[1]
Vellard, M. The enzyme as drug: application of enzymes as pharmaceuticals. Curr. Opin. Biotechnol., 2003, 14(4), 444-450.
[2]
Kidd, J.G. Regression of transplanted lymphomas induced in vivo by means of normal guinea pig serum: I. course of transplanted cancers of various kinds in mice and rats given guinea pig serum, horse serum, or rabbit serum. J. Exp. Med., 1953, 98(6), 565-582.
[3]
Broome, J. Evidence that the L-asparaginase of guinea pig serum is responsible for its antilymphoma effects: I. properties of the L-asparaginase of guinea pig serum in relation to those of the antilymphoma substance. J. Exp. Med., 1963, 118(1), 99-120.
[4]
Mashburn, L.T.; Wriston, Jr, J.C. Tumor inhibitory effect of L-asparaginase from Escherichia coli. Arch. Biochem. Biophys., 1964, 105(2), 450-453.
[5]
Yellin, T.O.; Wriston, Jr, J.C. Purification and properties of guinea pig serum asparaginase. Biochemistry, 1966, 5(5), 1605-1612.
[6]
Campbell, H.; Mashburn, L.; Boyse, E.; Old, L. Two L-asparaginases from Escherichia coli B. Their separation, purification, and antitumor activity. Biochemistry, 1967, 6(3), 721-730.
[7]
Wade, H.; Elsworth, R.; Herbert, D.; Keppie, J.; Sargeant, K. A new L-asparaginase with antitumour activity. Lancet, 1968, 292(7571), 776-777.
[8]
Salzer, W.; Seibel, N.; Smith, M. Erwinia asparaginase in pediatric acute lymphoblastic leukemia. Expert Opin. Biol. Ther., 2012, 12(10), 1407-1414.
[9]
Capizzi, R.L.; Bertino, J.; Skeel, R.; Creasey, W.; Zanes, R.; Olayon, C.; Peterson, R.; Handschumacher, R. L-asparaginase: Clinical, biochemical, pharmacological, and immunological studies. Ann. Intern. Med., 1971, 74(6), 893-901.
[10]
Haskell, C.; Canellos, G. l-asparaginase resistance in human leukemia—asparagine synthetase. Biochem. Pharmacol., 1969, 18(10), 2578-2580.
[11]
Kiriyama, Y.; Kubota, M.; Takimoto, T.; Kitoh, T.; Tanizawa, A.; Akiyama, Y.; Mikawa, H. Biochemical characterization of U937 cells resistant to L-asparaginase: The role of asparagine synthetase. Leukemia, 1989, 3(4), 294-297.
[12]
Stams, W.A.; den Boer, M.L.; Beverloo, H.B.; Meijerink, J.P.; Stigter, R.L.; van Wering, E.R.; Janka-Schaub, G.E.; Slater, R.; Pieters, R. Sensitivity to L-asparaginase is not associated with expression levels of asparagine synthetase in t (12; 21)+ pediatric ALL. Blood, 2003, 101(7), 2743-2747.
[13]
Broome, J. L-Asparaginase: Discovery and development as a tumor-inhibitory agent. Cancer Treat. Rep., 1981, 65, 111-114.
[14]
Iiboshi, Y.; Papst, P.J.; Hunger, S.P.; Terada, N. L-Asparaginase inhibits the rapamycin-targeted signaling pathway. Biochem. Biophys. Res. Commun., 1999, 260(2), 534-539.
[15]
Story, M.D.; Voehringer, D.W.; Stephens, L.C.; Meyn, R.E. L-asparaginase kills lymphoma cells by apoptosis. Cancer Chemother. Pharmacol., 1993, 32(2), 129-133.
[16]
Ueno, T.; Ohtawa, K.; Mitsui, K.; Kodera, Y.; Hiroto, M.; Matsushima, A.; Inada, Y.; Nishimura, H. Cell cycle arrest and apoptosis of leukemia cells induced by L-asparaginase. Leukemia, 1997, 11(11), 1858.
[17]
Avramis, V.I.; Tiwari, P.N. Asparaginase (native ASNase or pegylated ASNase) in the treatment of acute lymphoblastic leukemia. Int. J. Nanomedicine, 2006, 1(3), 241.
[18]
Shrivastava, A.; Khan, A.A.; Khurshid, M.; Kalam, M.A.; Jain, S.K.; Singhal, P.K. Recent developments in l-asparaginase discovery and its potential as anticancer agent. Crit. Rev. Oncol. Hematol., 2016, 100, 1-10.
[19]
Nesbit, M.; Chard, R.; Evans, A.; Karon, M.; Hammond, G.D. Evaluation of intramuscular versus intravenous administration of L-asparaginase in childhood leukemia. Am. J. Pediatr. Hematol. Oncol., 1979, 1(1), 9-13.
[20]
Panosyan, E.H.; Seibel, N.L.; Martin-Aragon, S.; Gaynon, P.S.; Avramis, I.A.; Sather, H.; Franklin, J.; Nachman, J.; Ettinger, L.J.; La, M. Asparaginase antibody and asparaginase activity in children with higher-risk acute lymphoblastic leukemia: Children’s Cancer Group Study CCG-1961. J. Pediatr. Hematol. Oncol., 2004, 26(4), 217-226.
[21]
Asselin, B.L. The three asparaginases. In: Drug resistance in leukemia and lymphoma III; Springer, 1999; pp. 621-629.
[22]
Zalewska-Szewczyk, B.; Andrzejewski, W.; Młynarski, W.; Jędrychowska-Dańska, K.; Witas, H.; Bodalski, J. The anti-asparagines antibodies correlate with L-asparagines activity and may affect clinical outcome of childhood acute lymphoblastic leukemia. Leuk. Lymphoma, 2007, 48(5), 931-936.
[23]
Alberts, S.R.; Bretscher, M.; Wiltsie, J.C.; O’neill, B.P.; Mokri, B.; Witzig, T.E. Thrombosis related to the use of L-asparaginase in adults with acute lymphoblastic leukemia: A need to consider coagulation monitoring and clotting factor replacement. Leuk. Lymphoma, 1999, 32(5-6), 489-496.
[24]
Beinart, G.; Damon, L. Thrombosis associated with l‐asparaginase therapy and low fibrinogen levels in adult acute lymphoblastic leukemia. Am. J. Hematol., 2004, 77(4), 331-335.
[25]
Nowak-Göttl, U.; Ahlke, E.; Fleischhack, G.; Schwabe, D.; Schobess, R.; Schumann, C.; Junker, R. Thromboembolic events in children with acute lymphoblastic leukemia (BFM protocols): Prednisone versus dexamethasone administration. Blood, 2003, 101(7), 2529-2533.
[26]
Knoderer, H.M.; Robarge, J.; Flockhart, D.A. Predicting asparaginase‐associated pancreatitis. Pediatr. Blood Cancer, 2007, 49(5), 634-639.
[27]
Raja, R.A.; Schmiegelow, K.; Frandsen, T.L. Aspara-ginase‐associated pancreatitis in children. Br. J. Haematol., 2012, 159(1), 18-27.
[28]
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.
[29]
Husain, I.; Sharma, A.; Kumar, S.; Malik, F. Purification and characterization of glutaminase free asparaginase from Pseudomonas otitidis: Induce apoptosis in human leukemia MOLT-4 cells. Biochimie, 2016, 121, 38-51.
[30]
Narta, U.; Roy, S.; Kanwar, S.S.; Azmi, W. Improved production of L-asparaginase by Bacillus brevis cultivated in the presence of oxygen-vectors. Bioresour. Technol., 2011, 102(2), 2083-2085.
[31]
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.
[32]
Batool, T.; Makky, E.A.; Jalal, M.; Yusoff, M.M. A comprehensive review on L-asparaginase and its applications. Appl. Biochem. Biotechnol., 2016, 178(5), 900-923.
[33]
Lubkowski, J.; Palm, G.J.; Gilliland, G.L.; Derst, C.; Röhm, K.H.; Wlodawer, A. Crystal structure and amino acid sequence of Wolinella succinogenes l‐asparaginase. Eur. J. Biochem., 1996, 241(1), 201-207.
[34]
Distasio, J.A.; Niederman, R.A.; Kafkewitz, D.; Goodman, D. Purification and characterization of L-asparaginase with anti-lymphoma activity from Vibrio succinogenes. J. Biol. Chem., 1976, 251(22), 6929-6933.
[35]
Covini, D.; Tardito, S.; Bussolati, O.R.; Chiarelli, L.V.; Pasquetto, M.; Digilio, R.; Valentini, G.; Scotti, C. Expanding targets for a metabolic therapy of cancer: L-asparaginase. Recent Patents Anticancer Drug Discov., 2012, 7(1), 4-13.
[36]
Nefelova, M.; Ignatov, S.; Chigalenchik, A.; Vinogradov, B.; Egorov, N. Biosynthesis of L-asparaginase-2 by cultures of Bacillus polymyxa var. Ross. Prikl. Biokhim. Mikrobiol., 1978, 14(4), 510-514.
[37]
Moola, Z.B.; Scawen, M.; Atkinson, T.; Nicholls, D. Erwinia chrysanthemi L-asparaginase: epitope mapping and production of antigenically modified enzymes. Biochem. J., 1994, 302(3), 921-927.
[38]
Tiwari, N.; Dua, R. Purification and preliminary characterization of L-asparaginase from Erwinia aroideae NRRL B-138. Indian J. Biochem. Biophys., 1996, 33(5), 371-376.
[39]
Stark, R.; Suleiman, M.S.; Hassan, I.; Greenman, J.; Millar, M. Amino acid utilisation and deamination of glutamine and asparagine by Helicobacter pylori. J. Med. Microbiol., 1997, 46(9), 793-800.
[40]
Pastuszak, I.; Szymona, M. Purification and properties of L-asparaginase from Mycobacterium phlei. Acta Biochim. Pol., 1976, 23(1), 37-44.
[41]
Rowly, B.; Wriston, J. L-asparaginase from Serratia marcescens. Biochem. Biophys. Res. Commun., 1967, 28, 160-171.
[42]
Manna, S.; Sinha, A.; Sadhukhan, R.; Chakrabarty, S. Purification, characterization and antitumor activity of L-asparaginase isolated from Pseudomonas stutzeri MB-405. Curr. Microbiol., 1995, 30(5), 291-298.
[43]
Rozalska, M.; Mikucki, J. Staphylococcal L-asparaginase: catabolic repression of synthesis. Acta Microbiol. Pol., 1992, 41(3-4), 145-150.
[44]
Curran, M.P.; Daniel, R.M.; Guy, G.R.; Morgan, H.W. A specific L-asparaginase from Thermus aquaticus. Arch. Biochem. Biophys., 1985, 241(2), 571-576.
[45]
Tosa, T.; Sano, R.; Yamamoto, K.; Nakamura, M.; Chibata, I. L-Asparaginase form Proteus vulgaris. Purification, crystallization, and enzymic properties. Biochemistry, 1972, 11(2), 217-222.
[46]
Kumar, S.; Dasu, V.V.; Pakshirajan, K. Purification and characterization of glutaminase-free L-asparaginase from Pectobacterium carotovorum MTCC 1428. Bioresour. Technol., 2011, 102(2), 2077-2082.
[47]
Singh, Y.; Gundampati, R.K.; Jagannadham, M.V.; Srivastava, S. Extracellular L-asparaginase from a protease-deficient Bacillus aryabhattai ITBHU02: purification, biochemical characterization, and evaluation of antineoplastic activity in vitro. Appl. Biochem. Biotechnol., 2013, 171(7), 1759-1774.
[48]
Mahajan, R.V.; Kumar, V.; Rajendran, V.; Saran, S.; Ghosh, P.C.; Saxena, R.K. Purification and characterization of a novel and robust L-asparaginase having low-glutaminase activity from Bacillus licheniformis: In vitro evaluation of anti-cancerous properties. PLoS One, 2014, 9(6), e99037.
[49]
Badoei-Dalfard, A. Purification and characterization of l-asparaginase from Pseudomonas aeruginosa strain SN004: Production optimization by statistical methods. Biocatal. Agric. Biotechnol., 2015, 4(3), 388-397.
[50]
Husain, I.; Sharma, A.; Kumar, S.; Malik, F. Purification and characterization of glutaminase free asparaginase from Enterobacter cloacae: in-vitro evaluation of cytotoxic potential against human myeloid leukemia HL-60 cells. PLoS One, 2016, 11(2), e0148877.
[51]
Shakambari, G.; Birendranarayan, A.K.; Lincy, M.J.A.; Rai, S.K.; Ahamed, Q.T.; Ashokkumar, B.; Saravanan, M.; Mahesh, A.; Varalakshmi, P. Hemocompatible glutaminase free L-asparaginase from marine Bacillus tequilensis PV9W with anticancer potential modulating p53 expression. RSC Advances, 2016, 6(31), 25943-25951.
[52]
Dejong, P.J. L-Asparaginase production by Streptomyces griseus. Appl. Microbiol., 1972, 23(6), 1163-1164.
[53]
Narayana, K.; Kumar, K.; Vijayalakshmi, M. L-asparaginase production by Streptomyces albidoflavus. Indian J. Microbiol., 2008, 48(3), 331-336.
[54]
Basha, N.S.; Rekha, R.; Komala, M.; Ruby, S. Production of extracellular anti-leukaemic enzyme l asparaginase from marine actinomycetes by solid state and submerged fermentation: Purification and characterisation. Trop. J. Pharm. Res., 2009, 8(4), 353-360.
[55]
Kavitha, A.; Vijayalakshmi, M. Optimization and purification of L-asparaginase produced by Streptomyces tendae TK-VL_333. Zeitschrift für Naturforschung. C, 2010, 65(7-8), 528-531.
[56]
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.
[57]
El-Naggar, N.E-A.; Deraz, S.F.; Soliman, H.M.; El-Deeb, N.M.; El-Ewasy, S.M. Purification, characterization, cytotoxicity and anticancer activities of L-asparaginase, anti-colon cancer protein, from the newly isolated alkaliphilic Streptomyces fradiae NEAE-82. Sci. Rep., 2016, 6, 32926.
[58]
Saxena, R.K.; Sinha, U. L-asparaginase and glutaminase activities in the culture filtrates of Aspergillus nidulans. Curr. Sci., 1981.
[59]
Sarquis, M.I.; Oliveira, E.M.; Santos, A.S.; Costa, G.L. Production of L-asparaginase by filamentous fungi. Mem. Inst. Oswaldo Cruz, 2004, 99(5), 489-492.
[60]
Mohapatra, B.; Bapuji, M.; Banerjee, U. Production and properties of L-asparaginase from Mucor species associated with a marine sponge (Spirastrella sp.). Cytobios, 1997, 92(370-371), 165-173.
[61]
Mishra, A. Production of L-asparaginase, an anticancer agent, from Aspergillus niger using agricultural waste in solid state fermentation. Appl. Biochem. Biotechnol., 2006, 135(1), 33-42.
[62]
Nakahama, K.; Imada, A.; Igarasi, S.; Tubaki, K. Formation of L-asparaginase by Fusarium species. Microbiology, 1973, 75(2), 269-273.
[63]
Shrivastava, A.; Khan, A.A.; Shrivastav, A.; Jain, S.K.; Singhal, P.K. Kinetic studies of L-asparaginase from Penicillium digitatum. Prep. Biochem. Biotechnol., 2012, 42(6), 574-581.
[64]
Baskar, G.; Renganathan, S. Optimization of L‐asparaginase production by Aspergillus terreus MTCC 1782 using response surface methodology and artificial neural network‐linked genetic algorithm. Asia-Pac. J. Chem. Eng., 2012, 7(2), 212-220.
[65]
Elshafei, A.M.; Hassan, M.M.; Abd, M.; Abouzeid, E.; Mahmoud, D.A.; Elghonemy, D.H. Purification, characterization and antitumor activity of L-asparaginase from Penicillium brevicompactum 2 NRC 829 3. Br. Microbiol. Res. J., 2011, 2(3), 158-174.
[66]
Farag, A.M.; Hassan, S.W.; Beltagy, E.A.; El-Shenawy, M.A. Optimization of production of anti-tumor l-asparaginase by free and immobilized marine Aspergillus terreus. Egypt. J. Aquat. Res., 2015, 41(4), 295-302.
[67]
Dias, F.F.; Sato, H.H. Sequential optimization strategy for maximum l-asparaginase production from Aspergillus oryzae CCT 3940. Biocatal. Agric. Biotechnol., 2016, 6, 33-39.
[68]
Jones, G.E.; Mortimer, R.K. Biochemical properties of yeast L-asparaginase. Biochem. Genet., 1973, 9(2), 131-146.
[69]
Dunlop, P.C.; Roon, R.J. L-Asparaginase of Saccharomyces cerevisiae: An extracellular Enzyme. J. Bacteriol., 1975, 122(3), 1017-1024.
[70]
Kil, J-O.; Kim, G-N.; Park, I. Extraction of extracellular L-asparaginase from Candida utilis. Biosci. Biotechnol. Biochem., 1995, 59(4), 749-750.
[71]
Paul, J. Isolation and characterization of a Chlamydomonas L-asparaginase. Biochem. J., 1982, 203(1), 109-115.
[72]
Mohamed, S.A.; Elshal, M.F.; Kumosani, T.A.; Aldahlawi, A.M. Purification and characterization of asparaginase fromPhaseolus
vulgaris seeds. Evid. Based Complement. Alternat. Med.,; , 2015, 2015, . Article ID 309214, 6 pages
[73]
Shanmugaprakash, M.; Jayashree, C.; Vinothkumar, V.; Senthilkumar, S.; Siddiqui, S.; Rawat, V.; Arshad, M. Biochemical characterization and antitumor activity of three phase partitioned L-asparaginase from Capsicum annuum L. Separ. Purif. Tech., 2015, 142, 258-267.
[74]
Kim, S-K.; Min, W-K.; Park, Y-C.; Seo, J-H. Application of repeated aspartate tags to improving extracellular production of Escherichia coli L-asparaginase isozyme II. Enzyme Microb. Technol., 2015, 79, 49-54.
[75]
Vidya, J.; Sajitha, S.; Ushasree, M.V.; Sindhu, R.; Binod, P.; Madhavan, A.; Pandey, A. Genetic and metabolic engineering approaches for the production and delivery of L-asparaginases: An overview. Bioresour. Technol., 2017, 245, 1775-1781.
[76]
Ferrara, M.A.; Severino, N.M.; Mansure, J.J.; Martins, A.S.; Oliveira, E.M.; Siani, A.C.; Pereira, Jr, N.; Torres, F.A.; Bon, E.P. Asparaginase production by a recombinant Pichia pastoris strain harbouring Saccharomyces cerevisiae ASP3 gene. Enzyme Microb. Technol., 2006, 39(7), 1457-1463.
[77]
Hatanaka, T.; Usuki, H.; Arima, J.; Uesugi, Y.; Yamamoto, Y.; Kumagai, Y.; Yamasato, A.; Mukaihara, T. Extracellular production and characterization of two Streptomyces L-asparaginases. Appl. Biochem. Biotechnol., 2011, 163(7), 836-844.
[78]
Huang, L.; Liu, Y.; Sun, Y.; Yan, Q.; Jiang, Z. Biochemical characterization of a novel L-Asparaginase with low glutaminase activity from Rhizomucor miehei and its application in food safety and leukemia treatment. Appl. Environ. Microbiol., 2014, 80(5), 1561-1569.
[79]
Ghoshoon, M.B.; Berenjian, A.; Hemmati, S.; Dabbagh, F.; Karimi, Z.; Negahdaripour, M.; Ghasemi, Y. Extracellular production of recombinant L-Asparaginase II in Escherichia coli: Medium optimization using response surface methodology. Int. J. Pept. Res. Ther., 2015, 21(4), 487-495.
[80]
Han, S.; Jung, J.; Park, W. Biochemical characterization of L-asparaginase in NaCl-tolerant Staphylococcus sp. OJ82 isolated from fermented seafood. J. Microbiol. Biotechnol., 2014, 24(8), 1096-1104.
[81]
Chityala, S.; Dasu, V.V.; Ahmad, J.; Prakasham, R.S. High yield expression of novel glutaminase free L-asparaginase II of Pectobacterium carotovorum MTCC 1428 in Bacillus subtilis WB800N. Bioprocess Biosyst. Eng., 2015, 38(11), 2271-2284.
[82]
Sajitha, S.; Vidya, J.; Binod, P.; Pandey, A. Cloning and expression of l-asparaginase from E. coli in eukaryotic expression system. Biochem. Eng. J., 2015, 102, 14-17.
[83]
Feng, Y.; Liu, S.; Jiao, Y.; Gao, H.; Wang, M.; Du, G.; Chen, J. Enhanced extracellular production of L-asparaginase from Bacillus subtilis 168 by B. subtilis WB600 through a combined strategy. Appl. Microbiol. Biotechnol., 2017, 101(4), 1509-1520.
[84]
Kishore, V.; Nishita, K.; Manonmani, H. Cloning, expression and
characterization of l-asparaginase from Pseudomonas fluorescens for large scale production in E. coli BL21 3 Biotech, 2015, 5 (6), 975-981.
[85]
Yano, S.; Minato, R.; Thongsanit, J.; Tachiki, T.; Wakayama, M. Overexpression of type I L-asparaginase of Bacillus subtilis in Escherichia coli, rapid purification and characterisation of recombinant type I L-asparaginase. Ann. Microbiol., 2008, 58(4), 711-716.
[86]
Oza, V.P.; Parmar, P.P.; Patel, D.H.; Subramanian, R. Cloning, expression and characterization of l-asparaginase from Withania somnifera L. for large scale production. 3 Biotech, 2011, 1 1(1), 21-26.
[87]
Kotzia, G.A.; Labrou, N.E. L-Asparaginase from Erwinia chrysanthemi 3937: Cloning, expression and characterization. J. Biotechnol., 2007, 127(4), 657-669.
[88]
El-Sharkawy, A.S.; Farag, A.M.; Embaby, A.M.; Saeed, H.; El-Shenawy, M. Cloning, expression and characterization of aeruginosa EGYII L-Asparaginase from Pseudomonas aeruginosa strain EGYII DSM 101801 in E. coli BL21 (DE3) pLysS. J. Mol. Catal., B Enzym., 2016, 132, 16-23.
[89]
Chohan, S.M.; Rashid, N. TK1656, a thermostable L-asparaginase from Thermococcus kodakaraensis, exhibiting highest ever reported enzyme activity. J. Biosci. Bioeng., 2013, 116(4), 438-443.
[90]
Zuo, S.; Xue, D.; Zhang, T.; Jiang, B.; Mu, W. Biochemical characterization of an extremely thermostable l-asparaginase from Thermococcus gammatolerans EJ3. J. Mol. Catal., B Enzym., 2014, 109, 122-129.
[91]
Vidya, J.; Vasudevan, U.M.; Soccol, C.R.; Pandey, A. Cloning, functional expression and characterization of L-asparaginase II from E. coli MTCC 739. Food Technol. Biotechnol., 2011, 49(3), 286-290.
[92]
Meena, B.; Anburajan, L.; Dheenan, P.S.; Begum, M.; Vinithkumar, N.V.; Dharani, G.; Kirubagaran, R. Novel glutaminase free l-asparaginase from Nocardiopsis alba NIOT-VKMA08: production, optimization, functional and molecular characterization. Bioprocess Biosyst. Eng., 2015, 38(2), 373-388.
[93]
Eisele, N.; Linke, D.; Bitzer, K.; Na’amnieh, S.; Nimtz, M.; Berger, R.G. The first characterized asparaginase from a basidiomycete, Flammulina velutipes. Bioresour. Technol., 2011, 102(3), 3316-3321.
[94]
Jia, M.; Xu, M.; He, B.; Rao, Z. Cloning, expression, and characterization of L-asparaginase from a newly isolated Bacillus subtilis B11–06. J. Agric. Food Chem., 2013, 61(39), 9428-9434.
[95]
Pokrovskaya, M.; Aleksandrova, S.; Pokrovsky, V.; Omeljanjuk, N.; Borisova, A.; Anisimova, N.Y.; Sokolov, N. Cloning, expression and characterization of the recombinant Yersinia pseudotuberculosis L-asparaginase. Protein Expr. Purif., 2012, 82(1), 150-154.
[96]
Pokrovskaya, M.; Pokrovskiy, V.; Aleksandrova, S.; Anisimova, N.Y.; Andrianov, R.; Treschalina, E.; Ponomarev, G.; Sokolov, N. Recombinant intracellular Rhodospirillum rubrum L-asparaginase with low L-glutaminase activity and antiproliferative effect. Biomed. Khim., 2012, 6(2), 123-131.
[97]
Einsfeldt, K.; Baptista, I.C.; Pereira, J.C.; Costa-Amaral, I.C.; da Costa, E.S.; Ribeiro, M.C.; Land, M.G.; Alves, T.L.; Larentis, A.L.; Almeida, R.V. Recombinant L-asparaginase from Zymomonas mobilis: a potential new antileukemic agent produced in Escherichia coli. PLoS One, 2016, 11(6), e0156692.
[98]
Bansal, S.; Gnaneswari, D.; Mishra, P.; Kundu, B. Structural stability and functional analysis of L-asparaginase from Pyrococcus furiosus. Biochemistry (Mosc.), 2010, 75(3), 375-381.
[99]
Pandey, A. Solid-state fermentation. Biochem. Eng. J., 2003, 13(2-3), 81-84.
[100]
Hölker, U.; Höfer, M.; Lenz, J. Biotechnological advantages of laboratory-scale solid-state fermentation with fungi. Appl. Microbiol. Biotechnol., 2004, 64(2), 175-186.
[101]
Acuña-Argüelles, M.; Gutierrez-Rojas, M.; Viniegra-González, G.; Favela-Torres, E. Production and properties of three pectinolytic activities produced byAspergillus niger in submerged and solid-state fermentation. Appl. Microbiol. Biotechnol., 1995, 43(5), 808-814.
[102]
Hölker, U.; Lenz, J. Solid-state fermentation—are there any biotechnological advantages? Curr. Opin. Microbiol., 2005, 8(3), 301-306.
[103]
Doriya, K.; Jose, N.; Gowda, M.; Kumar, D. Solid-state fermentation vs submerged fermentation for the production of L-asparaginase. Adv. Food Nutr. Res., 2016, 78, 115-135.
[104]
El-Bessoumy, A.A.; Sarhan, M.; Mansour, J. Production, isolation, and purification of L-asparaginase from Pseudomonas aeruginosa 50071 using solid-state fermentation. BMB Rep., 2004, 37(4), 387-393.
[105]
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.
[106]
Hosamani, R.; Kaliwal, B. L-asparaginase an anti-tumor agent production by Fusarium equiseti using solid state fermentation. Int. J. Drug Discov., 2011, 3(2), 88-99.
[107]
Kumar, N.M.; Ramasamy, R.; Manonmani, H. Production and optimization of l-asparaginase from Cladosporium sp. using agricultural residues in solid state fermentation. Ind. Crops Prod., 2013, 43, 150-158.
[108]
Ghosh, S.; Murthy, S.; Govindasamy, S. Chandrasekaran, M. Optimization of L-asparaginase production by Serratia marcescens (NCIM 2919) under solid state fermentation using coconut oil cake. Sustain. Chem. Proc., 2013, 1(1), 9.
[109]
Meghavarnam, A.K.; Janakiraman, S. Solid state fermentation: An effective fermentation strategy for the production of L-asparaginase by Fusarium culmorum (ASP-87). Biocatal. Agric. Biotechnol., 2017, 11, 124-130.
[110]
Asselin, B.L.; Whitin, J.C.; Coppola, D.J.; Rupp, I.P.; Sallan, S.E.; Cohen, H.J. Comparative pharmacokinetic studies of three asparaginase preparations. J. Clin. Oncol., 1993, 11(9), 1780-1786.
[111]
Avramis, V.I.; Panosyan, E.H. Pharmacokinetic/pharmacodynamic relationships of asparaginase formulations. Clin. Pharmacokinet., 2005, 44(4), 367-393.
[112]
Panetta, J.; Gajjar, A.; Hijiya, N.; Hak, L.; Cheng, C.; Liu, W.; Pui, C.; Relling, M. Comparison of native E. coli and PEG asparaginase pharmacokinetics and pharmacodynamics in pediatric acute lymphoblastic leukemia. Clin. Pharmacol. Ther., 2009, 86(6), 651-658.
[113]
Holcenberg, J.S.; Teller, D.C. Physical properties of antitumor glutaminase-asparaginase from Pseudomonas 7A. J. Biol. Chem., 1976, 251(17), 5375-5380.
[114]
Panosyan, E.; Avramis, I.; Seibel, N.; Grigoryan, R.; Gaynon, P.; Sather, H.; Siegel, S.; Avramis, V. In: Glutamine (Gln) deamination by asparaginases (ASNases) in children with higher risk acute lymphoblastic leukemia (HR ALL),(CCG-1961 study), Blood, AMER SOC HEMATOLOGY 1900 M STREET. NW SUITE 200, WASHINGTON, DC 20036 USA: , 2002. pp. 759A-760A.
[115]
Tareke, E.; Rydberg, P.; Karlsson, P.; Eriksson, S.; Törnqvist, M. Analysis of acrylamide, a carcinogen formed in heated foodstuffs. J. Agric. Food Chem., 2002, 50(17), 4998-5006.
[116]
Mottram, D.S.; Wedzicha, B.L.; Dodson, A.T. Food chemistry: Acrylamide is formed in the Maillard reaction. Nature, 2002, 419(6906), 448.
[117]
Friedman, M. Chemistry, biochemistry, and safety of acrylamide. A review. J. Agric. Food Chem., 2003, 51(16), 4504-4526.
[118]
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. Agric. Food Chem., 2009, 57(10), 4168-4176.
[119]
Zyzak, D.V.; Sanders, R.A.; Stojanovic, M.; Tallmadge, D.H.; Eberhart, B.L.; Ewald, D.K.; Gruber, D.C.; Morsch, T.R.; Strothers, M.A.; Rizzi, G.P. Acrylamide formation mechanism in heated foods. J. Agric. Food Chem., 2003, 51(16), 4782-4787.
[120]
Organization, W.H. Compendium of food additive specifications. FAO JECFA Monographs; Joint FAO/WHO Expert Committee on Food Additives, 2006, p. 3.
[121]
Kumar, N.M.; Shimray, C.A.; Indrani, D.; Manonmani, H. Reduction of acrylamide formation in sweet bread with L-asparaginase treatment. Food Bioprocess Technol., 2014, 7(3), 741-748.
[122]
Zhang, S.; Xie, Y.; Zhang, C.; Bie, X.; Zhao, H.; Lu, F.; Lu, Z. Biochemical characterization of a novel l-asparaginase from Bacillus megaterium H-1 and its application in French fries. Food Res. Int., 2015, 77, 527-533.
[123]
Nie, S.; Xing, Y.; Kim, G.J.; Simons, J.W. Nanotechnology applications in cancer. Annu. Rev. Biomed. Eng., 2007, 9, 257-288.
[124]
Nishiyama, N. Nanomedicine: Nanocarriers shape up for long life. Nat. Nanotechnol., 2007, 2(4), 203.
[125]
Ferrari, M. Cancer nanotechnology: Opportunities and challenges. Nat. Rev. Cancer, 2005, 5(3), 161.
[126]
Cuenca, A.G.; Jiang, H.; Hochwald, S.N.; Delano, M.; Cance, W.G.; Grobmyer, S.R. Emerging implications of nanotechnology on cancer diagnostics and therapeutics. Cancer, 2006, 107(3), 459-466.
[127]
Wang, X.; Yang, L.; Chen, Z.G.; Shin, D.M. Application of nanotechnology in cancer therapy and imaging. CA Cancer J. Clin., 2008, 58(2), 97-110.
[128]
Ulu, A.; Ates, B. Immobilization of l-asparaginase on carrier materials: A comprehensive review. Bioconjug. Chem., 2017, 28(6), 1598-1610.
[129]
Graham, M.L. Pegaspargase: A review of clinical studies. Adv. Drug Deliv. Rev., 2003, 55(10), 1293-1302.
[130]
Parveen, S.; Sahoo, S.K. Nanomedicine. Clin. Pharmacokinet., 2006, 45(10), 965-988.
[131]
Duncan, R. Polymer conjugates as anticancer nanomedicines. Nat. Rev. Cancer, 2006, 6(9), 688.
[132]
Gaspar, M.M.; Blanco, D.; Cruz, M.E.; Alonso, M.J. Formulation of L-asparaginase-loaded poly (lactide-co-glycolide) nanoparticles: influence of polymer properties on enzyme loading, activity and in vitro release. J. Control. Release, 1998, 52(1-2), 53-62.
[133]
Tabandeh, M.R.; Aminlari, M. Synthesis, physicochemical and immunological properties of oxidized inulin–l-asparaginase bioconjugate. J. Biotechnol., 2009, 141(3-4), 189-195.
[134]
Kwon, Y.M.; Chung, H.S.; Moon, C.; Yockman, J.; Park, Y.J.; Gitlin, S.D.; David, A.E.; Yang, V.C. L-Asparaginase encapsulated intact erythrocytes for treatment of acute lymphoblastic leukemia (ALL). J. Control. Release, 2009, 139(3), 182-189.
[135]
Zhang, Y-Q.; Wang, Y-J.; Wang, H-Y.; Zhu, L.; Zhou, Z-Z. Highly efficient processing of silk fibroin nanoparticle-l-asparaginase bioconjugates and their characterization as a drug delivery system. Soft Matter, 2011, 7(20), 9728-9736.
[136]
Ghosh, S.; Chaganti, S.R.; Prakasham, R. Polyaniline nanofiber as a novel immobilization matrix for the anti-leukemia enzyme l-asparaginase. J. Mol. Catal., B Enzym., 2012, 74(1-2), 132-137.
[137]
Bahreini, E.; Aghaiypour, K.; Abbasalipourkabir, R.; Mokarram, A.R.; Goodarzi, M.T.; Saidijam, M. Preparation and nanoencapsulation of l-asparaginase II in chitosan-tripolyphosphate nanoparticles and in vitro release study. Nanoscale Res. Lett., 2014, 9(1), 340.
[138]
Ulu, A.; Koytepe, S.; Ates, B. Design of starch functionalized biodegradable P (MAA-co-MMA) as carrier matrix for l-asparaginase immobilization. Carbohydr. Polym., 2016, 153, 559-572.