New alkaline protease from Nocardiopsis sp.: partial purification and characterization

Moreira, Keila Aparecida; Porto, T. S.; Teixeira, Marie; Porto, Tatiana Souza; Filho, J. L. Lima

doi:10.1016/s0032-9592(02)00312-6

Cited by 38 publications

(26 citation statements)

References 21 publications

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“…Many studies have investigated the effect of ions on the physicochemical characteristics of milk-clotting by adding NaCl or CaCl 2 (VAN HOOYDONK; HAGEDOORN ;BOERRIGTER, 1986;FOX, 1997), but few have demonstrated that ions had a significant influence (FAMELART; LE GRAET; RAULOT, 1999). These results agree with Moreira et al (2003), who observed no significant inhibition of the activity of a protease from Nocardiopsis sp. owing to metal ions but determined that the protease activity can be increased in the presence of the K + .…”

Section: Effect Of Ph On Enzyme Activity and Stabilitysupporting

confidence: 93%

Potential of quixaba (Sideroxylon obtusifolium) latex as a milk-clotting agent

et al. 2013

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Section: Effect Of Ph On Enzyme Activity and Stabilitysupporting

confidence: 93%

Potential of quixaba (Sideroxylon obtusifolium) latex as a milk-clotting agent

et al. 2013

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“…The model evaluates the effect of each independent variable to a response. The mathematical relationship of the independent variables and the response can be calculated by the quadratic polynomial equation (Moreira et al, 2003). The computation was carried out by multiple regression analysis making use of the least squares method.…”

Section: Response Surface Methodologymentioning

confidence: 99%

Optimization of medium for the production of subtilisin from Bacillus subtilis MTCC 441

Navaneeth¹,

Bhuvanesh²,

Bhaskar³

et al. 2009

Afr. J. Biotechnol.

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Subtilisins (E.C.3.4.21.62) are alkaline proteases that are secreted by members of the genus Bacillus. They are serine proteases that exhibit high specific activity on proteinaceous substrates, function optimally at moderate temperatures, and are stable under alkaline conditions. Thus the use of subtilisin as an enzyme additive could help in development of quality laundry detergents. In this work the subtilisin production from Bacillus subtilis (MTCC 441) was improved by altering and optimizing the media components. This alteration was brought up by process development strategy. The effect of yeast extract, casein, peptone and sodium chloride on subtilisin production was studied and were optimized using Box Behnken Design. The optimal growth conditions for B. subtilis MTCC 441 were found to 37 o C, and pH 7.5. The optimal media composition for subtilisin production was found to be yeast extract at 6.75 g/L, peptone at 4.41 g/L, sodium chloride at 6.08 g/L, casein at 10.75 g/L with glucose at 5 g/L. The predicted and observed response were 181.00 U/mg (with desirability =0.87) and 185.70 U/mg, respectively.

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“…This enzyme accounts for 40% of the total worldwide enzyme sales. It is expected to be an upward trend in the use of alkaline proteases in the future Moreira et al, 2003). 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 .…”

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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New alkaline protease from Nocardiopsis sp.: partial purification and characterization

Cited by 38 publications

References 21 publications

Potential of quixaba (Sideroxylon obtusifolium) latex as a milk-clotting agent

Potential of quixaba (Sideroxylon obtusifolium) latex as a milk-clotting agent

Optimization of medium for the production of subtilisin from Bacillus subtilis MTCC 441

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

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