Microbial proteinases

Kalisz, Henryk M.

doi:10.1007/bfb0047944

Cited by 114 publications

(93 citation statements)

References 220 publications

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“…The protease from Endothia parasitica was found to be inactive within 5 min at 60ºC (8). The present protease from S. clavuligerus exhibited greater thermal stability than the enzymes from other fungal sources, suggesting possible biotechnological and industrial impotance.…”

Section: Effect Of Temperature On Activity and Stability Of Proteasementioning

confidence: 76%

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Partial Characterization of Proteases From Streptomyces Clavuligerus Using an Inexpensive Medium

Moreira

Cavalcanti

Duarte

et al. 2001

Braz. J. Microbiol.

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The partial characterization of extracellular proteases from Streptomyces clavuligerus NRRL 3585 and 644 mutant was investigated. The enzyme production was carried out in batch fermentation using soy bean filtrate as nitrogen source. Maximum activity was obtained after 96h of fermentation with an initial pH of 7.0. The enzyme was partially purified by ammonium sulphate precipitation. Enzymes from the two strains retained 37% of their initial activities at pH 8.0 after 2 h incubation at 25ºC. Enzyme half-life at pH 8.0 and 60ºC was 40.30 and 53.32 min, respectively for both strains (partially purified extract). The optimum pH was obtained at pH 7.0-8.0 and 8.4 for enzymes produced for 3585 and 644 strains (crude extract), respectively, and 8.4 and 8.0 for enzymes from the partially purified extract 3585 and 644 strains, respectively. The optimum temperature for the crude extract was 21ºC for both strains. However, for the partially preparation the optimum temperature was 50ºC and 40°C for S. clavuligerus NRRL 3585 and 644 strains respectively.

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Section: Effect Of Temperature On Activity and Stability Of Proteasementioning

confidence: 76%

“…Optimum temperature for thermostable proteases by Aspergillus niger and Aspergillus saitoi have been found to be 60º and 30ºC, respectively (8,18).…”

Section: Palavras-chavementioning

confidence: 99%

Partial Characterization of Proteases From Streptomyces Clavuligerus Using an Inexpensive Medium

Moreira

Cavalcanti

Duarte

et al. 2001

Braz. J. Microbiol.

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“…It was stable up to 50°C, but lost almost 90% of its activity at 60°C after 1 h incubation at pH 3·0. The optimum temperature for enzymes from Aspergillus saitoi and Rhizopus oligosporus were 30°C and 40°C, respectively (Kalisz 1988 ;Farley and Ikasari 1992). Thermostability of acid proteinases from A. saitoi was 50°C at pH 3·0 for 15 min (Tanaka et al 1977).…”

Section: Effect Of Temperaturementioning

confidence: 99%

Purification and characterization of acid proteinase from Neosartorya fischeri var. spinosa IBT 4872

Hang

1998

Lett Appl Microbiol

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N G. 1998. An acid proteinase from Neosartorya fischeri var. spinosa IBT 4872 was purified 38-fold with a yield of 11% by ultrafiltration, ammonium sulphate fractionation, Sephadex-G200 gel filtration, DEAE-Sephadex anion exchange chromatography, and hydroxyapatite chromatography. The enzyme was most active at pH 3·0 and 50°C and had a molecular weight of 45 kDa, as determined by SDS-PAGE. It was stable over a pH range of 3·0 to 6·0 and exhibited thermal stability up to 50°C. The Km value for haemoglobin was 0·44% (w/v). The activity was inhibited by pepstatin, suggesting that the enzyme is an aspartic proteinase.

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“…Subtilisin is one of the most extensively studied of all bacterial proteins, due to its commercial importance (Ward, 1985). This protease is produced at the onset of sporulation and a complex network of genes and regulators, which regulates the transition state of protein (Kalisz, 1988), controls the expression. They are generally secreted extracellularly for the purpose of scavenging nutrients (Graycar, 1999).…”

Section: Introductionmentioning

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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Microbial proteinases

Cited by 114 publications

References 220 publications

Partial Characterization of Proteases From Streptomyces Clavuligerus Using an Inexpensive Medium

Partial Characterization of Proteases From Streptomyces Clavuligerus Using an Inexpensive Medium

Purification and characterization of acid proteinase from Neosartorya fischeri var. spinosa IBT 4872

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

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