An extremely thermotolerant, alkaliphilic subtilisin-like protease from hyperthermophilic Bacillus sp. MLA64

Lagzian, Milad; Asoodeh, Ahmad

doi:10.1016/j.ijbiomac.2012.08.009

Cited by 22 publications

(13 citation statements)

References 50 publications

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“…This result is consistent with that observed in Bacillus sp. MLA64 (Lagzian & Asoodeh, 2012). In fact both strains kept their activities beyond 110°C.…”

Section: Effect Of Temperature On Protease Activitymentioning

confidence: 92%

Screening and characterization of thermo-active enzymes of biotechnological interest produced by thermophilic Bacillus isolated from hot springs in Tunisia

Thebti¹,

Riahi²,

Gharsalli³

2016

Acta Biochim Pol

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As part of the contribution to the global efforts in research of thermostable enzymes being of industrial interest, we focus on the isolation of thermophilic bacteria from Tunisian hot springs. Among the collection of 161 strains of thermophilic Bacillus isolated from different samples of thermal water in Tunisia, 20% are capable of growing at 100°C and the rest grow at 70°C or above. Preliminary activity tests on media supplemented with enzyme-substrates confirmed that 35 strains produced amylases, 37 - proteases, 43 - cellulases, 31 - xylanases and 37 - mannanases. The study of the effect of temperature on enzyme activity led to determination of the optimal temperatures of activities that vary between 60 and 100°C. Several enzymes were active at high temperatures (80, 90 and 100°C) and kept their activity even at 110°C. Several isolated strains producing enzymes with high optimal temperatures of activity were described for the first time in this study. Both strains B62 and B120 are producers of amylase, protease, cellulase, xylanase, and mannanase. The sequencing of 16S DNA identified isolated strains as Geobacillus kaustophillus, Aeribacillus pallidus, Geobacillus galactosidasus and Geobacillus toebii.

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“…This result is consistent with that observed in Bacillus sp. MLA64 (Lagzian & Asoodeh, 2012). In fact both strains kept their activities beyond 110°C.…”

Section: Effect Of Temperature On Protease Activitymentioning

confidence: 92%

Screening and characterization of thermo-active enzymes of biotechnological interest produced by thermophilic Bacillus isolated from hot springs in Tunisia

Thebti¹,

Riahi²,

Gharsalli³

2016

Acta Biochim Pol

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“…The protein concentration was determined with a BCA Protein Assay Kit (Sangon Biotech, Shanghai, China) using bovine serum albumin (BSA) as a reference. Protease activity was assayed according to the modified method . Briefly, the protease diluent (0.25 mL) was incubated with 0.75 mL of 50 mmol L −1 Tris–HCl buffer (pH 8.0) containing 1% (w/v) casein at 45°C for 10 min.…”

Section: Methodsmentioning

confidence: 99%

Purification, characterization and potential applications of a novel halotolerant metalloprotease from marine bacterium Vibrio sp. LA‐05

Zhang

Lang

et al. 2018

J of Chemical Tech & Biotech

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BACKGROUND: Many reported proteases showed low activity and stability under harsh operating conditions, e.g. high pH, salinity and surfactants, which hinders expansion of their applications in industry. Here, a novel halotolerant metalloprotease from marine bacterium Vibrio sp. LA-05 endowed with superior properties was purified and characterized, and its industrial application also evaluated. RESULTS:The protease was active and stable at 25-40 ∘ C and pH 6.0-10.0. Moreover, it was remarkably stable in high salt solution, tolerant to denaturing agents, organic solvents, surfactants and bleaching agents, and quite compatible and stable with many commercial detergents. Its residual activities were above 22% even after co-incubation with 20% NaCl for 480 h. Except Ariel and Tide, the residual activities were all above 55% after co-incubation with five other liquid detergents for 240 h. The corresponding theoretical analyses show that it is a metalloprotease containing 1 mol of zinc ion per mole of protease, the mature active protease predominantly in -helix form consists of 321 amino acids, and the central zinc ion along with 11 other conserved and crucial amino acid residues forms the catalytic domain. CONCLUSION: These excellent properties indicated that the protease has considerable potential as a bio-additive in the application of detergent formulations.

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“…Proteases are used in laundry detergents for over 50 years to facilitate release of proteinaceous materials in stains (blood and milk) and account for approximately 25% of total worldwide sales of enzymes . Thermostable alkaline proteases are having application in detergent industry as additive (Lagzian et al, 2012) In the present study, the authors produced protease enzyme from Bacillus thuringinsis SH-II-1A (Foda et al, 2013). The bacillus strain was obtained from natural source of slaughter house waste drainage soil of different locations (Joachim et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Isolation, purification and partial characterization of thermostable serine alkaline protease from a newly isolated Bacillus thuringinsis-SH-II-1A

Harer¹,

Bhatia²,

Bhatia³

2018

Afr. J. Biotechnol.

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In the present study, the isolation, purification and partial characterization of thermostable serine alkaline protease produced from Bacillus thuringinsis SH-II-1A was reported. The culture was isolated from soil of slaughter house waste and identified further from ribosomal sequence. The crude enzyme was purified by ammonium sulfate precipitation, dialysis and Sephadex G-200 gel permeation chromatography up to 17.04 fold with recovery of 8.47%. Relative molecular weight (67 kDa) of purified enzyme was observed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Maximum production of enzyme and cell biomass was observed for 48 h of incubation period at 45°C. Strong activity of enzyme was observed at pH 10 to 11; also stability of up to 2 and 20 h incubation at the same pH range confirms alkaline protease. Optimum temperature recorded for protease activity was 45°C, and 100% thermal stability up to 350 min of incubation was recorded. Among different natural substrates tried, casein was found as ideal substrate. Enzyme activity was strongly enhanced by metal ions like Ca 2+ , Mg 2+ and Mn 2+ whereas, 100% enzyme activity was inhibited by phenylmethylsulphonyl fluoride (PMSF), and up to 92% inhibition by diisopropyl fluorophosphates (DFP) confirmed serine protease. Detergent compatibility of the enzyme was studied in the presence of 10 mM CaCl 2 and 1 M glycine at 45°C. This indicates 80 to 100% stability for a period of 0.5 to 2.5 h incubation. Improved washing performance and removal of blood stains from the cotton cloth was observed when detergent Surf excel was used with enzyme. Overall, the observed properties of isolated protease conclude its commercial application in detergent and leather industries.

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An extremely thermotolerant, alkaliphilic subtilisin-like protease from hyperthermophilic Bacillus sp. MLA64

Cited by 22 publications

References 50 publications

Screening and characterization of thermo-active enzymes of biotechnological interest produced by thermophilic Bacillus isolated from hot springs in Tunisia

Screening and characterization of thermo-active enzymes of biotechnological interest produced by thermophilic Bacillus isolated from hot springs in Tunisia

Purification, characterization and potential applications of a novel halotolerant metalloprotease from marine bacterium Vibrio sp. LA‐05

Isolation, purification and partial characterization of thermostable serine alkaline protease from a newly isolated Bacillus thuringinsis-SH-II-1A

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