A Study on L-Asparaginase of<i>Nocardia levis</i>MK-VL_113

Kavitha, Alapati; Vijayalakshmi, M.

doi:10.1100/2012/160434

Cited by 15 publications

(7 citation statements)

References 25 publications

(32 reference statements)

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“…This result was similar to the work of Verma [29] who reported the importance of yeast extract at low concentration for cell growth and L-asparaginase synthesis. In contrast, Kavitha and Vijayalakshimi [32] showed that 1.5 % yeast extract concentration was optimum for L-asparaginase production. Also, Deokar et al [25] showed that 1.74 % yeast extract concentration was optimum for L-asparaginase synthesis by Erwinia carotovora.…”

Section: Discussionmentioning

confidence: 90%

Screening, Production and Optimization of L-Asparaginase From Soil Bacteria Isolated in Ibadan, South-western Nigeria

Wakil¹,

Adelegan²

2015

J. Basic Appl. Sci.

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L-Asparaginase producing bacteria were isolated from soil samples under optimum conditions using submerged fermentation. Their abilities to produce asparaginase at different pH, temperature, incubation temperature, utilization of different carbon and nitrogen sources as well as their specific conditions for optimal activity were also investigated. Streptococcus spp. D1, Bacillus polymyxa and Streptococcus spp. D2 showed optimum asparaginase production at pH 8 with activities of 11.6 U/ml, 8.8 U/ml and 7.9 U/ml respectively. The pH 7 was observed as optimum pH for Bacillus firmus (8.8 U/ml) while optimum pH 6 was observed for Bacillus circulans and Paenibacillus validus. Maximum L-asparaginase productivity was attained at a temperature of 45°C by Bacillus firmus, Streptococcus sp. D1 and Bacillus circulans with activity of 4.6 U/ml, 5.6 U/ml and 3.8 U/ml respectively while 35°C incubation temperature was optimum for Paenibacillus validus and Bacillus polymyxa with enzyme activity of 6.2 U/ml and 6.1 U/ml respectively. Mannitol supported the maximum asparaginase production of Bacillus circulans, Streptococcus sp. D2 and Bacillus polymyxa while maltose was observed as the best carbon source for Streptococcus sp. D1 and Bacillus firmus; and sucrose for Paenibacillus validus. The optimum nitrogen source was casein for Bacillus circulans (7.57 U/ml) and Streptococcus spp. D1 (6.19 U/ml), Yeast extract for Bacillus polymyxa (7.037 U/ml) and Bacillus firmus (5.368 U/ml) while NaNO3 supported optimum L-asparaginase production for Streptococcus sp. D2 (6.006 U/ml) and Paenibacillus validus (4.754 U/ml). At optimum conditions, Bacillus polymyxa had the highest (4.835 U/ml) while Bacillus circulans had the least (2.981 U/ml) asparaginase activity. In all, the bacterial isolates prefers slightly alkaline to alkaline medium (pH 6-8) for optimum asparaginase production.

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Section: Discussionmentioning

confidence: 90%

Screening, Production and Optimization of L-Asparaginase From Soil Bacteria Isolated in Ibadan, South-western Nigeria

Wakil¹,

Adelegan²

2015

J. Basic Appl. Sci.

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“…In order to demonstrate the production of L-Asparaginase, strain CA01 was cultured on ADS medium. The same medium is used in many studies related to the production and characterization of L-Asparaginase (25,26,27,28,29,30,31). The production yield of the enzyme depends substantially on the physicochemical conditions of the bacterial culture which implies an optimization of all the factors that can influence this production.…”

Section: Discussionmentioning

confidence: 99%

Characterization and optimization of extracellular L-Asparaginase production by selected Actinomycete strain isolated from an algerian wheat bran

Chergui¹,

Kecha

Tighrine³

et al. 2018

Cell Mol Biol (Noisy-le-grand)

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L-Asparaginase is an enzyme that hydrolyses the amino acid L-Asparagine into aspartic acid and ammonia. As a medication, L-Asparaginase is used in chemotherapy to treat acute lymphoblastic leukaemia by depleting circulating Asparagine and depriving tumor cells. Interest in Actinomycetes as potential producers of antibiotics and enzymes encouraged us to investigate an isolated strain (CA01) from soft wheat bran.The Actinomycete strain was characterized based on its morphological and biochemical characteristics and selected due to a proved promising ability to produce L-Asparaginase optimized in both solid and liquid media cultures.The conditions of enzyme production were standardized according to a one-factor-at-a-time (OFAT) experimental design.To obtain optimal medium combination, a Box-Behnken Response Surface Methodology (RSM) has been adopted by choosing the most influential factors. The optimal conditions for the enzyme production were (g/l): L-Asparagine 10.7; Glucose 2.7; starch 7, in based medium containing (g/l): K 2 HPO 4 0.5; MgSO 4 , 7H 2 O 0.1, corresponding to an optimal enzymatic activity of 8.03 IU/ml at 27.83°C. The maximum production of enzyme was reached on the sixth day of experiment. The ANOVA test (P value ˂ 0.05) and adjusted R 2 values close to the experimental R 2 show that the obtained model of the active L-Asparaginase of CA01 strain production is significant with the following linear terms: temperature, substrate concentration, Glucose concentration and there squared.

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“…The purified enzyme exhibited the specific activity of 390 IU/mg with 60-fold purification and yield of 42% [ Table 2]. Various researchers have used different techniques for purification of L-asparaginase enzyme from different actinomycetes and obtained specific activity in the range of 660-5035 IU/mg and yield in the range of 25-60% [14][15][16][17]21]. …”

Section: Production and Purification Of L-asparaginasementioning

confidence: 99%

“…Various researchers have reported production of L-asparaginase by Streptomyces spp. such as S. halstedii [15], S. tendae [16], and Streptomyces ginsengisoli [35].…”

Section: Isolation and Characterization Of Actinomycetes And Screeninmentioning

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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A Study on L-Asparaginase ofNocardia levisMK-VL_113

Cited by 15 publications

References 25 publications

Screening, Production and Optimization of L-Asparaginase From Soil Bacteria Isolated in Ibadan, South-western Nigeria

Screening, Production and Optimization of L-Asparaginase From Soil Bacteria Isolated in Ibadan, South-western Nigeria

Characterization and optimization of extracellular L-Asparaginase production by selected Actinomycete strain isolated from an algerian wheat bran

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

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