Extraction of Extracellular<scp>L</scp>-Asparaginase from<i>Candida utilis</i>

Kil, Ji-Oeun; Kim, Gi-Nahm; Park, Inshik

doi:10.1271/bbb.59.749

Cited by 34 publications

(22 citation statements)

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“…The presence of an extracellular L-asparaginase in C. utilis after growth without ammonium sulfate was demonstrated by Kil et al (1995) and is confirmed here. In S. cerevisiae, Asp3 is known to convert asparagine into aspartate and ammonia, and to be regulated by nitrogen catabolite repression (Kim et al, 1988;Huang et al, 2010).…”

Section: Discussionsupporting

confidence: 82%

Growth-dependent secretome of Candida utilis

et al. 2011

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Recently, the food yeast Candida utilis has emerged as an excellent host for production of heterologous proteins. Since secretion of the recombinant product is advantageous for its purification, we characterized the secreted proteome of C. utilis. Cells were cultivated to the exponential or stationary growth phase, and the proteins in the medium were identified by MS. In parallel, a draft genome sequence of C. utilis strain DSM 2361 was determined by massively parallel sequencing. Comparisons of protein and coding sequences established that C. utilis is not a member of the CUG clade of Candida species. In total, we identified 37 proteins in the culture solution, 17 of which were exclusively present in the stationary phase, whereas three proteins were specific to the exponential growth phase. Identified proteins represented mostly carbohydrate-active enzymes associated with cell wall organization, while no proteolytic enzymes and only a few cytoplasmic proteins were detected. Remarkably, cultivation in xylose-based medium generated a protein pattern that diverged significantly from glucose-grown cells, containing the invertase Inv1 as the major extracellular protein, particularly in its highly glycosylated S-form (slow-migrating). Furthermore, cultivation without ammonium sulfate induced the secretion of the asparaginase Asp3. Comparisons of the secretome of C. utilis with those of Kluyveromyces lactis and Pichia pastoris, as well as with those of the human fungal pathogens Candida albicans and Candida glabrata, revealed a conserved set of 10 and six secretory proteins, respectively.

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Section: Discussionsupporting

confidence: 82%

Growth-dependent secretome of Candida utilis

et al. 2011

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“…Microbial production of L-asparaginase has attracted more attention because of cost-effective and eco-friendly process. A wide range of microorganisms such as filamentous fungi [10,11], bacteria [12][13][14], yeast [15,16] and actinomycetes [17] have been reported in the literature for production of this enzyme. L-asparaginase production has been widely carried out by submerged fermentation (SmF) process.…”

Section: Introductionmentioning

confidence: 99%

Optimization of L-asparaginase production by Serratia marcescens (NCIM 2919) under solid state fermentation using coconut oil cake

Ghosh

Murthy

Sharmila

et al. 2013

sustain chem process

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Background: The present study focused on utilization of agrowaste byproducts generated from oil mill for L-asparaginase enzyme production using Serratia marcescens under solid state fermentation. Classical and statistical methods were employed to optimize the process variables and the results were compared. Results: The classical one factor at a time (OFAT) and response surface methodology (RSM) are employed to optimize the fermentation process. When used as the sole carbon source in SSF, coconut oil cake (COC) showed maximum enzyme production. The optimal values of substrate amount, initial moisture content, pH and temperature were found to be 6 g, 40%, 6 and 35°C respectively under classical optimization method with maximum enzyme activity of 3.87 (U gds -1 ). Maximum enzyme activity of 5.86 U gds -1 was obtained at the predicted optimal conditions of substrate amount 7.6 g of COC, initial moisture content of substrate 50%, temperature 35.5°C and pH 7.4. Validation results proved that a good relation existed between the experimental and the predicted model. Conclusions: RSM optimization approach enhances the enzyme production to 33% when compared to classical method. Utilization of coconut oil cake as a low cost substrate in SSF for L-asparaginase production makes the process economical and also reduces the environmental pollution by converting the oil mill solid waste into a useful bioproduct.

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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

125

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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Extraction of ExtracellularL-Asparaginase fromCandida utilis

Cited by 34 publications

References 1 publication

Growth-dependent secretome of Candida utilis

Growth-dependent secretome of Candida utilis

Optimization of L-asparaginase production by Serratia marcescens (NCIM 2919) under solid state fermentation using coconut oil cake

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

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