Biochemical characterization and antitumor activity of three phase partitioned l-asparaginase from Capsicum annuum L.

Shanmugaprakash, M.; Jayashree, C.; Vinothkumar, V.; Senthilkumar, S.; Siddiqui, Sahabjada; Rawat, Vinita; Arshad, Mohammad

doi:10.1016/j.seppur.2014.12.036

Cited by 30 publications

(24 citation statements)

References 46 publications

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“…It is also clear from figure 1 that plant enzyme is more stable over pH range whereas the enzyme activity of microbial enzyme gradually decreases with the increasing pH. The results were similar to the fact that microbial enzyme shows highest activity at pH 8.0-10.0 18,19 . The optimum pH for B. subtilis (MTCC-2822) was 7.5 and 86 % activity was retained at pH 8.0 16 .…”

Section: Kinetic Characterization Of Enzymes Effect Of Phsupporting

confidence: 72%

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Comparative Characterization of L-Asparaginase Extracted From Plant and Microbial Sources

Kaur¹,

Kumar²,

Kumar³

2017

Int. J. Res. Ayurveda Pharm.

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L-asparaginase has been used for the treatment of different leukemia such as Acute Lymphoblastic Leukemia. Unlike normal cells leukemic cells cannot synthesize asparagine on their own. Therefore, when L-asparaginase is injected into blood it breaks down asparagine to aspartic acid and ammonia and hence tumor cells die due to asparagine starvation. It is produced by both microbes as well as plants. Therefore, in the present study we compared the L-asparaginase extracted from plants as well as microbes. Among the plants S. nigrum showed the highest activity (52 IU/ml) whereas among microbes B. subtilis (MTCC-121) had the highest activity (43.11 IU/ml). Both the enzymes were kinetically characterized and it was found that plant enzyme was stable over pH and temperature variations. The effect of metal ions was same on both the enzymes whereas chelators enhanced the plant enzyme whereas had no effect on microbial enzyme. Plant enzyme showed the highest activity and was more stable to the environmental variations as compared to microbial enzyme.

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Section: Kinetic Characterization Of Enzymes Effect Of Phsupporting

confidence: 72%

“…Lasparaginase extracted from P. vulgaris had the optimum temperature at 37°C 17 . Pectobacterium carotovorum and Pseudomonase aeruginosa were used for the production of Lasparaginase which also showed the highest activity at 40°C 21,19 .…”

Section: Effect Of Temperaturementioning

confidence: 99%

Comparative Characterization of L-Asparaginase Extracted From Plant and Microbial Sources

Kaur¹,

Kumar²,

Kumar³

2017

Int. J. Res. Ayurveda Pharm.

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“…These conditions include substrate concentration, reaction time, pH and temperature. Kozak and Jurga [53] and Shanmugaprakash, et al [13] reported the L-asparaginase activity may affect the change of these parameters. Therefore, It is possible to increase the enzyme activity by increasing substrate concentration, reaction, pH and temperature.…”

Section: Optimum Conditions For L-asparaginase Activitymentioning

confidence: 99%

“…L-asparaginase was detected in different plant species used as a source of protein for human food [4,9]. Recently, several investigators search some plant sources for L-asparaginase production to meet the increase continuous need for L-asparaginases [10][11][12][13]. L-asparagine is the most abundant metabolite for the storage and transport of nitrogen that is utilized in protein biosynthesis [14][15][16].…”

Section: Introductionmentioning

confidence: 99%

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Anticancer Activity of L-Asparaginase Produced from Vigna Unguiculata

Moharib

2018

World Scientific Research

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The present study aimed to production of purified L-asparaginase from Vignaunguiculata. Different physiological parameters, such as pH, temperature and incubation period, were optimized for growth and maximum L-asparaginase production. The optimum parameters were 37°C, 30 min and pH 8.5. Maximum L-asparaginase was 886.4U/ml with a specific activity of 1140.7 U/ml (31 fold purification with 28 %yield) were obtained at optimum conditions. The purified L-asparaginase produced from Vignaunguiculata was used for characterization and general properties. The effect of pH and temperature on L-asparaginase activity as well as stability at different pH and temperature were determined. The optimum pH 8.5 and 37ºC temperature on L-asparaginase showed 100% residual activity. Stability of pH around 8.5 and temperature 70ºC showed 90 and 78 % residual activity at 30 and 60 min respectively. The Lasparaginase showed high stability at alkaline pH (pH 8.5) when incubated for up to 60h.The molecular weight of the produced L-asparaginase was close to 68.5 kDa. Cytotoxic activity of Lasparaginase was examined in vitro using four carcinoma cell lines. L-aspargenase has higher effective in growth inhibition against HEPG2 and HCT-116 but lower against HELLA and MCF7 carcinoma cell lines. The data show that L-aspargenase has a higher cytotoxic activity against HEPG2 and HCT116, revealed higher percentage of cell death, indicating antitumor properties, and demonstrate direct effect on cancer cell proliferation of HEPG2 and HCT116. Therefore, Vignaunguiculata was considered to be a suitable source for production of Lasparaginase has higher activity and good stability. Purified L-asparaginase obtained from Vignaunguiculata could be employed in drug chemotherapy and treatment of cancer.

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Three-phase partitioning for the separation of proteins, enzymes, biopolymers, oils and pigments: a review

et al. 2022

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Biochemical characterization and antitumor activity of three phase partitioned l-asparaginase from Capsicum annuum L.

Cited by 30 publications

References 46 publications

Comparative Characterization of L-Asparaginase Extracted From Plant and Microbial Sources

Comparative Characterization of L-Asparaginase Extracted From Plant and Microbial Sources

Anticancer Activity of L-Asparaginase Produced from Vigna Unguiculata

Three-phase partitioning for the separation of proteins, enzymes, biopolymers, oils and pigments: a review

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