High activity alkaline protease from Conidiobolus coronatus (NCL 86.8.20): Enzyme production and compatibility with commercial detergents

Phadatare, Sangita U.; Deshpande, Vasanti; Srinivasan, M. C.

doi:10.1016/0141-0229(93)90119-m

Cited by 148 publications

(88 citation statements)

References 9 publications

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“…Studies on Streptomyces clavuligerus cultures for protease production showed that the amount of enzyme produced varies greatly with the culture media used (Porto et al, 1996). Proteases from Streptomyces origin offer an advantage as the mycelium can be easily removed by filtration (Phadatare et al, 1993). By using immobilized cells, the protease can be produced in a shorter reaction time.…”

Section: Introductionmentioning

confidence: 99%

OPTIMIZATION OF ALKALINE PROTEASE PRODUCTION BY <i>STREPTOMYCES AMBOFACIENS</i> IN FREE AND IMMOBILIZED FORM

Abdelwahed¹,

Danial

El‐Naggar³

et al. 2014

American Journal of Biochemistry and Biotechnology

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Section: Introductionmentioning

confidence: 99%

OPTIMIZATION OF ALKALINE PROTEASE PRODUCTION BY <i>STREPTOMYCES AMBOFACIENS</i> IN FREE AND IMMOBILIZED FORM

Abdelwahed¹,

Danial

El‐Naggar³

et al. 2014

American Journal of Biochemistry and Biotechnology

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“…Similar results were obtained by Ponsare et al (16) nitrogen sources like tryptone, peptone and yeast extract. Organic nitrogen sources have been found to be better nitrogen sources for growth and protease production in some organisms (2,15) and inorganic nitrogen sources (ammonium sulphate and potassium nitrate) gave better enzyme yields in other organisms (20).…”

Section: Effect Of Culture Conditions On Enzyme Secretionmentioning

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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“…To determine the stability of Bacillus sp SMIA-2 amylase in the presence of the different detergents, an amylase concentration of 1 mg.mL -1 was added in detergent solution and incubated at 50ºC for 60 minutes. Aliquots (0.5 mL) were taken at different time intervals and the residual activity determined at 90ºC and compared with the control sample incubated at 50ºC without any detergent (2,21). Fig.…”

Section: Evaluation Of Enzyme For Use In Detergent Formulationmentioning

confidence: 99%

Properties of an amylase from thermophilic Bacillus SP.

Carvalho

Corrêa

Silva

et al. 2008

Braz. J. Microbiol.

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α-Amylase production by thermophilic Bacillus sp strain SMIA-2 cultivated in liquid cultures containing soluble starch as a carbon source and supplemented with 0.05% whey protein and 0.2% peptone reached a maximum activity at 32 h, with levels of 37 U/mL. Studies on the amylase characterization revealed that the optimum temperature of this enzyme was 90ºC. The enzyme was stable for 1 h at temperatures ranging from 40-50ºC while at 90ºC, 66% of its maximum activity was lost. However, in the presence of 5 mM CaCl2, the enzyme was stable at 90ºC for 30 min and retained about 58% residual activity after 1 h. The optimum pH of the enzyme was found to be 8.5. After incubation of enzyme for 2 h at pH 9.5 and 11.0 was observed a decrease of about 6.3% and 16.5% of its original activity. At pH 6.0 the enzyme lost about 36% of its original activity. . In the presence of 2.0 M NaCl, 63% of amylase activity was retained after 2 h incubation at 45ºC. The amylase exhibited more than 70% activity when incubated for 1 h at 50ºC with sodium dodecyl sulphate. However, very little residual activity was obtained with sodium hypochlorite and with hydrogen peroxide the enzyme was completely inhibited. The compatibility of Bacillus sp SMIA-2 amylase with certain commercial detergents was shown to be good as the enzyme retained 86%, 85% and 75% of its activity after 20 min incubation at 50ºC in the presence of the detergent brands Omo ® , Campeiro ® and Tide ® , respectively.

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High activity alkaline protease from Conidiobolus coronatus (NCL 86.8.20): Enzyme production and compatibility with commercial detergents

Cited by 148 publications

References 9 publications

OPTIMIZATION OF ALKALINE PROTEASE PRODUCTION BY <i>STREPTOMYCES AMBOFACIENS</i> IN FREE AND IMMOBILIZED FORM

OPTIMIZATION OF ALKALINE PROTEASE PRODUCTION BY <i>STREPTOMYCES AMBOFACIENS</i> IN FREE AND IMMOBILIZED FORM

Production and properties of an extracellular protease from thermophilic Bacillus sp

Properties of an amylase from thermophilic Bacillus SP.

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