Biochemical characterization and thermodynamic principles of purified l-Asparaginase from novel Brevibacillus borstelensis ML12

Mukherjee, Rupkatha; Bera, Debabrata

doi:10.1016/j.bcab.2021.102260

Cited by 5 publications

(3 citation statements)

References 47 publications

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“…was reported to have an optimum temperature of 40°C [40], and 37°C for Rhizobium etli [41] but did not exhibit resistance to other temperature ranges. L-asparaginase produced by Brevibacillus borstelensis ML12 [39] demonstrated stability at a temperature similar to that of A. niger studied in this work. These results highlight the distinct characteristic of L-asparaginase produced by A. niger, where it showed greater resistance to different temperatures compared to L-asparaginases produced by other microorganisms.…”

Section: Discussionsupporting

confidence: 59%

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Production, Characterization, Purification and Antitumor Activity of L-asparaginase from <em>Aspergillus niger</em>

da Silva Duarte,

de Carvalho Silva,

Assunção Borges

et al. 2024

Preprint

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Cervical cancer is caused by a persistent and high-grade infection, caused by the Human Papilloma Virus (HPV), which, when entering cervical cells, alters their physiology and generates serious lesions. HPV 18 - is among those most involved in carcinogenesis in this region, but there are still no drug treatments that cause cure or total remission of lesions caused by HPV. Knowing that L-Asparaginase is an amidohydrolase, which plays a significant role in the pharmaceutical industry, particularly in the treatment of specific cancers, due to its antitumor properties, some studies have demonstrated its cytotoxic effect against cervical cancer cells. However, the commercial version of this enzyme has side effects, such as hypersensitivity, allergic reactions and silent inactivation due to the formation of antibodies. To mitigate these adverse effects, several alternatives have been explored, including the use of L-asparaginase from other microbiological sources, which is the case with the use of the fungus Aspergillus niger, a high producer of L-asparaginase. The study investigated the influence of the type of fermentation, precipitant, purification, characterization and in vitro cytotoxicity of L-asparaginase. The results revealed that semisolid fermentation produced higher enzymatic activity and protein concentration of A. niger. The characterized enzyme showed excellent stability at pH 9.0, temperature of 50ºC, resistance to surfactants and metallic ions, and an increase in enzymatic activity was also noted with the organic solvent ethanol. Furthermore, it exhibited low cytotoxicity in GM and RAW cells, and significant cytotoxicity in HeLa cells. These findings indicate that L-asparaginase derived from Aspergillus niger may be a promising alternative for pharmaceutical production. Its attributes, including stability, activity and low toxicity in healthy cells, suggest that this modified enzyme could overcome challenges associated with antitumor therapy.

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Section: Discussionsupporting

confidence: 59%

“…Regarding temperature and stability, unlike other L-asparaginases produced by A. niger AKV-MKBU [23], Brevibacillus borstelensis ML12 [39] showed an optimum temperature of 30°C. Bacillus sp.…”

Section: Discussionmentioning

confidence: 87%

Production, Characterization, Purification and Antitumor Activity of L-asparaginase from <em>Aspergillus niger</em>

da Silva Duarte,

de Carvalho Silva,

Assunção Borges

et al. 2024

Preprint

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“…Traditional approaches of isolating and identifying L-ASNase from various sources were well investigated. It includes, Bacillus halotolerans OHEM18 (El-Fakharany et al 2022 ), Brevibacillus borstelensis ML12 (Mukherjee and Bera 2022 ). Further, efforts were also made to improve the properties of the existing enzymes or recombinantly reproduce it.…”

Section: Introductionmentioning

confidence: 99%

Biochemical characterization of extremozyme L-asparaginase from Pseudomonas sp. PCH199 for therapeutics

et al. 2023

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L-asparaginase (L-ASNase) from microbial sources is a commercially vital enzyme to treat acute lymphoblastic leukemia. However, the side effects associated with the commercial formulations of L-ASNases intrigued to explore for efficient and desired pharmacological enzymatic features. Here, we report the biochemical and cytotoxic evaluation of periplasmic L-ASNase of Pseudomonas sp. PCH199 isolated from the soil of Betula utilis, the Himalayan birch. L-ASNase production from wild-type PCH199 was enhanced by 2.2-fold using the Response Surface Methodology (RSM). Increased production of periplasmic L-ASNase was obtained using an optimized osmotic shock method followed by its purification. The purified L-ASNase was a monomer of 37.0 kDa with optimum activity at pH 8.5 and 60 ℃. It also showed thermostability retaining 100.0% (200 min) and 90.0% (70 min) of the activity at 37 and 50 ℃, respectively. The Km and Vmax values of the purified enzyme were 0.164 ± 0.009 mM and 54.78 ± 0.4 U/mg, respectively. L-ASNase was cytotoxic to the K562 blood cancer cell line (IC50 value 0.309 U/mL) within 24 h resulting in apoptotic nuclear morphological changes as examined by DAPI staining. Therefore, the dynamic functionality in a wide range of pH and temperature and stability of PCH199 L-ASNase at 37 ℃ with cytotoxic potential proves to be pharmaceutically important for therapeutic application.

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Thermostable bacterial L-asparaginase for polyacrylamide inhibition and in silico mutational analysis

Sundaram,

Kannan,

Chintaluri

et al. 2024

Int Microbiol

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Biochemical characterization and thermodynamic principles of purified l-Asparaginase from novel Brevibacillus borstelensis ML12

Cited by 5 publications

References 47 publications

Production, Characterization, Purification and Antitumor Activity of L-asparaginase from <em>Aspergillus niger</em>

Production, Characterization, Purification and Antitumor Activity of L-asparaginase from <em>Aspergillus niger</em>

Biochemical characterization of extremozyme L-asparaginase from Pseudomonas sp. PCH199 for therapeutics

Thermostable bacterial L-asparaginase for polyacrylamide inhibition and in silico mutational analysis

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