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Volumn 47, Issue 3, 2017, Pages 219-228

Optimization of L-asparaginase production from novel Enterobacter sp., by submerged fermentation using response surface methodology

Author keywords

antileukemic drug; Enterobacter aerogenes MTCC111; enzyme activity; L Asparaginase; optimization; substrate specificity

Indexed keywords

ANTINEOPLASTIC AGENT; ASPARAGINASE; ASPARAGINE; CARBON; NITROGEN;

EID: 85014899262     PISSN: 10826068     EISSN: 15322297     Source Type: Journal    
DOI: 10.1080/10826068.2016.1201683     Document Type: Article
Times cited : (33)

References (55)
  • 1
    • 33947212990 scopus 로고    scopus 로고
    • L-Asparaginase: A Promising Chemotherapeutic Agent
    • Verma, N.,; Kumar, K.,; Kaur, G.,; Anand, S., L-Asparaginase:A Promising Chemotherapeutic Agent. Crit. Rev. Biotechnol. 2007, 27(1), 45–62.
    • (2007) Crit. Rev. Biotechnol. , vol.27 , Issue.1 , pp. 45-62
    • Verma, N.1    Kumar, K.2    Kaur, G.3    Anand, S.4
  • 3
    • 84864739193 scopus 로고    scopus 로고
    • Production, Immobilization and Anti-tumor Activity of L-Asparaginase of Bacillus sp R36
    • Moharam, M.,; Gamal-Eldeen, A.,; El-Sayed, S., Production, Immobilization and Anti-tumor Activity of L-Asparaginase of Bacillus sp R36. J. Am. Sci. 2010, 6(8), 131–140.
    • (2010) J. Am. Sci. , vol.6 , Issue.8 , pp. 131-140
    • Moharam, M.1    Gamal-Eldeen, A.2    El-Sayed, S.3
  • 4
    • 66149098057 scopus 로고    scopus 로고
    • Evaluating the Potential for Enzymatic Acrylamide Mitigation in a Range of Food Products using an Asparaginase from Aspergillus oryzae
    • Hendriksen, H.V.,; Kornbrust, B.A.,; Østergaard, P.R.,; Stringer, M.A., Evaluating the Potential for Enzymatic Acrylamide Mitigation in a Range of Food Products using an Asparaginase from Aspergillus oryzae. J. Agr. Food Chem. 2009, 57(10), 4168–4176.
    • (2009) J. Agr. Food Chem. , vol.57 , Issue.10 , pp. 4168-4176
    • Hendriksen, H.V.1    Kornbrust, B.A.2    Østergaard, P.R.3    Stringer, M.A.4
  • 6
    • 77957314159 scopus 로고    scopus 로고
    • Therapeutic Alternatives to Native L-Asparaginase in the Treatment of Adult Acute Lymphoblastic Leukemia
    • Thomas, X.,; Cannas, G.,; Chelghoum, Y.,; Gougounon, A., Therapeutic Alternatives to Native L-Asparaginase in the Treatment of Adult Acute Lymphoblastic Leukemia. Bull. Cancer 2010, 97(9), 1105–1117.
    • (2010) Bull. Cancer , vol.97 , Issue.9 , pp. 1105-1117
    • Thomas, X.1    Cannas, G.2    Chelghoum, Y.3    Gougounon, A.4
  • 7
    • 0042999388 scopus 로고    scopus 로고
    • Pegaspargase: A Review of Clinical Studies
    • Graham, M.L., Pegaspargase:A Review of Clinical Studies. Adv. Drug Deliv. Rev. 2003, 55(10), 1293–1302.
    • (2003) Adv. Drug Deliv. Rev. , vol.55 , Issue.10 , pp. 1293-1302
    • Graham, M.L.1
  • 8
    • 0037089437 scopus 로고    scopus 로고
    • Comparison of Escherichia coli–Asparaginase with Erwinia-asparaginase in the Treatment of Childhood Lymphoid Malignancies: Results of a Randomized European Organisation for Research and Treatment of Cancer—Children’s Leukemia Group Phase 3 Trial
    • Duval, M.,; Suciu, S.,; Ferster, A.,; Rialland, X.,; Nelken, B.,; Lutz, P.,; Benoit, Y.,; Robert, A.,; Manel, A.M.,; Vilmer, E., Comparison of Escherichia coli–Asparaginase with Erwinia-asparaginase in the Treatment of Childhood Lymphoid Malignancies:Results of a Randomized European Organisation for Research and Treatment of Cancer—Children’s Leukemia Group Phase 3 Trial. Blood. 2002, 99(8), 2734–2749.
    • (2002) Blood. , vol.99 , Issue.8 , pp. 2734-2749
    • Duval, M.1    Suciu, S.2    Ferster, A.3    Rialland, X.4    Nelken, B.5    Lutz, P.6    Benoit, Y.7    Robert, A.8    Manel, A.M.9    Vilmer, E.10
  • 9
    • 84904388114 scopus 로고    scopus 로고
    • Microbial L-Asparaginase as a Potential Therapeutic Agent for the Treatment of Acute Lymphoblastic Leukemia: The Pros and Cons
    • El-Naggar, NE.A.,; El-Ewasy, S.M.,; El-Shweihy, N.M., Microbial L-Asparaginase as a Potential Therapeutic Agent for the Treatment of Acute Lymphoblastic Leukemia:The Pros and Cons. Int. J. Pharmacol. 2014, 10(4), 182–199.
    • (2014) Int. J. Pharmacol. , vol.10 , Issue.4 , pp. 182-199
    • El-Naggar, N.E.A.1    El-Ewasy, S.M.2    El-Shweihy, N.M.3
  • 10
    • 0015522573 scopus 로고
    • L-Asparaginase from Erwinia carotovora Substrate Specificity and Enzymatic Properties
    • Howard, J.B.,; Carpenter, F.H., L-Asparaginase from Erwinia carotovora Substrate Specificity and Enzymatic Properties. J. Biol. Chem. 1972, 247(4), 1020–1030.
    • (1972) J. Biol. Chem. , vol.247 , Issue.4 , pp. 1020-1030
    • Howard, J.B.1    Carpenter, F.H.2
  • 11
    • 0014403435 scopus 로고
    • Asparagine Synthetase in Asparaginase Resistant and Susceptible Mouse Lymphomas
    • Prager, M.D.,; Bachynsky, N., Asparagine Synthetase in Asparaginase Resistant and Susceptible Mouse Lymphomas. Biochem. Bioph. Res. Commun. 1968, 31(1), 43–47.
    • (1968) Biochem. Bioph. Res. Commun. , vol.31 , Issue.1 , pp. 43-47
    • Prager, M.D.1    Bachynsky, N.2
  • 12
    • 4143063669 scopus 로고    scopus 로고
    • Asparaginase Pharmacokinetics After Intensive Polyethylene Glycol-conjugated L-Asparaginase Therapy for Children with Relapsed Acute Lymphoblastic Leukemia
    • Hawkins, D.S.,; Park, J.R.,; Thomson, B.G.,; Felgenhauer, J.L.,; Holcenberg, J.S.,; Panosyan, E.H.,; Avramis, V.I., Asparaginase Pharmacokinetics After Intensive Polyethylene Glycol-conjugated L-Asparaginase Therapy for Children with Relapsed Acute Lymphoblastic Leukemia. Clin. Cancer Res. 2004, 10(16), 5335–5341.
    • (2004) Clin. Cancer Res. , vol.10 , Issue.16 , pp. 5335-5341
    • Hawkins, D.S.1    Park, J.R.2    Thomson, B.G.3    Felgenhauer, J.L.4    Holcenberg, J.S.5    Panosyan, E.H.6    Avramis, V.I.7
  • 13
  • 14
    • 53149100089 scopus 로고    scopus 로고
    • L-Asparaginase Production by Streptomyces albidoflavus
    • Narayana, K.,; Kumar, K.,; Vijayalakshmi, M., L-Asparaginase Production by Streptomyces albidoflavus. Indian J. Microbiol. 2008, 48(3), 331–336.
    • (2008) Indian J. Microbiol. , vol.48 , Issue.3 , pp. 331-336
    • Narayana, K.1    Kumar, K.2    Vijayalakshmi, M.3
  • 15
    • 71049173179 scopus 로고    scopus 로고
    • Production, Purification and Characterization of L-Asparaginase from Streptomyces gulbargensis
    • Amena, S.,; Vishalakshi, N.,; Prabhakar, M.,; Dayanand, A.,; Lingappa, K., Production, Purification and Characterization of L-Asparaginase from Streptomyces gulbargensis. Braz. J. Microbiol. 2010, 41(1), 173–178.
    • (2010) Braz. J. Microbiol. , vol.41 , Issue.1 , pp. 173-178
    • Amena, S.1    Vishalakshi, N.2    Prabhakar, M.3    Dayanand, A.4    Lingappa, K.5
  • 16
    • 84884749129 scopus 로고    scopus 로고
    • Screening and Characterization of Extracelluar L-Asparaginase Producing Bacillus subtilis Strain hswx88, Isolated from Taptapani Hotspring of Odisha, India
    • Pradhan, B.,; Dash, S.K.,; Sahoo, S., Screening and Characterization of Extracelluar L-Asparaginase Producing Bacillus subtilis Strain hswx88, Isolated from Taptapani Hotspring of Odisha, India. Asian Pac. J. Trop. Biomed. 2013, 3(12), 936–941.
    • (2013) Asian Pac. J. Trop. Biomed. , vol.3 , Issue.12 , pp. 936-941
    • Pradhan, B.1    Dash, S.K.2    Sahoo, S.3
  • 17
    • 70350567914 scopus 로고    scopus 로고
    • Enhancement of L-Asparaginase Production by Isolated Bacillus circulans (MTCC 8574) using Response Surface Methodology
    • Hymavathi, M.,; Sathish, T.,; Rao, C.S.,; Prakasham, R., Enhancement of L-Asparaginase Production by Isolated Bacillus circulans (MTCC 8574) using Response Surface Methodology. Appl. Biochem. Biotechnol. 2009, 159(1), 191–198.
    • (2009) Appl. Biochem. Biotechnol. , vol.159 , Issue.1 , pp. 191-198
    • Hymavathi, M.1    Sathish, T.2    Rao, C.S.3    Prakasham, R.4
  • 18
    • 84896449328 scopus 로고    scopus 로고
    • Production of Antimicrobial Agent Inhibitory to Some Human Pathogenic Multidrug-resistant Bacteria and Candida albicans by Streptomyces sp NEAE-1
    • El-Naggar, N.E.A.,; El-Bindary, A.A.,; Nour, N.S., Production of Antimicrobial Agent Inhibitory to Some Human Pathogenic Multidrug-resistant Bacteria and Candida albicans by Streptomyces sp NEAE-1. Int. J. Pharmacol. 2013, 9(6), 335–347.
    • (2013) Int. J. Pharmacol. , vol.9 , Issue.6 , pp. 335-347
    • El-Naggar, N.E.A.1    El-Bindary, A.A.2    Nour, N.S.3
  • 19
    • 84896443605 scopus 로고    scopus 로고
    • Statistical Optimization of Process Variables for Antimicrobial Metabolites Production by Streptomyces anulatus NEAE-94 Against Some Multidrug-resistant Strains
    • El-Naggar, N.E.A.,; El-Bindary, A.A.,; Nour, N.S., Statistical Optimization of Process Variables for Antimicrobial Metabolites Production by Streptomyces anulatus NEAE-94 Against Some Multidrug-resistant Strains. Int. J. Pharmacol. 2013, 9(6), 322–334.
    • (2013) Int. J. Pharmacol. , vol.9 , Issue.6 , pp. 322-334
    • El-Naggar, N.E.A.1    El-Bindary, A.A.2    Nour, N.S.3
  • 20
    • 84891602177 scopus 로고    scopus 로고
    • application of Statistical Experimental Design for Optimization of Silver Nanoparticles Biosynthesis by a Nanofactory Streptomyces viridochromogenes
    • El-Naggar, N.E.A.,; Abdelwahed, N.A., application of Statistical Experimental Design for Optimization of Silver Nanoparticles Biosynthesis by a Nanofactory Streptomyces viridochromogenes. J. Microbiol. 2014, 52(1), 53–63.
    • (2014) J. Microbiol. , vol.52 , Issue.1 , pp. 53-63
    • El-Naggar, N.E.A.1    Abdelwahed, N.A.2
  • 21
    • 84899134798 scopus 로고    scopus 로고
    • Fabrication of Biogenic Antimicrobial Silver Nanoparticles by Streptomyces aegyptia NEAE 102 as Eco-friendly Nanofactory
    • El-Naggar, N.E.A.,; Abdelwahed, N.A.,; Darwesh, O.M., Fabrication of Biogenic Antimicrobial Silver Nanoparticles by Streptomyces aegyptia NEAE 102 as Eco-friendly Nanofactory. J. Microbiol. Biotechnol. 2014, 24(4), 453–464.
    • (2014) J. Microbiol. Biotechnol. , vol.24 , Issue.4 , pp. 453-464
    • El-Naggar, N.E.A.1    Abdelwahed, N.A.2    Darwesh, O.M.3
  • 22
    • 7444263568 scopus 로고    scopus 로고
    • Optimization of Chitinase Production using Statistics Based Experimental Designs
    • Nawani, N.,; Kapadnis, B., Optimization of Chitinase Production using Statistics Based Experimental Designs. Process Biochem. 2005, 40(2), 651–660.
    • (2005) Process Biochem. , vol.40 , Issue.2 , pp. 651-660
    • Nawani, N.1    Kapadnis, B.2
  • 23
    • 33749024136 scopus 로고    scopus 로고
    • Statistical Optimization of Medium Components for the Production of Antrodia cinnamomea AC0623 in Submerged Cultures
    • Chang, C.Y.,; Lee, C.L.,; Pan, T.M., Statistical Optimization of Medium Components for the Production of Antrodia cinnamomea AC0623 in Submerged Cultures. Appl. Microbiol. Biotechnol. 2006, 72(4), 654–661.
    • (2006) Appl. Microbiol. Biotechnol. , vol.72 , Issue.4 , pp. 654-661
    • Chang, C.Y.1    Lee, C.L.2    Pan, T.M.3
  • 24
    • 58149185981 scopus 로고    scopus 로고
    • Biological Treatment of Toxic Petroleum Spent Caustic in Fluidized Bed Bioreactor using Immobilized Cells of Thiobacillus RAI01
    • Potumarthi, R.,; Mugeraya, G.,; Jetty, A., Biological Treatment of Toxic Petroleum Spent Caustic in Fluidized Bed Bioreactor using Immobilized Cells of Thiobacillus RAI01. Appl. Biochem. Biotechnol. 2008, 151(2–3), 532–546.
    • (2008) Appl. Biochem. Biotechnol. , vol.151 , Issue.2-3 , pp. 532-546
    • Potumarthi, R.1    Mugeraya, G.2    Jetty, A.3
  • 25
    • 37649014195 scopus 로고    scopus 로고
    • Evaluation of Various Parameters of Calcium-alginate Immobilization Method for Enhanced Alkaline Protease Production by Bacillus licheniformis NCIM-2042 using Statistical Methods
    • Potumarthi, R.,; Subhakar, C.,; Pavani, A.,; Jetty, A., Evaluation of Various Parameters of Calcium-alginate Immobilization Method for Enhanced Alkaline Protease Production by Bacillus licheniformis NCIM-2042 using Statistical Methods. Bioresour. Technol. 2008, 99(6), 1776–1786.
    • (2008) Bioresour. Technol. , vol.99 , Issue.6 , pp. 1776-1786
    • Potumarthi, R.1    Subhakar, C.2    Pavani, A.3    Jetty, A.4
  • 26
    • 34547973216 scopus 로고    scopus 로고
    • Optimization of Media Constituents Through Response Surface Methodology for Improved Production of alkaline proteases by Serratia rubidaea
    • Doddapaneni, K.K.,; Tatineni, R.,; Potumarthi, R.,; Mangamoori, L.N., Optimization of Media Constituents Through Response Surface Methodology for Improved Production of alkaline proteases by Serratia rubidaea. J. Chem. Technol. Biotechnol. 2007, 82(8), 721–729.
    • (2007) J. Chem. Technol. Biotechnol. , vol.82 , Issue.8 , pp. 721-729
    • Doddapaneni, K.K.1    Tatineni, R.2    Potumarthi, R.3    Mangamoori, L.N.4
  • 27
    • 38449086232 scopus 로고    scopus 로고
    • Optimization of Keratinase Production and Enzyme Activity using Response Surface Methodology with Streptomyces sp7
    • Tatineni, R.,; Doddapaneni, K.K.,; Potumarthi, R.C.,; Mangamoori, L.N., Optimization of Keratinase Production and Enzyme Activity using Response Surface Methodology with Streptomyces sp7. Appl. Biochem. Biotechnol. 2007, 141(2–3), 187–201.
    • (2007) Appl. Biochem. Biotechnol. , vol.141 , Issue.2-3 , pp. 187-201
    • Tatineni, R.1    Doddapaneni, K.K.2    Potumarthi, R.C.3    Mangamoori, L.N.4
  • 28
    • 70350641086 scopus 로고    scopus 로고
    • Multiple Responses Optimization and Modeling of Lipase Production by Rhodotorula mucilaginosa MTCC-8737 using Response Surface Methodology
    • Chennupati, S.,; Potumarthi, R.,; Rao, M.G.,; Manga, P.L.,; Sridevi, M.,; Jetty, A., Multiple Responses Optimization and Modeling of Lipase Production by Rhodotorula mucilaginosa MTCC-8737 using Response Surface Methodology. Appl. Biochem. Biotechnol. 2009, 159(2), 317–329.
    • (2009) Appl. Biochem. Biotechnol. , vol.159 , Issue.2 , pp. 317-329
    • Chennupati, S.1    Potumarthi, R.2    Rao, M.G.3    Manga, P.L.4    Sridevi, M.5    Jetty, A.6
  • 29
    • 70349582717 scopus 로고    scopus 로고
    • Constitutive Expression and Optimization of Nutrients for Streptokinase Production by Pichia pastoris using Statistical Methods
    • Vellanki, R.N.,; Potumarthi, R.,; Mangamoori, L.N., Constitutive Expression and Optimization of Nutrients for Streptokinase Production by Pichia pastoris using Statistical Methods. Appl. Biochem. Biotechnol. 2009, 158(1), 25–40.
    • (2009) Appl. Biochem. Biotechnol. , vol.158 , Issue.1 , pp. 25-40
    • Vellanki, R.N.1    Potumarthi, R.2    Mangamoori, L.N.3
  • 30
    • 84859499349 scopus 로고    scopus 로고
    • Heterologous Expression and Optimization using Experimental Designs Allowed Highly Efficient Production of the PHY US417 Phytase in Bacillus subtilis 168
    • Farhat-Khemakhem, A.,; Farhat, M.B.,; Boukhris, I.,; Bejar, W.,; Bouchaala, K.,; Kammoun, R.,; Maguin, E.,; Bejar, S.,; Chouayekh, H., Heterologous Expression and Optimization using Experimental Designs Allowed Highly Efficient Production of the PHY US417 Phytase in Bacillus subtilis 168. AMB Express. 2012, 2(1), 1–11.
    • (2012) AMB Express. , vol.2 , Issue.1 , pp. 1-11
    • Farhat-Khemakhem, A.1    Farhat, M.B.2    Boukhris, I.3    Bejar, W.4    Bouchaala, K.5    Kammoun, R.6    Maguin, E.7    Bejar, S.8    Chouayekh, H.9
  • 31
    • 0034005352 scopus 로고    scopus 로고
    • Studies on Nutritional and Oxygen Requirements for Production of L-Asparaginase by Enterobacter aerogenes
    • Mukherjee, J.,; Majumdar, S.,; Scheper, T., Studies on Nutritional and Oxygen Requirements for Production of L-Asparaginase by Enterobacter aerogenes. Appl. Microbiol. Biotechnol. 2000, 53(2), 180–184.
    • (2000) Appl. Microbiol. Biotechnol. , vol.53 , Issue.2 , pp. 180-184
    • Mukherjee, J.1    Majumdar, S.2    Scheper, T.3
  • 32
    • 0031042733 scopus 로고    scopus 로고
    • A Rapid Plate Assay for Screening L-Asparaginase Producing Micro-organisms
    • Gulati, R.,; Saxena, R.,; Gupta, R., A Rapid Plate Assay for Screening L-Asparaginase Producing Micro-organisms. Lett. Appl. Microbiol. 1997, 24(1), 23–26.
    • (1997) Lett. Appl. Microbiol. , vol.24 , Issue.1 , pp. 23-26
    • Gulati, R.1    Saxena, R.2    Gupta, R.3
  • 34
    • 71849104860 scopus 로고
    • Protein Measurement with the Folin Phenol Reagent
    • Lowry, O.H.,; Rosebrough, N.,; Farr, A.L.,; Randall, R.J., Protein Measurement with the Folin Phenol Reagent. J. Biol. Chem. 1951, 193(1), 265–275.
    • (1951) J. Biol. Chem. , vol.193 , Issue.1 , pp. 265-275
    • Lowry, O.H.1    Rosebrough, N.2    Farr, A.L.3    Randall, R.J.4
  • 35
    • 84857198807 scopus 로고    scopus 로고
    • Optimization of α-Amylase Production from Aspergillus niger using Spoiled Starch Rich Vegetables by Response Surface Methodology and Genetic Algorithm
    • BITS Pilani, Hyderabad, 16–18 December
    • Rajulapati, S.B.,; Lakshmi Narasu, M.,; Vundavilli, P., Optimization of α-Amylase Production from Aspergillus niger using Spoiled Starch Rich Vegetables by Response Surface Methodology and Genetic Algorithm. India Conference (INDICON), Annual IEEE. IEEE, BITS Pilani, Hyderabad, 16–18 December, 2011, 1–9.
    • (2011) India Conference (INDICON), Annual IEEE. IEEE , pp. 1-9
    • Rajulapati, S.B.1    Lakshmi Narasu, M.2    Vundavilli, P.3
  • 36
    • 84949553604 scopus 로고    scopus 로고
    • Optimization of Medium Components for Extracellular Glutaminase Free Asparaginase from Enterobacter cloacae
    • Sharma, A.,; Husain, I., Optimization of Medium Components for Extracellular Glutaminase Free Asparaginase from Enterobacter cloacae. Int. J. Curr. Microbiol. Appl. Sci. 2015, 4(1), 296–309.
    • (2015) Int. J. Curr. Microbiol. Appl. Sci. , vol.4 , Issue.1 , pp. 296-309
    • Sharma, A.1    Husain, I.2
  • 37
    • 85014957236 scopus 로고    scopus 로고
    • Biological Properties of L-Asparaginase. 2010, Mahatma Gandhi University, India, PhD thesis
    • Benny, P., Biological Properties of L-Asparaginase. 2010, Mahatma Gandhi University, India, PhD thesis.
    • Benny, P.1
  • 38
    • 84907447594 scopus 로고    scopus 로고
    • Partial Purification and Cytotoxic activity of L-Asparaginase from Streptomyces acrimycini NGP
    • Selvam, K.,; Vishnupriya, B., Partial Purification and Cytotoxic activity of L-Asparaginase from Streptomyces acrimycini NGP. Int. J. Res. Pharm. Biomed. Sci. 2013, 4(3), 859–869.
    • (2013) Int. J. Res. Pharm. Biomed. Sci. , vol.4 , Issue.3 , pp. 859-869
    • Selvam, K.1    Vishnupriya, B.2
  • 39
    • 84894195262 scopus 로고    scopus 로고
    • Isolation, Molecular Identification and Optimization of Fermentation Parameters for the Production of L-Asparaginase, an Anticancer Agent by Fusarium equiseti
    • Hosamani, R.,; Kaliwal, B., Isolation, Molecular Identification and Optimization of Fermentation Parameters for the Production of L-Asparaginase, an Anticancer Agent by Fusarium equiseti. Int. J. Microbiol. Res. 2011, 3(2), 108–119.
    • (2011) Int. J. Microbiol. Res. , vol.3 , Issue.2 , pp. 108-119
    • Hosamani, R.1    Kaliwal, B.2
  • 40
    • 84892142044 scopus 로고    scopus 로고
    • Media Optimization for the Production of Anti-leukemic Enzyme L-Asparaginase from E. coli K-12
    • Kumar, K.,; Punia, S.,; Verma, N., Media Optimization for the Production of Anti-leukemic Enzyme L-Asparaginase from E. coli K-12. Ann. Biol. Res. 2012, 3(10), 4828–4837.
    • (2012) Ann. Biol. Res. , vol.3 , Issue.10 , pp. 4828-4837
    • Kumar, K.1    Punia, S.2    Verma, N.3
  • 41
    • 84866483165 scopus 로고    scopus 로고
    • Efficient Production of L-Asparaginase from Bacillus licheniformis with Low-glutaminase Activity: Optimization, Scale up and Acrylamide Degradation Studies
    • Mahajan, R.V.,; Saran, S.,; Kameswaran, K.,; Kumar, V.,; Saxena, R., Efficient Production of L-Asparaginase from Bacillus licheniformis with Low-glutaminase Activity:Optimization, Scale up and Acrylamide Degradation Studies. Bioresour. Technol. 2012, 125, 11–16.
    • (2012) Bioresour. Technol. , vol.125 , pp. 11-16
    • Mahajan, R.V.1    Saran, S.2    Kameswaran, K.3    Kumar, V.4    Saxena, R.5
  • 42
    • 79961226219 scopus 로고    scopus 로고
    • Production of L-Asparaginase from Natural Substrates by Aspergillus terreus MTCC 1782: Optimization of Carbon Source and Operating Conditions
    • Gurunathan, B.,; Sahadevan, R., Production of L-Asparaginase from Natural Substrates by Aspergillus terreus MTCC 1782:Optimization of Carbon Source and Operating Conditions. Int. J. Chem. Reactor Eng. 2011, 9, 1–15.
    • (2011) Int. J. Chem. Reactor Eng. , vol.9 , pp. 1-15
    • Gurunathan, B.1    Sahadevan, R.2
  • 43
    • 58149182209 scopus 로고    scopus 로고
    • Cellulase Production Under Solid-state Fermentation by Trichoderma reesei RUT C30: Statistical Optimization of Process Parameters
    • Mekala, N.K.,; Singhania, R.R.,; Sukumaran, R.K.,; Pandey, A., Cellulase Production Under Solid-state Fermentation by Trichoderma reesei RUT C30:Statistical Optimization of Process Parameters. Appl. Biochem. Biotechnol. 2008, 151(2–3), 122–131.
    • (2008) Appl. Biochem. Biotechnol. , vol.151 , Issue.2-3 , pp. 122-131
    • Mekala, N.K.1    Singhania, R.R.2    Sukumaran, R.K.3    Pandey, A.4
  • 44
    • 84864456578 scopus 로고    scopus 로고
    • Surface Immobilization of Rhizopus oryzae (ATCC 96382) for Enhanced Production of Lipase Enzyme by Multiple Responses Optimization
    • Potumarthi, R.,; Liu, J.,; Wan, H.,; Danquah, M., Surface Immobilization of Rhizopus oryzae (ATCC 96382) for Enhanced Production of Lipase Enzyme by Multiple Responses Optimization. Asia Pac. J. Chem. Eng. 2012, 7(S3), S285–S295.
    • (2012) Asia Pac. J. Chem. Eng. , vol.7 , Issue.S3 , pp. S285-S295
    • Potumarthi, R.1    Liu, J.2    Wan, H.3    Danquah, M.4
  • 46
    • 0004236701 scopus 로고
    • Oxford, England: John Wiley & Sons, 2nd edition
    • Cochran, W.,; Cox, G., Experimental Designs. Oxford, England:John Wiley & Sons, 2nd edition. 1957.
    • (1957) Experimental Designs
    • Cochran, W.1    Cox, G.2
  • 47
    • 84889102641 scopus 로고    scopus 로고
    • Modeling and Optimization of L-Asparaginase Production by Enterobacter aerogenes using Artificial Neural Network Linked Genetic Algorithm
    • Baskar, G.,; Rajasekar, V.,; Renganathan, S., Modeling and Optimization of L-Asparaginase Production by Enterobacter aerogenes using Artificial Neural Network Linked Genetic Algorithm. Int. J. Chem. Eng. Appl. 2011, 2(2), 98–100.
    • (2011) Int. J. Chem. Eng. Appl. , vol.2 , Issue.2 , pp. 98-100
    • Baskar, G.1    Rajasekar, V.2    Renganathan, S.3
  • 48
    • 70450279012 scopus 로고    scopus 로고
    • Optimization of Carbon and Nitrogen Sources for L-Asparaginase Production by Enterobacter aerogenes using Response Surface Methodology
    • Baskar, G.,; Dharmendira Kumar, M.,; Anand Prabu, A.,; Renganathan, S.,; Yoo, C., Optimization of Carbon and Nitrogen Sources for L-Asparaginase Production by Enterobacter aerogenes using Response Surface Methodology. Chem. Biochem. Eng. Q. 2009, 23(3), 393–397.
    • (2009) Chem. Biochem. Eng. Q. , vol.23 , Issue.3 , pp. 393-397
    • Baskar, G.1    Dharmendira Kumar, M.2    Anand Prabu, A.3    Renganathan, S.4    Yoo, C.5
  • 49
    • 85014962084 scopus 로고    scopus 로고
    • Optimization of Culture Variables for the Production of L-Asparaginase from Pectobacterium carotovorum
    • Singhal, B.,; Swaroop, K., Optimization of Culture Variables for the Production of L-Asparaginase from Pectobacterium carotovorum. Afr. J. Biotechnol. 2013, 12(50), 6959–6967.
    • (2013) Afr. J. Biotechnol. , vol.12 , Issue.50 , pp. 6959-6967
    • Singhal, B.1    Swaroop, K.2
  • 51
    • 80054816274 scopus 로고    scopus 로고
    • Production of L-Asparaginase from Escherichia coli ATCC 11303: Optimization by Response Surface Methodology
    • Kenari, S.L.D.,; Alemzadeh, I.,; Maghsodi, V., Production of L-Asparaginase from Escherichia coli ATCC 11303:Optimization by Response Surface Methodology. Food. Bioprod. Process. 2011, 89(4), 315–321.
    • (2011) Food. Bioprod. Process. , vol.89 , Issue.4 , pp. 315-321
    • Kenari, S.L.D.1    Alemzadeh, I.2    Maghsodi, V.3
  • 52
    • 84930639313 scopus 로고    scopus 로고
    • Industrial Effluent as a Substrate for Glutaminase Free L-Asparaginase Production from Pseudomonas plecoglossicida Strain RS1; Media Optimization, Enzyme Purification and Its Characterization
    • Shakambari, G.,; Sumi, B.M.,; Ashokkumar, B.,; Palanivelu, P.,; Varalakshmi, P., Industrial Effluent as a Substrate for Glutaminase Free L-Asparaginase Production from Pseudomonas plecoglossicida Strain RS1; Media Optimization, Enzyme Purification and Its Characterization. RSC Adv. 2015, 5(60), 48729–48738.
    • (2015) RSC Adv. , vol.5 , Issue.60 , pp. 48729-48738
    • Shakambari, G.1    Sumi, B.M.2    Ashokkumar, B.3    Palanivelu, P.4    Varalakshmi, P.5
  • 53
    • 84864491081 scopus 로고    scopus 로고
    • Production and Optimization of L-Asparaginase from Cladosporium sp. using Agricultural Residues in Solid State Fermentation
    • Kumar, N.M.,; Ramasamy, R.,; Manonmani, H.K., Production and Optimization of L-Asparaginase from Cladosporium sp. using Agricultural Residues in Solid State Fermentation. Ind. Crops Prod. 2013, 43, 150–158.
    • (2013) Ind. Crops Prod. , vol.43 , pp. 150-158
    • Kumar, N.M.1    Ramasamy, R.2    Manonmani, H.K.3
  • 54
    • 78650083676 scopus 로고    scopus 로고
    • Sequential Optimization and Kinetic Modeling of L‐Asparaginase Production by Pectobacterium carotovorum in Submerged Fermentation
    • Sanjeeviroyar, A.,; Rajendran, A.,; Muthuraj, M.,; Basha, K.M.,; Thangavelu, V., Sequential Optimization and Kinetic Modeling of L‐Asparaginase Production by Pectobacterium carotovorum in Submerged Fermentation. Asia Pac. J. Chem. Eng. 2010, 5(5), 743–755.
    • (2010) Asia Pac. J. Chem. Eng. , vol.5 , Issue.5 , pp. 743-755
    • Sanjeeviroyar, A.1    Rajendran, A.2    Muthuraj, M.3    Basha, K.M.4    Thangavelu, V.5
  • 55
    • 0015308327 scopus 로고
    • L-Asparaginase Synthesis by Erwinia aroideae
    • Liu, F.S.,; Zajic, J.E., L-Asparaginase Synthesis by Erwinia aroideae. Appl. Microbial. 1972, 23(3), 667–668.
    • (1972) Appl. Microbial. , vol.23 , Issue.3 , pp. 667-668
    • Liu, F.S.1    Zajic, J.E.2


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