Therapeutic l-asparaginase: upstream, downstream and beyond

Critical Reviews in Biotechnology

Volumn 37, Issue 1, 2017, Pages 82-99

  Lopes, André Moreni ^a   Oliveira Nascimento, Laura de ^b   Ribeiro, Artur ^c   Tairum, Carlos Abrunhosa ^d   Breyer, Carlos Alexandre ^d   Oliveira, Marcos Antonio de ^d   Monteiro, Gisele ^a   Souza Motta, Cristina Maria de ^e   Magalhães, Pérola de Oliveira ^f   Avendaño, Jorge Gonzalo Farías ^g   Cavaco Paulo, Artur Manuel ^c   Mazzola, Priscila Gava ^b   Rangel Yagui, Carlota de Oliveira ^a   Sette, Lara Durães ^d   Converti, Attilio ^h   Pessoa, Adalberto ^a  

^a UNIVERSITY OF SÃO PAULO   (Brazil)

^b UNIVERSITY OF CAMPINAS   (Brazil)

^c UNIVERSITY OF MINHO   (Portugal)

^d SÃO PAULO STATE UNIVERSITY UNESP   (Brazil)

^e FEDERAL UNIVERSITY OF PERNAMBUCO   (Brazil)

^f UNIVERSITY OF BRASILIA   (Brazil)

^g UNIVERSIDAD DE LA FRONTERA   (Chile)

^h UNIVERSITY OF GENOA   (Italy)

Author keywords

Acute lymphoblastic leukemia; antineoplastic activity; biopharmaceutical; l asparaginase; microbial l asparaginase production

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; COST EFFECTIVENESS; DISEASES; ENZYMES; GENETIC ENGINEERING; MICROORGANISMS; PROTEINS;

ACUTE LYMPHOBLASTIC LEUKEMIA; ANTINEOPLASTIC ACTIVITY; BIOCHEMICAL CHARACTERISTICS; BIOPHARMACEUTICAL; L -ASPARAGINASE; METABOLIC FLUX ANALYSIS; PURIFICATION PROTOCOL; RECOMBINANT MICROORGANISM;

BIOCHEMICAL ENGINEERING;

ASPARAGINASE; ANTINEOPLASTIC AGENT;

CANCER CHEMOTHERAPY; CATALYSIS; CHEMICAL MODIFICATION; CHROMATOGRAPHY; DOWNSTREAM PROCESSING; DRUG BIOAVAILABILITY; DRUG FORMULATION; ENZYME ACTIVITY; ENZYME ENGINEERING; ENZYME PURIFICATION; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SYNTHESIS; FERMENTATION; FREEZE DRYING; HUMAN; LIQUID LIQUID EXTRACTION; METABOLIC FLUX ANALYSIS; MUTAGENESIS; NONHUMAN; PRECIPITATION; PRIORITY JOURNAL; REVIEW; SIDE EFFECT; ANIMAL; BACTERIUM; CHEMISTRY; FUNGUS; METABOLISM; PROTEIN ENGINEERING;

ANIMALS; ANTINEOPLASTIC AGENTS; ASPARAGINASE; BACTERIA; DRUG COMPOUNDING; FUNGI; PROTEIN ENGINEERING;

EID: 84951292119     PISSN: 07388551     EISSN: 15497801     Source Type: Journal    
DOI: 10.3109/07388551.2015.1120705     Document Type: Review

References (166)

1. Abdel-Fatah MK, Abdel-Mageed AR, Abdel-All SM, et al. (1998). Purification and characterization of l-asparaginase produced by Streptomyces phaeochromogenes FS-39. J Drug Res, 22, 195–212
2. Abdel-Fatah MK. (1997). Studies on the asparaginolytic enzymes of streptomycetes II Purification and characterization of l-asparaginase from Streptomyces longsporusflavus (F-15) strain. Egypt J Microbiol, 31, 303–22
3. Abdel-Fattah YR, Olama ZA. (2002). l-asparaginase production by Pseudomonas aeruginosa in solid-state culture:evaluation and optimization of culture conditions using factorial designs. Process Biochem, 38, 115–22
4. Adams GD, Irons LI. (1993). Some implications of structural collapse during freeze-drying using Erwinia caratovoral-asparaginase as a model. J Chem Technol Biotechnol, 58, 71–6
5. Adams GD, Ramsay JR. (1996). Optimizing the lyophilization cycle and the consequences of collapse on the pharmaceutical acceptability of Erwinial-asparaginase. J Pharm Sci, 85, 1301–5
6. Aghaiypour K, Wlodawer A, Lubkowski J. (2001). Structural basis for the activity and substrate specificity of Erwinia chrysanthemil-asparaginase. Biochemistry, 40, 5655–64
7. Agrawal V, Woo JH, Borthakur G, et al. (2013). Red blood cell-encapsulated l-asparaginase:potential therapy of patients with asparagine synthetase deficient acute myeloid leukemia. Protein Peptide Lett, 20, 392–402
8. Albertsson PA. (1986). Partition of proteins in liquid polymer–polymer two-phase systems. In:Partition of cell particles and macromolecules. 3rd ed. New York:Wiley Intersciences, 709–71
9. Alegre RM, Minim LA. (1993). Cheese whey utilization for l-asparaginase production from Erwinia aroideae NRRL B-138 in pilot plant. Arq Biol Tecnol, 36, 525–34
10. Alhussaini MS. (2013). Mycobiota of wheat flour and detection of α-amylase and l-asparaginase enzymes. Life Sci J, 10, 1112–22
11. Amena S, Vishalakshi N, Prabhakar M, et al. (2010). Production, purification and characterization of l-asparaginase from Streptomyces gulbargensis. Braz J Microbiol, 41, 173–8
12. Anasontzis GE, Penã MS, Spadiut O, et al. (2014). Effects of temperature and glycerol- and methanol-feeding profiles on the production of recombinant galactose oxidase in Pichia pastoris. Biotechnol Prog, 30, 728–35
13. Antoniewicz MR. (2013). Dynamic metabolic flux analysis–tools for probing transient states of metabolic networks. Curr Opin Biotechnol, 24, 973–8
14. Apostolidou E, Swords R, Alvarado Y, et al. (2007). Treatment of ALL:a new era. Drugs, 67, 2153–71
15. Asselin BL, Whitin JC, Coppola DJ, et al. (1993). Comparative pharmacokinetic studies of three asparaginase preparations. J Clin Oncol, 11, 1780–86
16. Aung HP, Bocola M, Schleper S, et al. (2000). Dynamics of a mobile loop at the active site of Escherichia coli asparaginase. Biochim Biophys Acta, 1481, 349–59
17. Avramis VI, Panosyan EH. (2005). Pharmacokinetic/pharmacodynamic relationships of asparaginase formulations. Clin Pharmacokinet, 44, 367–93
18. Avramis VI, Tiwari PN. (2006). Asparaginase (native ASNase or pegylated ASNase) in the treatment of acute lymphoblastic leukemia. Int J Nanomed, 1, 241–54
19. Basha NS, Rekha R, Komala M, et al. (2009). Production of extracellular anti-leukaemic enzyme l-asparaginase from marine actinomycetes by solid state and submerged fermentation:purification and characterisation. Trop J Pharm Res, 8, 353–60
20. Boghigian BA, Seth G, Kiss R, et al. (2010). Metabolic flux analysis and pharmaceutical production. Metab Eng, 12, 81–95
21. Borek D, Kozak M, Pei J, et al. (2014). Crystal structure of active site mutant of antileukemic l-asparaginase reveals conserved zinc-binding site. FEBS J, 281, 4097–111
22. Bussolati O, Belletti S, Uggeri J, et al. (1995). Characterization of apoptotic phenomena induced by treatment with l-asparaginase in NIH3T3 cells. Exp Cell Res, 220, 283–91
23. Chan WK, Lorenzi PL, Anishkin A, et al. (2014). The glutaminase activity of l-asparaginase is not required for anticancer activity against ASNS-negative cells. Blood, 123, 3596–606
24. Chien WW, Le Beux C, Rachinel N, et al. (2015). Differential mechanisms of asparaginase resistance in B-type acute lymphoblastic leukemia and malignant natural killer cell lines. Sci Rep, doi:10.1038/srep08068
25. Cregg JM, Cereghino JL, Shi J, et al. (2000). Recombinant protein expression in Pichia pastoris. Mol Biotechnol, 16, 23–52
26. Datasus. Brazilian health ministry. Secretariat of health surveillance. Department of analysis of health situation. System of mortality information (SIM). Brasilia, DF, Brazil. Available from:http://www.datasus.gov.br [last accessed 10 Dec 2013]
27. De Bont JM, van der Holt B, Dekker AW, et al. (2004). Significant difference in outcome for adolescents with ALL treated on pediatric vs adult protocols in the Netherlands. Leukemia, 18, 2032–5
28. Derst C, Henseling J, Röhm KH. (1992). Probing the role of threonine and serine residues of E. coli asparaginase II by site-specific mutagenesis. Protein Eng, 8, 785–9
29. Derst C, Wehner A, Volker Specht V, et al. (1994). States and functions of tyrosine residues in Escherichia coli asparaginase II. Eur J Biochem, 224, 533–40
30. Derst C, Henseling J, Röhm KH. (2000). Engineering the substrate specificity of Escherichia coli asparaginase:II. Selective reduction of glutaminase activity by amino acid replacements at position 248. Protein Sci, 9, 2009–17
31. Dinndorf PA, Gootenberg J, Cohen MH, et al. (2007). FDA drug approval summary:pegaspargase (Oncaspar®) for the first-line treatment of children with acute lymphoblastic leukemia (ALL). Oncologist, 12, 991–8
32. Dutra-Molino JV, Araujo Feitosa V, Lencastre-Novaes LC, et al. (2014). Biomolecules extracted by ATPS:practical examples. Rev Mex Ing Quim, 13, 359–77
33. El-Bessoumy AA, Sarhan M, Mansour J. (2004). Production, isolation, and purification of l-asparaginase from Pseudomonas aeruginosa 50071 using solid-state fermentation. J Biochem Mol Biol, 37, 387–93
34. Fishburn CS. (2008). The pharmacology of PEGylation:balancing PD with PK to generate novel therapeutics. J Pharm Sci, 10, 4167–83
35. Fisher SH, Wray LV, Jr. (2002). Bacillus subtilis 168 contains two differentially regulated genes encoding l-asparaginase. J Bacteriol, 184, 2148–54
36. Gaynon PS, Carrel AL. (1999). Glucocorticosteroid therapy in childhood acute lymphoblastic leukemia. Adv Exp Med Biol, 457, 593–605
37. Geckil H, Gencer S. (2004). Production of l-asparaginase in Enterobacter aerogenes expressing Vitreoscilla hemoglobin for efficient oxygen uptake. Appl Microbiol Biotechnol, 63, 691–7
38. Geckil H, Ates B, Gencer S, et al. (2005). Membrane permeabilization of Gram-negative bacteria with potassium phosphate/hexane aqueous phase system for the release of l-asparaginase:an enzyme used in cancer therapy. Process Biochem, 40, 573–9
39. Geckil H, Gencer S, Ates B, et al. (2006). Effect of Vitreoscilla hemoglobin on production of a chemotherapeutic enzyme, l-asparaginase, by Pseudomonas aeruginosa. Biotechnol J, 1, 203–8
40. Gervais D, Allison N, Jennings A, et al. (2013). Validation of a 30-year-old process for the manufacture of l-asparaginase from Erwinia chrysanthemi. Bioprocess Biosyst Eng, 36, 453–60
41. Ghosh S, Murthy S, Govindasamy S, et al. (2013). Optimization of l-asparaginase production by Serratia marcescens (NCIM 2919) under solid state fermentation using coconut oil cake. Sust Chem Proc, 1, 1–8
42. Gladilina IuA, Sokolov NN, Krasotkina JV. (2009). Cloning, expression, and purification of Helicobacter pyloril-asparaginase. Biomed Khim, 3, 89–91
43. Glatz CE. (1990). Separation processes in biotechnology. New York:Marcel Dekker
44. Golunski S, Astolfi V, Carniel N, et al. (2011). Ethanol precipitation and ultrafiltration of inulinases from Kluyveromyces marxianus. Sep Purif Technol, 78, 261–5
45. Goudar CT, Biener RK, Piret JM, et al. (2014). Metabolic flux estimation in mammalian cell cultures. Methods Mol Biol, 1104, 193–209
46. Gräslund S, Nordlund P, Weigelt J, et al. (2008). Protein production and purification. Nat Methods, 5, 135–46
47. Gunasekaran S, McDonald L, Manavathu M, et al. (1995). Effect of culture media on growth and l-asparaginase production in Nocardia asteroides. Biomed Lett, 52, 197–201
48. Gupta N, Dash JS, Basak UC. (2009). l-asparaginases from fungi of Bhitarkanika mangrove ecosystem. AsPac J Mol Biol Biotechnol, 17, 27–30
49. Gurunathan B, Renganathan S. (2011). Design of experiments and artificial neural network linked genetic algorithm for modeling and optimization of l-asparaginase production by Aspergillus terreus MTCC 1782. Biotechnol Bioproc Eng, 16, 50–8
50. Gurunathan B, Sahadevan R. (2012). Optimization of culture conditions and bench-scale production of l-asparaginase by submerged fermentation of Aspergillus terreus MTCC 1782. J Microbiol Biotechnol, 22, 923–9
51. Gutierrez JA, Pan YX, Koroniak L, et al. (2006). An inhibitor of human asparagine synthetase suppresses proliferation of an l-asparaginase-resistant leukemia cell line. Chem Biol, 13, 1339–47
52. Harms E, Wehner A, Aung HP., Röhm KH. (1991). A catalytic role for threonine-12 of E. coli asparaginase II as established by site-directed mutagenesis. FEBS Lett, 285, 55–8
53. Harris JM, Chess RB. (2003). Effect of pegylation on pharmaceuticals. Nat Rev Drug Discov, 2, 214–21
54. Hashimoto K, Suzuki F, Sakagami H. (2009). Declined asparagine synthetase mRNA expression and enhanced sensitivity to asparaginase in HL-60 cells committed to monocytic differentiation. Anticancer Res, 4, 1303–8
55. Heitink-Pollé KM, Prinsen BH, de Koning TJ, et al. (2013). High incidence of symptomatic hyperammonemia in children with acute lymphoblastic leukemia receiving pegylated asparaginase. J Inherit Metab Dis, 7, 103–8
56. Hellman K, Miller DS, Cammack KA. (1983). The effect of freeze-drying on the quaternary structure of l-asparaginase from Erwinia carotovora. Biochim Biophys Acta, 749, 133–42
57. Holleman A, Cheok MH, den Boer ML, et al. (2004). Gene-expression patterns in drug-resistant acute lymphoblastic leukemia cells and response to treatment. N Engl J Med, 351, 533–42
58. Hosamani R, Kaliwal BB. (2011). l-asparaginase–an anti-tumor agent production by Fusarium equiseti using solid state fermentation. Int J Drug Discov, 3, 88–99
59. http://www.pymol.org [last accessed 17 Sep 2015]
60. http://www.clinicaltrials.gov/show/NCT01551524 [last accessed 29 May 2014]
61. http://www.rcsb.org [last accessed on 17 Sep 2015]
62. Hymavathi M, Sathish T, Rao CS, et al. (2009). Enhancement of l-asparaginase production by isolated Bacillus circulans (MTCC 8574) using response surface methodology. Appl Biochem Biotechnol, 159, 191–8
63. Ikeuchi H, Meyer ME, Ding Y, et al. (2009). A critical electrostatic interaction mediates inhibitor recognition by human asparagine synthetase. Bioorg Med Chem, 17, 6641–50
64. Ikeuchi H, Ahn YM, Otokawa T, et al. (2012). A sulfoximine-based inhibitor of human asparagine synthetase kills l-asparaginase-resistant leukemia cells. Bioorg Med Chem, 20, 5915–27
65. INCA. National Cancer Institute José Alencar Gomes da Silva. Available from:http://www.inca.gov.br/estimativa/2014/sintese-de-resultados-comentarios.asp [last accessed 27 May 2014]
66. Izutsu K, Yoshioka S, Terao T. (1994). Effect of mannitol crystallinity on the stabilization of enzymes during freeze-drying. Chem Pharm Bull, 42, 5–8
67. Jain R, Zaidi KU, Verma Y, et al. (2012). l-asparaginase:a promising enzyme for treatment of ALL. People’s J Sci Res, 5, 29–35
68. Jameel F, Bogner R, Mauri F, et al. (1997). Investigation of physicochemical changes to l-asparaginase during freeze–thaw cycling. J Pharm Pharmacol, 49, 472–7
69. Jaskólski M, Kozak M, Lubkowski J, et al. (2001). Structures of two highly homologous bacterial l-asparaginases:a case of enantiomorphic space groups. Acta Crystallogr D, 57, 369–77
70. Jian-Hang Z, Xi-Luan Y, Hong-Jun C, et al. (2007). In situ extraction of intracellular l-asparaginase using thermoseparating aqueous two-phase systems. J Chromatogr A, 1147, 127–34
71. Jianhua C, Yujun W, Ruibo J, et al. (2006). Probing the antigenicity of E. coli l-asparaginase by mutational analysis. Mol Biotechnol, 33, 57–65
72. Kafkewitz D, Bendich A. (1983). Enzyme-induced asparagine and glutamine depletion and immune system function. Am J Clin Nutr, 37, 1025–30
73. Kenari SLD, Alemzadeh I, Maghsodi V. (2011). Production of l-asparaginase from Escherichia coli ATCC 11303:optimization by response surface methodology. Food Bioprod Process, 89, 315–21
74. Kil JO, Kim GN, Park I. (1995). Extraction of extracellular l-asparaginase from Candida utilis. Biosci Biotechnol Biochem, 59, 749–50
75. Koshi A, Dhevendaran K, Georgekutty MI, et al. (1997). l-asparaginase in Streptomyces plicatus isolated from the alimentary canal of the fish, Gerres filamentosus (Cuvier). J Mar Biotechnol, 5, 181–5
76. Kotzia GA, Labrou NE. (2005). Cloning, expression and characterisation of Erwinia carotovoral-asparaginase. J Biotechnol, 119, 309–23
77. Kotzia GA, Labrou NE. (2007). l-asparaginase from Erwinia chrysanthemi 3937:cloning, expression and characterization. J Biotechnol, 127, 657–69
78. Kumar NSM, Manonmani HK. (2013). Purification, characterization and kinetic properties of extracellular l-asparaginase produced by Cladosporium sp. World J Microbiol Biotechnol, 29, 577–87
79. Kumar DS, Sobha K. (2012). l-Asparaginase from microbes:a comprehensive review. Adv Biol Res, 3, 137–57
80. Kumar S, Pakshirajan K, Venkata Dasu V. (2009). Development of medium for enhanced production of glutamine-free l-asparaginase from Pectobacterium carotovorum MTCC 1428. Appl Microbiol Biotechnol, 84, 477–86
81. Kumar S, Venkata Dasu V, Pakshirajan K. (2010). Localization and production of novel l-asparaginase from Pectobacterium carotovorum MTCC 1428. Proc Biochem, 45, 223–9
82. Kumar K, Kaur J, Walia S, et al. (2014). l-asparaginase, an effective agent in the treatment of acute lymphoblastic leukemia. Leuk Lymphoma, 55, 256–62
83. Kwon YM, Chung HS, Moon C, et al. (2009). l-asparaginase encapsulated intact erythrocytes for treatment of acute lymphoblastic leukemia (ALL). J Control Release, 139, 182–9
84. Lam H, Kavoosi M, Haynes CA, et al. (2004). Affinity-enhanced protein partitioning in decyl β-d-glucopyranoside two-phase aqueous micellar systems. Biotechnol Bioeng, 89, 381–92
85. Lapmak K, Lumyong S, Thongkuntha S, et al. (2010). l-asparaginase production by Bipolaris sp. BR438 isolated from brown rice in Thailand. Chinag Mai J Sci, 37, 160–4
86. Lebedeva ZI, Berezov TT. (1997). Improved method of purification and properties of glutaminase-asparaginase from Pseudomonas aurantiaca 548. B Exp Biol Med, 124, 1156–8
87. Loureiro CB, Borges KS, Andrade AF, et al. (2012). Purification and biochemical characterization of native and pegylated form of l-asparaginase from Aspergillus terreus and evaluation of its antiproliferative activity. Adv Microbiol, 2, 138–45
88. Lubkowski J, Palm GJ, Gilliland GL, et al. (1996). Crystal structure and amino acid sequence of Wolinella succinogenesl-asparaginase. Eur J Biochem, 241, 201–7
89. Lubkowski J, Dauter M, Aghaiypour K, et al. (2003). Atomic resolution structure of Erwinia chrysanthemil-asparaginase. Acta Crystallogr D, 59, 84–92
90. Mahajan RV, Saran S, Kameswaran K, et al. (2012). Efficient production of l-asparaginase from Bacillus licheniformis with low-glutaminase activity:optimization, scale up and acrylamide degradation studies. Bioresour Technol, 125, 11–16
91. Manna S, Sinha A, Sadhukhan R, et al. (1995). Purification, characterization and antitumor activity of l-asparaginase isolated from Pseudomonas stutzeri MB-405. Curr Microbiol, 30, 291–8
92. Mashburn LT, Wriston JC. (1963). Tumor inhibitory effect of l-asparaginase. Biochem Biophys Res Commun, 12, 50–5
93. Mehta RK, Verma S, Pati R, et al. (2014). Mutations in subunit interface and B-cell epitopes improve antileukemic activities of Escherichia coli asparaginase-II. J Biol Chem, 289, 3555–70
94. Mehvar R. (2000). Modulation of the pharmacokinetics and pharmacodynamics of proteins by polyethylene glycol conjugation. J Pharm Sci, 3, 125–36
95. Michalska K, Jaskolski M. (2006). Structural aspects of l-asparaginases, their friends and relations. Acta Biochim Pol, 53, 627–40
96. Minim LA, Alegre M. (1992). Production of enzyme l-asparaginase from Erwinia aroideae. Arq Biol Tecnol, 35, 277–83
97. Mishra A. (2006). Production of l-asparaginase, an anticancer agent, from Aspergillus niger using agricultural waste in solid state fermentation. Appl Biochem Biotechnol, 135, 33–42
98. Moorthy V, Ramalingam A, Sumantha A, et al. (2010). Production, purification and characterisation of extracellular l-asparaginase from a soil isolate of Bacillus sp. Afr J Microbiol Res, 4, 1862–7
99. Nair A, Kumar R, Agalya Devi R, et al. (2013). Screening of commonly available solid process residues as substrate for l-asparaginase production by Aspergillus terreus MTCC 1782. Res J Pharm Biol Chem Sci, 4, 1731–7
100. Narayana KJP, Kumar KG, Vijayalakshmi M. (2008). l-asparaginase production by Streptomyces albidoflavus. Indian J. Microbiol, 48, 331–6
101. Nawaz MS, Zhang D, Khan AA, et al. (1998). Isolation and characterization of Enterobacter cloacae capable of metabolizing asparagine. Appl Microbiol Biotechnol, 50, 568–72
102. Offman MN, Krol M, Patel N, et al. (2011). Rational engineering of l-asparaginase reveals importance of dual activity for cancer cell toxicity. Blood, 17, 1614–21
103. Palm GJ, Lubkowski J, Derst C, et al. (1996). A covalently bound catalytic intermediate in Escherichia coli asparaginase:crystal structure of a Thr-89-Val mutant. FEBS Lett, 390, 211–16
104. Parmentier JH, Maggi M, Tarasco E, et al. (2015). Glutaminase activity determines cytotoxicity of l-asparaginases on most leukemia cell lines. Leuk Res, 39, 757–62
105. Pasut G, Veronese FM. (2009). PEG conjugates in clinical development or use as anticancer agents:an overview. Adv Drug Deliv Rev, 61, 1177–88
106. Pasut G, Sergi M, Veronese FM. (2008). Anti-cancer PEG-enzymes:30 years old, but still a current approach. Adv Drug Deliv Rev, 60, 69–78
107. Patel N, Krishnan S, Offman MN, et al. (2009). A dyad of lymphoblastic lysosomal cysteine proteases degrades the antileukemic drug l-asparaginase. J Clin Invest, 119, 1964–73
108. Patro KRP, Basak UC, Mohapatra AK, et al. (2014). Development of new medium composition for enhanced production of l-asparaginase by Aspergillus flavus. J Environ Biol, 12, 167–74
109. Pieters R, Hunger SP, Boos J, et al. (2011). l-asparaginase treatment in acute lymphoblastic leukemia. Cancer, 117, 238–49
110. Pinheiro IO, Araujo JM, Ximenes ECPA, et al. (2001). Production of l-asparaginase by Zymomonas mobilis strain CP4. Biomater Diagn, 6, 243–4
111. Prakasham RS, Rao ChS, Rao RS, et al. (2007). l-asparaginase production by isolated Staphylococcus sp.–6A:design of experiment considering interaction effect for process parameter optimization. J Appl Microbiol, 102, 1382–91
112. Pritsa AA, Kyriakidis DA. (2001). l-asparaginase of Thermus thermophilus:purification, properties and identification of essential amino acids for its catalytic activity. Mol Cell Biochem, 216, 93–101
113. Pui CH, Evans WE. (2006). Treatment of acute lymphoblastic leukemia. N Engl J Med, 354, 166–78
114. Pui CH, Howard SC. (2008). Current management and challenges of malignant disease in the CNS in pediatric leukemia. Lancet Oncol, 9, 257–68
115. Qin M, Zhao F. (2003). l-asparaginase release from Escherichia coli cells with aqueous two-phase micellar systems. Appl Biochem Biotechnol, 110, 11–21
116. Raha SK, Roy SK, Dey SK, et al. (1990). Purification and properties of an l-asparaginase from Cylindrocarpon obtusisporum MB-10. Biochem Int, 21, 987–1000
117. Ramaiah N, Chandramohan D. (1992). Production of l-asparaginase from marine luminous bacteria. Indian J Mar Sci, 21, 212–14
118. Ramakrishnan MS, Joseph R. (1996). Characterization of an extracellular asparaginase of Rhodosporidium toruloides CBS14 exhibiting unique physicochemical properties. Can J Microbiol, 42, 316–25
119. Ramya LN, Doble M, Rekha VP, et al. (2012). l-asparaginase as potent anti-leukemic agent and its significance of having reduced glutaminase side activity for better treatment of acute lymphoblastic leukaemia. Appl Biochem Biotechnol, 167, 2144–59
120. Rani SA, Sundaram L, Vasantha PB. (2012). Isolation and screening of l-asparaginase producing fungi from soil samples. Int J Pharm Pharm Sci, 4, 279–82
121. Richards NG, Kilberg MS. (2006). Asparagine synthetase chemotherapy. Annu Rev Biochem, 75, 629–54
122. Rizzari C, Conter V, Starý J, et al. (2013). Optimizing asparaginase therapy for acute lymphoblastic leukemia. Curr Opin Oncol, 1, 1–9
123. Rytting ME. (2012). Role of l-asparaginase in acute lymphoblastic leukemia:focus on adult patients. Blood Lymphatic Cancer Targets Ther, 2, 117–24
124. Sanches M, Barbosa JA, Oliveira RT, et al. (2003). Structural comparison of Escherichia colil-asparaginase in two monoclinic space groups. Acta Crystallogr D, 59, 416–22
125. Sangeetha PT, Ramesh MN, Prapulla SG. (2004). Production of fructosyl transferase by Aspergillus oryzae CFR202 in solid-state fermentation using agricultural by-products. Appl Microbiol Biotechnol, 65, 530–7
126. Sarquis MI, Oliveira EM, Santos AS, et al. (2004). Production of l-asparaginase by filamentous fungi. Mem Inst Oswaldo Cruz, 99, 489–92
127. Schalk AM, Lavie A. (2014). Structural and kinetic characterization of guinea pig l-asparaginase type III. Biochemistry, 53, 2318–28
128. Sette LD, Pagnocca FC, Rodrigues A. (2013). Microbial culture collections as pillars for promoting fungal diversity, conservation and exploitation. Fungal Genet Biol, 60, 2–8
129. Shrivastava A, Khan AA, Shrivastav A, et al. (2012). Kinetic studies of l-asparaginase from Penicillium digitatum. Prep Biochem Biotechnol, 42, 574–81
130. Shrivastava A, Khan AA, Khurshid M, et al. (2015). Recent developments in l-asparaginase discovery and its potential as anticancer agent. Crit Rev Oncol Hematol, doi:10.1016/j.critrevonc.2015.01.002
131. Sidoruk KV, Pokrovsky VS, Borisova AA, et al. (2011). Creation of a producent, optimization of expression, and purification of recombinant Yersinia pseudotuberculosisl-asparaginase. B Exp Biol Med, 152, 219–23
132. Singh SK, Kolhe P, Wang W, et al. (2009). Large-scale freezing of biologics–a practitioner's review, part one:fundamental aspects. BioProcess Int, 7, 32–44
133. Singh Y, Gundampati RK, Jagannadham MV, et al. (2013). Extracellular l-asparaginase from a protease-deficient Bacillus aryabhattai ITBHU02:purification, biochemical characterization, and evaluation of antineoplastic activity in vitro. Appl Biochem Biotechnol, 171, 1759–74
134. Sinha A, Manna S, Rey SK, et al. (1991). Induction of l-asparaginase synthesis in Vibrio proteus. Indian J Med Res, 93, 289–92
135. Soares AL, Guimarães GM, Polakiewicz B, et al. (2002). Effects of polyethylene glycol attachment on physicochemical and biological stability of E. coli l-asparaginase. Int J Pharm, 237, 163–70
136. Souza RL, Ventura SP, Soares CM, et al. (2015). Lipase purification using ionic liquids as adjuvants in aqueous two-phase systems. Green Chem, 17, 3026–34
137. Sudha SS. (2009). Marine environment:a potential source for l-asparaginase producing microorganisms. IUP J Biotechnol, 3, 57–62
138. Sundaramoorthi C, Rajakumari R, Dharamsi A, et al. (2012). Production and immobilization of l-asparaginase from marine source. Int J Pharm Pharm Sci, 4, 229–32
139. Swain AL, Jaskólski M, Housset D, et al. (1993). Crystal structure of Escherichia colil-asparaginase, an enzyme used in cancer therapy. Proc Natl Acad Sci USA, 90, 1474–8
140. Tabandeh MR, Aminlari M. (2009). Synthesis, physicochemical and immunological properties of oxidized inulin–l-asparaginase bio conjugate. J Biotechnol, 141, 189–95
141. Tardito S, Uggeri J, Bozzetti C, et al. (2007). The inhibition of glutamine synthetase sensitizes human sarcoma cells to l-asparaginase. Cancer Chemother Pharmacol, 60, 751–8
142. Thakur M, Lincoln L, Niyonzima FN, et al. (2014). Isolation, purification and characterization of fungal extracellular l-asparaginase from Mucor hiemalis. J Biocatal Biotransform, 2, 12–14
143. Theantana T, Hyde KD, Lumyong S. (2007). Asparaginase production by endophytic fungi isolated from some Thai medicinal plants. KMITL Sci Tech J, 7, 13–18
144. Theantana T, Hyde KD, Lumyong S. (2009). Asparaginase production by endophytic fungi from Thai medicinal plants:cytotoxicity properties. Int J Integr Biol, 7, 1–8
145. Thenmozhi C, Sankar R, Karuppiah V, et al. (2011). l-asparaginase production by mangrove derived Bacillus cereus MAB5:optimization by response surface methodology. Asian Pac J Trop Med, 4, 486–91
146. Thirunavukkarasu N, Suryanarayanan TS, Murali TS, et al. (2011). l-asparaginase from marine derived fungal endophytes of seaweeds. Mycosphere, 2, 147–55
147. Tippani R, Sivadevuni G. (2012). Nutritional factors effecting the production of l-asparaginase by the Fusarium sp. Afr J Biotechnol, 11, 3692–6
148. Tirosh O, Barenholz Y, Katzhendler J, et al. (1998). Hydration of polyethylene glycol-grafted liposomes. Biophys J, 74, 1371–9
149. Tong WH, Pieters R, Kaspers GJ, et al. (2014). A prospective study on drug monitoring of PEG-l-asparaginase and Erwinia asparaginase and asparaginase antibodies in pediatric acute lymphoblastic leukemia. Blood, 123, 2026–33
150. Uppuluri KB, Reddy DSR. (2009). Optimization of l-asparaginase production by isolated Aspergillus niger using sesame cake in a column bioreactor. J Pure Appl Microbiol, 3, 83–90
151. Uppuluri KB, Dasari RKVR, Sajja V, et al. (2013). Optimization of l-asparaginase production by isolated Aspergillus niger C4 from sesame (black) oil cake under SSF using Box–Behnken design in column bioreactor. Int J Chem React Eng, 11, 103–9
152. Venil C, Lakshmanaperumalsamy P. (2009). Solid-state fermentation for production of l-asparaginase in rice bran by Serratia marcescens SB08. Int J Microbiol, 7, 30
153. Verma S, Mehta RK, Maiti P, et al. (2014). Improvement of stability and enzymatic activity by site-directed mutagenesis of E. coli asparaginase II. Biochim Biophys Acta, 1844, 1219–30
154. Verna N, Kumar G, Anand S. (2007). l-asparaginase:a promising chemotherapeutic agent. Crit Rev Biotechnol, 27, 45–62
155. Veronese FM, Pasut G. (2005). PEGylation, successful approach to drug delivery. Drug Discov Today, 10, 1451–8
156. Veronese FM. (2001). Protein and protein PEGylation:a review of problems and solutions. Biomaterials, 22, 405–17
157. Villa P, Corada M, Bartosek I. (1986). l-asparaginase effects on inhibition of protein synthesis and lowering of the glutamine content in cultured rat hepatocytes. Toxicol Lett, 32, 235–41
158. Vuddaraju SP, Nikku MY, Chaduvula AIR, et al. (2010). Application of statistical experimental designs for the optimization of medium constituents for the production of l-asparaginase by Serratia marcescens. J Microbial Biochem Technol, 2, 89–94
159. Warangkar SC, Khobragade CN. (2010). Purification, characterization, and effect of thiol compounds on activity of the Erwinia carotovoral-asparaginase. Enzyme Res, 1, 1–10
160. Ward KR, Adams GD, Alpar HO, et al. (1999). Protection of the enzyme l-asparaginase during lyophilisation a molecular modelling approach to predict required level of lyoprotectant. Int J Pharm, 187, 153–62
161. Wehner A, Harms E, Jennings MP, et al. (1992). Site-specific mutagenesis of Escherichia coli asparaginase II. Eur J Biochem, 208, 475–80
162. Wei DZ, Liu H. (1998). Promotion of l-asparaginase using n-dodecane. Biotechnol Technol, 12, 129–31
163. Werner A, Röhm, KH, Mller, HJ. (2005). Mapping of B-cell epitopes in E. coli asparaginase II, an enzyme used in leukemia treatment. Biol Chem, 386, 535–40
164. Wypij JM, Pondenis HC. (2013). E. coli-derived l-asparaginase retains enzymatic and cytotoxic activity in vitro for canine and feline lymphoma after cold storage. Vet Med Int, doi:10.1155/2013/786162
165. Yang BB, Lum PK, Hayashi MM, et al. (2004). Polyethylene glycol modification of filgrastim results in decreased renal clearance of the protein in rats. J Pharm Sci, 93, 1367–73
166. Zia MA, Bashir R, Ahmed I, et al. (2013). Production of l-asparaginase from Aspergillus niger using agro wastes by-products in submerged fermentation process. J Teknol, 62, 47–51