A comprehensive review on microbial l‐asparaginase: Bioprocessing, characterization, and industrial applications
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DOI: 10.1002/bab.1888
Abstract: l‐Asparaginase (E.C.3.5.1.1.) is a vital enzyme that hydrolyzes l‐asparagine to l‐aspartic acid and ammonia. This property of l‐asparaginase inhibits the protein synthesis in cancer cells, making l‐asparaginase a mainstay of pediatric chemotherapy practices to treat… read more here.
Keywords: microbial asparaginase; comprehensive review; asparaginase; characterization ... See more keywords
Post‐refolding stability considerations for optimization of in‐vitro refolding: L‐asparaginase as a case study
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DOI: 10.1002/biot.202200505
Abstract: L‐Asparaginase is an essential enzyme for the food and biopharmaceutical industry. The stability, however, of L‐asparaginase is widely known to be an issue. Commercial manufacturing of any biopharmaceutical involves hold‐ups during processing, and can result… read more here.
Keywords: post refolding; stability considerations; asparaginase; case ... See more keywords
Safety and effective salvage regimen comprising a novel combination of brentuximab vedotin, L‐asparaginase, and dexamethasone for refractory anaplastic large cell lymphoma, anaplastic lymphoma kinase negative
Sign Up to like & getrecommendations! Published in 2019 at "Hematological Oncology"
DOI: 10.1002/hon.2565
Abstract: Currently, the CHOP regimen (cyclophosphamide, vincristine, adriamycin, and prednisolone) is most commonly administered initial treatment for newly diagnosed peripheral T‐cell lymphoma (PTCL). However, PTCLs respond poorly to this regimen and thus have a poor prognosis.… read more here.
Keywords: lymphoma; oncology; therapy; asparaginase ... See more keywords
Antimicrobial‐resistant Neisseria gonorrhoeae can be targeted using inhibitors against evolutionary conservedl‐asparaginase
Sign Up to like & getrecommendations! Published in 2022 at "Journal of Cellular Biochemistry"
DOI: 10.1002/jcb.30271
Abstract: The emergence of multiple drug‐resistant “super gonorrhoea” complicates the management and treatment of Neisseria gonorrhoeae infections due to the progressive accumulation of mutations in the biological targets of frontline antimicrobials. Continuous evaluation and reporting of… read more here.
Keywords: neisseria gonorrhoeae; asparaginase; antimicrobial resistant; drug ... See more keywords
Bacterial l‐asparaginases for cancer therapy: Current knowledge and future perspectives
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DOI: 10.1002/jcp.28563
Abstract: l‐Asparaginases hydrolyzing plasma l‐asparagine and l‐glutamine has attracted tremendous attention in recent years owing to remarkable anticancer properties. This enzyme is efficiently used for acute lymphoblastic leukemia (ALL) and lymphosarcoma and emerged against ALL in… read more here.
Keywords: therapy; bacterial asparaginases; cancer; asparaginase ... See more keywords
Production and optimization of l‐asparaginase by Streptomyces koyangensis SK4 isolated from Arctic sediment
Sign Up to like & getrecommendations! Published in 2022 at "Journal of Basic Microbiology"
DOI: 10.1002/jobm.202200116
Abstract: Actinomycetes isolated from the Arctic sediment were evaluated for the production of the enzyme l‐asparaginase, an enzyme used to treat acute lymphoblastic leukemia. The most potent strain Streptomyces koyangensis SK4 was selected for l‐asparaginase enzyme… read more here.
Keywords: arctic sediment; asparaginase; production; koyangensis sk4 ... See more keywords
Microbial l-asparaginase: purification, characterization and applications
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DOI: 10.1007/s00203-020-01814-1
Abstract: l-asparaginase (E.C.3.5.1.1) is an important enzyme that has been purified and characterized for over decades to study and evaluate its anti-carcinogenic activity against different lymphoproliferative disorders such as acute lymphoblastic leukemia (ALL) and Hodgkin’s lymphoma.… read more here.
Keywords: asparaginase purification; microbial asparaginase; characterization applications; purification ... See more keywords
Interferences that impact measuring optimal l-asparaginase activity and consequent errors interpreting these data
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DOI: 10.1007/s00253-019-09890-0
Abstract: Abstractl-asparaginase is an enzyme produced by microorganisms, plants, and animals, which is used clinically for the treatment for acute lymphoblastic leukemia (ALL) and, in the food industry, to control acrylamide formation in baked foods. The… read more here.
Keywords: impact measuring; measuring optimal; asparaginase activity; interferences impact ... See more keywords
In silico characterization of a cyanobacterial plant-type isoaspartyl aminopeptidase/asparaginase
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DOI: 10.1007/s00894-018-3635-6
Abstract: Asparaginases are found in a range of organisms, although those found in cyanobacteria have been little studied, in spite of their great potential for biotechnological application. This study therefore sought to characterize the molecular structure… read more here.
Keywords: silico characterization; cyanobacterial plant; characterization cyanobacterial; asparaginase ... See more keywords
Decreasing the immunogenicity of Erwinia chrysanthemi asparaginase via protein engineering: computational approach
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DOI: 10.1007/s11033-019-04921-5
Abstract: Immunogenicity of therapeutic proteins is one of the main challenges in disease treatment. l-Asparaginase is an important enzyme in cancer treatment which sometimes leads to undesirable side effects such as immunogenic or allergic responses. Here,… read more here.
Keywords: protein; erwinia chrysanthemi; immunogenicity; chrysanthemi asparaginase ... See more keywords
Genotoxic activity of l-asparaginase produced by Streptomyces ansochromogenes UFPEDA 3420
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DOI: 10.1007/s11274-019-2612-2
Abstract: Abstractl-asparaginase is an enzyme capable of hydrolyzing the substrate asparagine in aspartic acid and ammonia. Due to this mechanism of action observed, l-asparaginase is widely used in the treatment of Acute Lymphoblastic Leukemia, since these… read more here.
Keywords: ansochromogenes ufpeda; produced streptomyces; asparaginase produced; ufpeda 3420 ... See more keywords