Purification and Characterization of the Highly Thermostable Proteases from Bacillus stearothermophilus TLS33

Sookkheo, Boonyaras; Sinchaikul, Supachok; Phutrakul, Suree; Chen, Shui‐Tein

doi:10.1006/prep.2000.1282

Cited by 106 publications

(60 citation statements)

References 21 publications

(8 reference statements)

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“…The optimal pH and temperature of the commercial keratinase KerA from B. licheniformis PWD-1 were pH 7.5 and 50 °C, respectively. Keratinase KerP is similar to other bacterial keratinases in optimal conditions (Sangali and Brandelli 2000;Sookkheo et al 2000;Zhang et al 2016). Moreover, the stability of KerP suggested potential industrial applications.…”

Section: Effect Of Ph and Temperature On Kerp Activitymentioning

confidence: 74%

Characterization and overexpression of a novel keratinase from Bacillus polyfermenticus B4 in recombinant Bacillus subtilis

Dong

Chang

Chen

2017

Bioresour. Bioprocess.

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Background: Keratins, insoluble proteins with a robust structure, are a major component of epidermal tissue and appendages such as hair, feathers, nails, and walls. Keratinous waste mainly emanates from poultry and leather industries, thereby severely contaminating the environment. Keratinase can lyse proteins with robust cross-linked structures, such as keratin, and can hence be used in animal feed, fertilizer, detergent, leather, pharmaceutical, and cosmetic industries. Bacillus polyfermenticus B4, isolated from feather compost, secretes keratinase to metabolize feathers. Hence, this study aimed to investigate the enzymatic characteristics and recombinant production of keratinase from B. polyfermenticus B4.Methods: A novel keratinase KerP was isolated from B. polyfermenticus B4 and overexpressed in B. subtilis PT5, via the T7 promoter. Results:The highest keratinolytic activity of recombinant KerP was observed at pH 9.0 and 60 °C. Enzyme activity was enhanced with Fe

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Section: Effect Of Ph and Temperature On Kerp Activitymentioning

confidence: 74%

Characterization and overexpression of a novel keratinase from Bacillus polyfermenticus B4 in recombinant Bacillus subtilis

Dong

Chang

Chen

2017

Bioresour. Bioprocess.

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“…After incubation of crude enzyme solution at room temperature for 24h at pH values of 5.5, 8.0 and 9.0, it was observed a decrease of about 51%, 18% and 66% of its original activity, respectively. Sookkheo et al (22) reported to three proteases, S, N and B from thermophilic Bacillus stearothermophilus TLS33, optimum pH values of 8.5, 7.5, and 7.0, respectively. The protease S was active over a very broad pH range, and about 60% of proteolytic activity was still detectable at pH 6 and 10 in the presence of 5 mM CaCl 2 .…”

Section: Effect Of Ph On Activity and Stability Of Proteasementioning

confidence: 99%

Production and properties of an extracellular protease from thermophilic Bacillus sp

Nascimento¹,

Martins²

2004

Braz. J. Microbiol.

156

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Protease production by thermophilic Bacillus sp strain SMIA-2 cultivated in liquid cultures containing trisodium citrate reached a maximum in 9h, with levels of 1.93U/mg protein. The microorganism utilized several carbon sources for the production of protease. Starch was the best substrate, followed by trisodium citrate, citric acid and sucrose. Among the various organic and inorganic nitrogen sources, ammonium nitrate was found to be the best. Studies on the protease characterization revealed that the optimum temperature of this enzyme was 60ºC. The enzyme was stable for 2h at 30ºC, while at 40ºC and 80ºC, 14% and 84% of the original activities were lost, respectively. The optimum pH of the enzyme was found to be 8.0. After incubation of crude enzyme solution for 24h at pH 5.5, 8.0 and 9.0, a decrease of about 51%, 18% and 66% of its original activity was observed respectively. A stronger inhibitory effect was observed in the presence of K + , Hg 2+ and Cu 2+ . Hg + resulted in the complete loss of activity at 1mM concentrations. Activity was stimulated by Mn 2+ and Ca +2 , indicating that these ions had a functional role in the molecular structure of the enzyme.

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“…Among the four fungal strains A, G, H shows high protease activity and hence undergoes the large scale production of these strains at optimized pH 11 (Sookkheo et al, 2000) also reported the optimum pH for protease activity to be between 7.0 and 8.5 (Borris, 1987) reported alkaline protease production is found to be higher at pH 9-13 (Graph 1).…”

Section: Effect Of Ph On Protease Productionmentioning

confidence: 95%

Optimization of a Novel Alkaline Protease from Cashew Industrial Soil Associated Aspergillus niger

Parvathy¹,

Prabhakumari²,

Chandran³

et al. 2017

Int.J.Curr.Microbiol.App.Sci

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Purification and Characterization of the Highly Thermostable Proteases from Bacillus stearothermophilus TLS33

Cited by 106 publications

References 21 publications

Characterization and overexpression of a novel keratinase from Bacillus polyfermenticus B4 in recombinant Bacillus subtilis

Characterization and overexpression of a novel keratinase from Bacillus polyfermenticus B4 in recombinant Bacillus subtilis

Production and properties of an extracellular protease from thermophilic Bacillus sp

Optimization of a Novel Alkaline Protease from Cashew Industrial Soil Associated Aspergillus niger

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