Purification and partial characterization of a low molecular weight l-asparaginase produced from corn cob waste

Makky, Essam A.; Loh, Yean Chun; Karim, Md. Rezaul

doi:10.1016/j.bcab.2014.07.004

Cited by 23 publications

(25 citation statements)

References 15 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%

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%

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

Kaur¹,

Kumar²,

Kumar³

2017

Int. J. Res. Ayurveda Pharm.

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“…Other investigators reported that these range of temperature was the most suitable for enzyme activity [57,58]. Results illustrated in Figure (4) showed that the maximum activity of L-asparaginase was obtained at 37°C of the reaction mixture.…”

Section: Effect Of Temperaturementioning

confidence: 86%

“…According to these results, it has been concluded that 30 minutes of incubation was suitable for reaching maximum L-aspargenase activity. Different studies reported that the reaction time is an important factor for determination of the enzyme activity and it was preferred to use methods with short time incubation to determine the enzyme activity [57,58]. Moreover, there is a linear relationship between enzyme activity and reaction time [8,55].…”

Section: Effects Of Substrate Concentrationmentioning

confidence: 99%

“…Moreover, alkaline pH (8.0-10) showed optimum pH for most bacterial L-asparaginases activity [60,61]. It has been reported that most plant L-asparaginases have its maximum activity in alkaline pH, and was determined in pH range of 7.5, 8.0 and 8.5 due to the balance between L-aspartic acid and L-aspartate [11,58]. In general most plants show maximum enzyme activity at or near neutral pH [60].…”

Section: Effect Of Phmentioning

confidence: 99%

“…The enzyme activity was increased to 490 U/ml at this temperature. Moreover, L-asparaginase isolated from most organisms has maximum activity at 37°C [37,46,58]. The increase or decrease in reaction temperature above or below the optimum temperature cause a decrease in enzyme activity.…”

Section: Effect Of Temperaturementioning

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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Characterization of Penicillium crustosum l-asparaginase and its acrylamide alleviation efficiency in roasted coffee beans at non-cytotoxic levels

2021

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Purification and partial characterization of a low molecular weight l-asparaginase produced from corn cob waste

Cited by 23 publications

References 15 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

Characterization of Penicillium crustosum l-asparaginase and its acrylamide alleviation efficiency in roasted coffee beans at non-cytotoxic levels

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