Applications of alkaline protease fromConidiobolus in animal cell culture

Chiplonkar, J. M.; Gangodkar, Shobha; Wagh, U. V.; Ghadge, Ghanashyam D.; Rele, M. V.; Srinivasan, M. C.

doi:10.1007/bf01040206

Cited by 19 publications

(6 citation statements)

References 3 publications

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“…Alkaline proteases from Conidiobolus species and their applications in animal cell culture [17], detergent [14,18], resolution of amino acids [10] and leather processing [5] have been reported from this laboratory. Alkaline protease secreted by the present strain of C. coronatus has been extensively evaluated in tanneries and finds applications in pre-tanning operations in leather manufacture [5].…”

Section: Discussionmentioning

confidence: 99%

Optimization and scale up of production of alkaline protease from Conidiobolus coronatus

Laxman

Sonawane

et al. 2005

Process Biochemistry

100

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Section: Discussionmentioning

confidence: 99%

Optimization and scale up of production of alkaline protease from Conidiobolus coronatus

Laxman

Sonawane

et al. 2005

Process Biochemistry

100

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“…Alkaline proteases from Aspergillus species are used in leather treatment, endo-and exoproteases from A. oryzae have been used to modify wheat gluten, an insoluble protein, by limited proteolysis facilitating its handling and machining and these proteases are also used in the health treatments (Chiplonkar et al 1985). Recently, we reported the best conditions for the alkaline protease production by this strain (Tremacoldi and Carmona 2005).…”

Section: Introductionmentioning

confidence: 98%

Purification and properties of an alkaline protease of Aspergillus clavatus

Tremacoldi

Monti

Selistre-de-Araújo

et al. 2006

World J Microbiol Biotechnol

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An extracellular alkaline serine protease has been purified from a strain of Aspergillus clavatus, to apparent homogeneity, by ammonium sulfate precipitation and chromatography on Sephadex G-75. Its molar mass, estimated by SDS-PAGE, was 35 kDa. Maximum protease activity was observed at pH 9.5 and 40°C. The enzyme was active between pH 6.0 and 11.0 and was found to be unstable up to 50°C. Calcium at 5 mM increased its thermal stability. The protease was strongly inhibited by PMSF and chymostatin as well as by SDS, Tween 80 and carbonate ion. Substrate specificity was observed with N-p-Tos-Gly-Pro-Arg-p-nitroanilide and N-Suc-Ala-Ala-Ala-p-nitroanilide being active substates. Parts of the amino acid sequence were up to 81% homologous with those of several fungal alkaline serine proteases.

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“…) are the most important group of commercial enzymes (Kumar & Takagi 1999). Alkaline proteases from Aspergillus species are used in leather treatment (Godfrey & West 1996), endo-and exoproteases from A. oryzae have been used to modify wheat gluten, an insoluble protein, by limited proteolysis thereby facilitating its handling and machining, and these proteases are also important in the pharmaceutical industry (Chiplonkar et al 1985). Genes encoding alkaline proteases from A. oryzae, A. sojae, A. fumigatus, A. flavus and A. nidulans have been cloned, sequenced and expressed (Hodgson 1994).…”

Section: Introductionmentioning

confidence: 99%

Production of extracellular alkaline proteases by Aspergillus clavatus

Tremacoldi

Carmona

2005

World J Microbiol Biotechnol

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The production of extracellular alkaline proteases from Aspergillus clavatus was evaluated in a culture filtrate medium, with different carbon and nitrogen sources. The fungus was cultivated at three different temperatures during 10 days. The proteolytic activity was determined on casein pH 9.5 at 37°C. The highest alkaline proteolytic activity (38 U/ml) was verified for culture medium containing glucose and casein at 1% (w/v) as substrates, obtained from cultures developed at 25°C for 6 days. Cultures developed in Vogel medium with glucose at 2% (w/v) and 0.2% (w/v) NH 4 NO 3 showed higher proteolytic activity (27 U/ml) when compared to the cultures with 1% of the same sugar. Optimum temperature was 40°C and the half-lives at 40, 45 and 50°C were 90, 25 and 18 min, respectively. Optimum pH of enzymatic activity was 9.5 and the enzyme was stable from pH 6.0 to 12.0.

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Applications of alkaline protease fromConidiobolus in animal cell culture

Cited by 19 publications

References 3 publications

Optimization and scale up of production of alkaline protease from Conidiobolus coronatus

Optimization and scale up of production of alkaline protease from Conidiobolus coronatus

Purification and properties of an alkaline protease of Aspergillus clavatus

Production of extracellular alkaline proteases by Aspergillus clavatus

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