Influence of alkali-treated cornsteep liquor containing medium on protein A production byStaphylococcus aureus

Muley, Ravindra; Sarkar, Sabyasachi; Ambedkar, S. S.; Naik, Suresh R.

doi:10.1007/bf02815537

Cited by 7 publications

(4 citation statements)

References 16 publications

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“…1) is present in many animal tissues, bacteria, plants, and in the serum of certain rodents, but not in mankind. L-Asparaginase is produced by a large number of microorganisms that include E. coli (Derst et al, 1994;Mercado & Arenas, 1999), Erwinia cartovora (Maladkar et al, 1993;Aghaiypour et al, 2001), Enterobacter aerogenes (Mukherjee et al, 2000), Corynebacterium glutamicum (Juan et al, 1990), Candida utilis (Kil et al, 1995), Staphylococcus aureus (Muley et al, 1998), Thermus thermophilus (Prista & Kyridio, 2001), and Pisum sativum (Siechiechowcicz & Ireland, 1989). L-Asparaginase catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia.…”

Section: Introductionmentioning

confidence: 99%

Production, Isolation, and Purification of L-Asparaginase from Pseudomonas Aeruginosa 50071 Using Solid-state Fermentation

Elbessoumy¹,

Sarhan²,

Mansour³

2004

BMB Reports

124

102

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The L-asparaginase (E. C. 3. 5. 1. 1) enzyme was purified to homogeneity from Pseudomonas aeruginosa 50071 cells that were grown on solid-state fermentation. Different purification steps (including ammonium sulfate fractionation followed by separation on Sephadex G-100 gel filtration and CM-Sephadex C50) were applied to the crude culture filtrate to obtain a pure enzyme preparation. The enzyme was purified 106-fold and showed a final specific activity of 1900 IU/mg with a 43% yield. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of the purified enzyme revealed it was one peptide chain with M r of 160 kDa. A Lineweaver-Burk analysis showed a K m value of 0.147 mM and V max of 35.7 IU. The enzyme showed maximum activity at pH 9 when incubated at 37ºC for 30 min. The amino acid composition of the purified enzyme was also determined.

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Section: Introductionmentioning

confidence: 99%

Production, Isolation, and Purification of L-Asparaginase from Pseudomonas Aeruginosa 50071 Using Solid-state Fermentation

Elbessoumy¹,

Sarhan²,

Mansour³

2004

BMB Reports

124

102

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“…The enzyme has been characterized from many bacterial genera [6]. In addition to E. coli [7], many other microorganisms are capable of producing L-asparaginase such as Erwinia carotovora [8], Erwinia chrysanthemi [9], Enterobacter aerogenes [10], Staphylococcus aureus [11], Thermus thermophilus [12], and Pseudomonas aeruginosa [13].…”

Section: Introductionmentioning

confidence: 99%

Purification of Dickeya solanil-Asparaginase and Study of the Influence of TiO2 and ZnO Nanoparticles on Its Enzymatic Activity

et al. 2019

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L-asparaginase catalyzes the hydrolysis of L-asparagine to L-aspartate and ammonia. In the present study, we describe the production, purification, and preliminary characterization of Dickeya solani L-asparaginase. The purification of L-asparaginase was done using ion-exchange chromatography on HiTrap Q-Sepharose Fast Flow followed by FPLC-gel filtration chromatography on Superdex 75 pg. The presence of the enzyme was confirmed by enzymatic activity measurements along with SDS-PAGE analysis. The purified L-asparaginase was shown to exhibit specificity towards L-asparagine, while being inactive against L-glutamine. This data allows us to suggest that the L-asparaginase from Dickeya solani might be clinically more relevant than, e.g., the L-asparaginase isolated from E. coli which hydrolyzed also L-glutamine and produces L-glutamate, a neurotoxic agent. We also demonstrated that the enzymatic activity was enhanced in the presence of TiO 2 and ZnO nanoparticles, making them good candidates to improve L-asparaginase activity. Indeed, the results obtained show that the TiO 2 nanoparticles increased the activity of L-asparaginase by a factor of 6.0 while the ZnO nanoparticles increased it twice.

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“…Due to its prompt therapeutic potential, screening of microbial sources for asparaginase activity has been greatly intensified and well documented in E . coli [4–6], Erwinia carotovora [7, 8], Enterobacter aerogenes [9], Corynebacterium glutamicum [10], Candida utilis [11], Serratia marcescens [12], Staphylococcus aureus [13], and Thermus thermophilus [14]. In addition, actinomycetes act as potential candidates for the production of L-asparaginase.…”

Section: Introductionmentioning

confidence: 99%

A Study on L-Asparaginase ofNocardia levisMK-VL_113

Kavitha

Vijayalakshmi

2012

The Scientific World Journal

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An enzyme-based drug, L-asparaginase, was produced byNocardia levisMK-VL_113 isolated from laterite soils of Guntur region. Cultural parameters affecting the production of L-asparaginase by the strain were optimized. Maximal yields of L-asparaginase were recorded from 3-day-old culture grown in modified asparagine-glycerol salts broth with initial pH 7.0 at temperature30∘C. Glycerol (2%) and yeast extract (1.5%) served as good carbon and nitrogen sources for L-asparaginase production, respectively. Cell-disrupting agents like EDTA slightly enhanced the productivity of L-asparaginase. Ours is the first paper on the production of L-asparaginase byN. levis.

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Influence of alkali-treated cornsteep liquor containing medium on protein A production byStaphylococcus aureus

Cited by 7 publications

References 16 publications

Production, Isolation, and Purification of L-Asparaginase from Pseudomonas Aeruginosa 50071 Using Solid-state Fermentation

Production, Isolation, and Purification of L-Asparaginase from Pseudomonas Aeruginosa 50071 Using Solid-state Fermentation

Purification of Dickeya solanil-Asparaginase and Study of the Influence of TiO2 and ZnO Nanoparticles on Its Enzymatic Activity

A Study on L-Asparaginase ofNocardia levisMK-VL_113

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