar plate and was then selected. The biochemical and physiological characterization of the isolate along with the 16S rRNA sequence analysis placed it in the genus Halobacillus. Protease production was maximal at 120 g/L NaCl (2 M) and it started from the post-exponential phase reaching a maximum level at the early decline phase of bacterial growth. Protease activity was optimal at 0.4 M NaCl, pH 9 and 45 °C. It showed an excellent stability over wide ranges of temperatures (30-60 °C), NaCl concentrations (0-5 M), and pH values (5-10), which make it a good candidate for industrial applications at harsh conditions. Crude protease was strongly inhibited by PMSF revealing the dominance of serine proteases. Protease activity exhibited high stability in the presence of several organic solvents and detergent additives. These findings make Halobacillus sp. CJ4 protease with a great interest for many biotechnological applications at high salt or low water content such as peptide synthesis and detergent formulation.

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“…In fact, there are very few studies reporting proteases from Halobacillus species. The available data showed a protease molecular weight range of 30–80 KDa .…”

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Characterization of thermo-solvent stable protease fromHalobacillussp. CJ4 isolated from Chott Eldjerid hypersaline lake in Tunisia

Daoud

Jlidi

Hmani

et al. 2016

J. Basic Microbiol.

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“…SK37 ( 21 ), Geomicrobium sp. EMB2 ( 22 ), and Halobacillus blutaparonensis M9 ( 23 ). However, reports from halophilic proteases are very limited in the literature ( 24 ).…”

Section: Introductionmentioning

confidence: 99%

Alkaline and Halophilic Protease Production by Bacillus luteus H11 and its Potential Industrial Applications

Kalwasińska

Jankiewicz

Felföldi

et al. 2018

Food Technol. Biotechnol.

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SUMMARY This paper presents the results of the study on the production of protease by Bacillus luteus H11 isolated from an alkaline soda lime. B. luteus H11 was identified as an alkalohalophilic bacterium, and its extracellular serine endoprotease also showed an extreme alkali- and halotolerance. It was remarkably stable in the presence of NaCl up to 5 M. The enzyme was active in a broad range of pH values and temperatures, with an optimum pH of 10.5 and a temperature of 45 °C. It had a molecular mass of about 37 kDa and showed activity against azocasein and a synthetic substrate for the subtilisin-like protease, N-succinyl- l -phenylalanine- p -nitroanilide. The halo-alkaline protease produced by B. luteus H11 seems to be significant from an industrial perspective because of its tolerance towards high salinity and alkalinity as well as its stability against some organic solvents, surfactants and oxidants. These properties make the protease suitable for applications in food, detergent and pharmaceutical industries, and also in environmental bioremediation.

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“…Proteases with proteolytic activities in a wide range of pH, and stability to salt (approx. 3 M) and solvents have been reported from microbial sources (Kumar & Takagi, ; Santos et al., ). Proteases with stability at high temperature and salt concentrations, and alkaline pH optima are desirable for applications in detergents and tanning (Joo et al, ).…”

Section: Discussionmentioning

confidence: 99%

Alkaline serine proteases from Helicoverpa armigera: potential candidates for industrial applications

Akbar

Sharma

2016

Arch Insect Biochem Physiol

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We characterized trypsin- and chymotrypsin-like serine alkaline proteases from cotton bollworm, Helicoverpa armigera, for their probable potential application as additives in various bio-formulations. Purification was achieved by using hydroxylapatite, DEAE sephadex and CM sephadex columns, which resulted in increased enzyme activity by 13.76- and 14.05-fold for trypsin and chymotrypsin, respectively. Michaelis-Menten constants (K ) for substrates of trypsin and chymotrypsin, BApNA and SAAPFpNA, were found to be 1.25 and 0.085 mM, correspondingly. Fluorescent zymogram analysis indicated the presence of five trypsin bands with molecular masses of ∼21, 25, 38, 40, and 66 kDa and two chymotrypsin bands with molecular masses of ∼29 and 34 kDa in SDS-PAGE. The optimum pH was 10.0 and optimum temperature was 50°C for proteolytic activity for the purified proteases. The proteases were inhibited by synthetic inhibitors such as PMSF, aprotonin, leupeptin, pefabloc, and antipain. TLCK and TPCK inhibited about 94 and 90% of trypsin and chymotrypsin activity, respectively, while EDTA, EGTA, E64, pepstatin, idoacetamide, and bestatin did not affect the enzymes. The purified enzymes exhibited high stability and compatibility with metal ions; oxidizing, reducing, and bleaching agents; organic solvents; and commercial detergents. Short life cycles, voracious feeding behavior, and production of multiple forms of proteases in the midgut with rapid catalytic activity and chemostability can serve H. armigera as an excellent alternative source of industrially important proteases for use as additives in stain removers, detergents, and other bio-formulations. Identification of enzymes with essential industrial properties from insect species could be a bioresource.

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Extracellular proteases of Halobacillus blutaparonensis strain M9, a new moderately halophilic bacterium

Cited by 18 publications

References 27 publications

Characterization of thermo-solvent stable protease fromHalobacillussp. CJ4 isolated from Chott Eldjerid hypersaline lake in Tunisia

Characterization of thermo-solvent stable protease fromHalobacillussp. CJ4 isolated from Chott Eldjerid hypersaline lake in Tunisia

Alkaline and Halophilic Protease Production by Bacillus luteus H11 and its Potential Industrial Applications

Alkaline serine proteases from Helicoverpa armigera: potential candidates for industrial applications

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