Factors Influencing L-Asparaginase Production by Staphylococci

Mikucki, J; Szarapińska-Kwaszewska, J; Krzemiński, Zbigniew

doi:10.1016/s0044-4057(77)80055-5

Cited by 6 publications

(2 citation statements)

References 25 publications

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“…Although vigorous aeration aided in gaining large amounts of biomass, nevertheless it reduced the enzyme yield. This might be caused by superficial denaturation of the enzyme protein, like that detected in guinea pig serum l- ASNase or due to the enzyme synthesis inhibition with oxygen as repressor (Mikucki et al 1977 ).…”

Section: Discussionmentioning

confidence: 99%

Optimization and characterization of antileukemic l-asparaginase produced by Fusarium solani endophyte

Osama,

El-Sherei,

Al-Mahdy

et al. 2023

AMB Expr

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Abstractl-asparaginase is an antileukemic enzyme that hydrolyzes l-asparagine into l-aspartic acid and ammonia, causing cell starvation and apoptosis in susceptible leukemic cell populations. Currently, l-asparaginase obtained from bacterial sources is constrained by several issues, including lesser productivity, stability, selectivity, and higher toxicity. The goal of this study is to provide fungal l-asparaginase with in-vitro effectiveness towards different human carcinomas. l-asparaginase from endophytic Fusarium solani (Gene Bank accession number MW209717) isolated from the roots of the medicinal plant Hedera helix L. was characterized and optimized experimentally for maximum l-asparaginase production in addition to evaluating its subsequent cytotoxicity towards acute monocytic leukemia and human skin fibroblast cell lines. The enzyme production was maximized using potato dextrose media (15.44 IU/ml/hr) at the 5th and 6th days of fermentation with incubation temperature 30 °C, 3% asparagine, 150–180 rpm agitation rate and a 250 ml flask. Enzyme characterization studies revealed that the enzyme maintained its thermal stability with temperatures up to 60 °C. However, its optimal activity was achieved at 35 °C. On measuring the enzymatic activity at various temperatures and different pH, maximum enzyme activity was recorded at 40 °C and pH 8 using 0.1 M asparagine concentration. Results also revealed promising cytotoxic activity against acute monocytic leukemia with IC50 = 3.66 µg/ml and low cytotoxicity against tested normal human skin fibroblast cell line which suggested that it might have selective toxicity, and consequently it could be used as a less toxic alternative to the current formulations.

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Section: Discussionmentioning

confidence: 99%

Optimization and characterization of antileukemic l-asparaginase produced by Fusarium solani endophyte

Osama,

El-Sherei,

Al-Mahdy

et al. 2023

AMB Expr

View full text Add to dashboard Cite

show abstract

“…Although the method provides good reproducibility results are inconsistent from different labs with the same sample. [105] Peterson RE [144] , perfomed a spectrophotometric method to estimate asparaginase activity using L-asparagine as substrate. Ammonia formed is measured at 500 nm and compared to a standard curve prepared from ammoniums sulphate solution as nitrogen source.…”

Section: Estimation Of L-asparaginase Activitymentioning

confidence: 99%

Overview on L-Asparaginase

Silpa¹

2017

WJPPS

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L-asparaginase is a potential anti-tumour enzyme that is known for its ability to reduce the amount of L-asparagine necessary for the tumor cells. It has been used against acute lymphoblastic leukemia and lymphosacoma. This review includes methods for isolation and screening of potential microbes for mass production of enzyme. The clinical use of L-asparaginase has been highlighted. Methods of strain improvement that can increase the efficiency of selected strains have also been described. Further sttempts have been also made to describe the various environmental and nutritional paramaeters affecting the enzyme production. The purification methods and also molecular sequencing of L-asparaginase is also discussed.

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A Comprehensive Review on l-Asparaginase and Its Applications

Batool

Makky

Jalal

et al. 2015

Appl Biochem Biotechnol

257

157

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L-asparaginase (LA) catalyzes the degradation of asparagine, an essential amino acid for leukemic cells, into ammonia and aspartate. Owing to its ability to inhibit protein biosynthesis in lymphoblasts, LA is used to treat acute lymphoblastic leukemia (ALL). Different isozymes of this enzyme have been isolated from a wide range of organisms, including plants and terrestrial and marine microorganisms. Pieces of information about the three-dimensional structure of L-asparaginase from Escherichia coli and Erwinia sp. have identified residues that are essential for catalytic activity. This review catalogues the major sources of L-asparaginase, the methods of its production through the solid state (SSF) and submerged (SmF) fermentation, purification, and characterization as well as its biological roles. In the same breath, this article explores both the past and present applications of this important enzyme and discusses its future prospects.

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Factors Influencing L-Asparaginase Production by Staphylococci

Cited by 6 publications

References 25 publications

Optimization and characterization of antileukemic l-asparaginase produced by Fusarium solani endophyte

Optimization and characterization of antileukemic l-asparaginase produced by Fusarium solani endophyte

Overview on L-Asparaginase

A Comprehensive Review on l-Asparaginase and Its Applications

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