Production of Extracellular Anti-leukaemic Enzyme Lasparaginase from Marine Actinomycetes by Solidstate and Submerged Fermentation: Purification and Characterisation

Basha, N. Saleem; Rekha, Ravikumar Deepa; Komala, M; Selmi-Ruby, Samia

doi:10.4314/tjpr.v8i4.45230

Cited by 75 publications

(58 citation statements)

References 16 publications

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“…), and chemicals, namely, dithiothreitol (DTT), SDS, ethylene diamine tetra acetic acid (EDTA), and mercaptoethanol (ME) were used to determine their effect on enzymatic activity. This mixture was incubated at room temperature for 30 min, and then enzyme assay was performed [17][18][19]21].…”

Section: Effect Of Ph Temperature and Substrate Concentration On Enzmentioning

confidence: 99%

“…L-asparaginase enzyme purification was carried out from various organisms such as actinobacteria [14], Streptomyces halstedii [15], Streptomyces tendae [16], and marine Streptomyces spp. [17]. Different purification techniques such as salt precipitation [13,17] and column chromatography [13,14,18] were used during purification steps.…”

Section: Microbialmentioning

confidence: 99%

“…[17]. Different purification techniques such as salt precipitation [13,17] and column chromatography [13,14,18] were used during purification steps. Enzyme was characterized with respect to various parameters such as temperature, pH, and molecular weight.…”

Section: Microbialmentioning

confidence: 99%

“…Enzyme was characterized with respect to various parameters such as temperature, pH, and molecular weight. Furthermore, studies were undertaken to assess the effect of metal ions and kinetic parameters [14,15,[17][18][19][20][21][22][23]. Production and purification of extracellular L-asparaginase are easier compared to intracellular enzymes.…”

Section: Microbialmentioning

confidence: 99%

“…Absorbance measurement (A 280 ) method was used to estimate protein content. L-asparaginase active fractions were pooled and used for further analysis [13,17,21,23]. …”

Section: Enzyme Purificationmentioning

confidence: 99%

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Submerged fermentation, purification, and characterization of L-asparaginase from Streptomyces sp. isolated from soil

2018

J App Biol Biotech

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Actinomycetes are most valuable microbes because they are reported to produce different kinds of novel antibiotics and bioactive compounds. L-asparaginase enzyme is a chemotherapeutic agent used in the treatment of cancer. The present study reports production and characterization of purified L-asparaginase from an actinomycetes isolate. The isolate (A-164) was found to be a potent producer of L-asparaginase with an enzyme activity of 26.67 international unit (IU)/ml. Biochemical characterization of the isolate indicated that it belongs to genus Streptomyces. Laboratory scale enzyme production studies were undertaken using the standard medium. Further, the enzyme was purified by salt precipitation, anion exchange chromatography, and size exclusion chromatography. The purified enzyme exhibited the specific activity of 390 IU/mg with 60-fold purification and yield of 42% with a molecular weight of 34 KDa. The purified enzyme demonstrated the highest activity at pH 6.0 and temperature 35°C. The enzyme retained its activity till temperature of 50°C, indicating that it is a thermostable enzyme. A study on the effect of various additives on enzyme activity was also undertaken. The K m and V max values for the purified L-asparaginase were 0.065 mM and 20.80 IU/ml, respectively. The enzyme can further be used for health care and industrial applications.

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Section: Effect Of Ph Temperature and Substrate Concentration On Enzmentioning

confidence: 99%

Section: Microbialmentioning

confidence: 99%

Section: Microbialmentioning

confidence: 99%

Section: Microbialmentioning

confidence: 99%

“…Absorbance measurement (A 280 ) method was used to estimate protein content. L-asparaginase active fractions were pooled and used for further analysis [13,17,21,23]. …”

Section: Enzyme Purificationmentioning

confidence: 99%

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