Applied Microbiology and Biotechnology

, Volume 99, Issue 3, pp 1069–1079 | Cite as

Recent research progress on microbial l-asparaginases

  • Shaohua Zuo
  • Tao Zhang
  • Bo Jiang
  • Wanmeng Mu


l-Asparaginases (EC are enzymes that catalyze the hydrolysis of l-asparagine to l-aspartic acid and found in a variety of organisms from microorganisms to mammals. However, they are mainly expressed and produced by microorganisms. Microbial l-asparaginases have received sustained attention due to their irreplaceable role in the therapy of acute lymphoblastic leukemia and for their inhibition of acrylamide formation during food processing. In this article, we review the application of microbial l-asparaginases in medical treatments and acrylamide mitigation. In addition, we describe in detail recent advances in the existing sources, purification, production, properties, molecular modification, and immobilization of l-asparaginase.


l-Asparaginase Acute lymphoblastic leukemia Acrylamide Production Modification Immobilization 



This work was supported by the 973 Project (No. 2012CB720802), the 863 Project (No. 2011AA100904), and the Support Project of Jiangsu Province (No. BK20130001) and Shaoxing City (No. 2013A23002).


  1. Agarwal A, Kumar S, Veeranki VD (2011) Effect of chemical and physical parameters on the production of l-asparaginase from a newly isolated Serratia marcescens SK-07. Lett Appl Microbiol 52:307–313PubMedCrossRefGoogle Scholar
  2. Agrawal V, Hee Woo J, Borthakur G, Kantarjian H, Frankel AE (2013) Red blood cell-encapsulated l-asparaginase: potential therapy of patients with asparagine synthetase deficient acute myeloid leukemia. Protein Peptide Lett 20:392–402CrossRefGoogle Scholar
  3. Allas S, Sahakian P, Fichtner I, Abribat T (2009) Pharmacokinetics and pharmacodynamics in mice of a pegylated recombinant Erwinia chrysanthemi-derived l-asparaginase. Blood 114:2033Google Scholar
  4. Amena S, Vishalakshi N, Prabhakar M, Dayanand A, Lingappa K (2010) Production, purification and characterization of l-asparaginase from Streptomyces gulbargensis. Braz J Microbiol 41:173–178PubMedCentralPubMedCrossRefGoogle Scholar
  5. Anese M, Quarta B, Frias J (2011a) Modelling the effect of asparaginase in reducing acrylamide formation in biscuits. Food Chem 126:435–440CrossRefGoogle Scholar
  6. Anese M, Quarta B, Peloux L, Calligaris S (2011b) Effect of formulation on the capacity of l-asparaginase to minimize acrylamide formation in short dough biscuits. Food Res Int 44:2837–2842CrossRefGoogle Scholar
  7. Asselin BL, Ryan D, Frantz CN, Bernal SD, Leavitt P, Sallan SE, Cohen HJ (1989) In vitro and in vivo killing of acute lymphoblastic leukemia cells by l-asparaginase. Cancer Res 49:4363–4368PubMedGoogle Scholar
  8. Babu UK, Ramagopal N, Reddy DSR (2010) Optimization of l-asparaginase production from isolated Aspergillus niger by using solid state fermentation on sesame cake via application of genetic algorithm, and artificial neural network-based design model. J Biotechnol 150:S538–S539CrossRefGoogle Scholar
  9. Bansal S, Gnaneswari D, Mishra P, Kundu B (2010) Structural stability and functional analysis of l-asparaginase from Pyrococcus furiosus. Biochemistry-Moscow 75:375–381PubMedCrossRefGoogle Scholar
  10. Bansal S, Srivastava A, Mukherjee G, Pandey R, Verma AK, Mishra P, Kundu B (2012) Hyperthermophilic asparaginase mutants with enhanced substrate affinity and antineoplastic activity: structural insights on their mechanism of action. FASEB J 26:1161–1171PubMedCrossRefGoogle Scholar
  11. Basha NS, Rekha R, Komala M, Ruby S (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 8:353–360CrossRefGoogle Scholar
  12. Baskar G, Renganathan S (2012) 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 7:212–220CrossRefGoogle Scholar
  13. Borek D, Jaskólski M (2001) Sequence analysis of enzymes with asparaginase activity. Acta Biochim Pol 48:893–902PubMedGoogle Scholar
  14. Bruneau L, Chapman R, Marsolais F (2006) Co-occurrence of both l-asparaginase subtypes in Arabidopsis: At3g16150 encodes a K+-dependent l-asparaginase. Planta 224:668–679PubMedCrossRefGoogle Scholar
  15. Cappelletti D, Chiarelli LR, Pasquetto MV, Stivala S, Valentini G, Scotti C (2008) Helicobacter pylori l-asparaginase: a promising chemotherapeutic agent. Biochem Biophys Res Commun 377:1222–1226PubMedCrossRefGoogle Scholar
  16. Cedar H, Schwartz JH (1967) Localization of the two l-asparaginases in anaerobically grown Escherichia coli. J Biol Chem 242:3753–3755PubMedGoogle Scholar
  17. Cedar H, Schwartz JH (1968) Production of l-asparaginase II by Escherichia coli. J Bacteriol 96:2043–2048PubMedCentralPubMedGoogle Scholar
  18. Chohan SM, Rashid N (2013) TK1656, a thermostable l-asparaginase from Thermococcus kodakaraensis, exhibiting highest ever reported enzyme activity. J Biosci Bioeng 116:438–443PubMedCrossRefGoogle Scholar
  19. Ciesarová Z, Kiss E, Boegl P (2006) Impact of l-asparaginase on acrylamide content in potato products. J Food Nutr Res 45:141–146Google Scholar
  20. Dharmaraj S (2011) Study of l-asparaginase production by Streptomyces noursei MTCC 10469, isolated from marine sponge Callyspongia diffusa. Iranian J Biotechnol 9:102–108Google Scholar
  21. Duval M, Suciu S, Ferster A, Rialland X, Nelken B, Lutz P, Benoit Y, Robert A, Manel A-M, Vilmer E (2002) 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 99:2734–2739PubMedCrossRefGoogle Scholar
  22. Ebrahiminezhad A, Rasoul-Amini S, Ghasemi Y (2011) l-Asparaginase production by moderate halophilic bacteria isolated from maharloo salt lake. Indian J Microbiol 1:307–311CrossRefGoogle Scholar
  23. Ebrahiminezhad A, Rasoul-Amini S, Ghoshoon MB, Ghasemi Y (2014) Chlorella vulgaris, a novel microalgal source for l-asparaginase production. Biocatal Agr Biotechnol 3:214–217Google Scholar
  24. Eisele N, Linke D, Bitzer K, Na’amnieh S, Nimtz M, Berger RG (2011) The first characterized asparaginase from a basidiomycete, Flammulina velutipes. Bioresour Technol 102:3316–3321PubMedCrossRefGoogle Scholar
  25. Ferrara MA, Severino NMB, Mansure JJ, Martins AS, Oliveira EMM, Siani AC, Pereira N Jr, Torres FAG, Bon EPS (2006) Asparaginase production by a recombinant Pichia pastoris strain harbouring Saccharomyces cerevisiae ASP3 gene. Enz Microb Tech 39:1457–1463CrossRefGoogle Scholar
  26. Ferrara MA, Bonomo Severino NM, Valente RH, Perales J, Bon EPS (2010) High-yield extraction of periplasmic asparaginase produced by recombinant Pichia pastoris harbouring the Saccharomyces cerevisiae ASP3 gene. Enz Microb Tech 47:71–76CrossRefGoogle Scholar
  27. Ghosh S, Chaganti SR, Prakasham R (2012) Polyaniline nanofiber as a novel immobilization matrix for the anti-leukemia enzyme l-asparaginase. J Mol Catal B-Enzym 74:132–137CrossRefGoogle Scholar
  28. Ghosh S, Murthy S, Govindasamy S, Chandrasekaran M (2013) Optimization of l-asparaginase production by Serratia marcescens (NCIM 2919) under solid state fermentation using coconut oil cake. Sustain Chem Process 1:1–8CrossRefGoogle Scholar
  29. Gladilina IA, Sokolov NN, Krasotkina IV (2008) Cloning, expression and purification of Helicobater pylori l-asparaginase. Biomed Khim 54:482–486PubMedGoogle Scholar
  30. Hatanaka T, Usuki H, Arima J, Uesugi Y, Yamamoto Y, Kumagai Y, Yamasato A, Mukaihara T (2011) Extracellular production and characterization of two Streptomyces l-asparaginases. Appl Biochem Biotechnol 163:836–844PubMedCrossRefGoogle Scholar
  31. Hedegaard RV, Frandsen H, Skibsted LH (2008) Kinetics of formation of acrylamide and Schiff base intermediates from asparagine and glucose. Food Chem 108:917–925CrossRefGoogle Scholar
  32. Hendriksen HV, Kornbrust BA, Østergaard PR, Stringer MA (2009) Evaluating the potential for enzymatic acrylamide mitigation in a range of food products using an asparaginase from Aspergillus oryzae. J Agric Food Chem 57:4168–4176PubMedCrossRefGoogle Scholar
  33. Hosamani R, Kaliwal B (2011) Isolation, molecular identification and optimization of fermentation parameters for the production of l-asparaginase, an anticancer agent by Fusarium equiseti. Int J Microbiol Res 3:108–119CrossRefGoogle Scholar
  34. Huang L, Liu Y, Sun Y, Yan Q, Jiang Z (2014) 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 Microb 80:1561–1569CrossRefGoogle Scholar
  35. Hüser A, Klöppner U, Röhm KH (1999) Cloning, sequence analysis, and expression of ansB from Pseudomonas fluorescens, encoding periplasmic glutaminase/asparaginase. FEMS Microbiol Lett 178:327–335PubMedCrossRefGoogle Scholar
  36. Hymavathi M, Sathish T, Rao CS, Prakasham RS (2009) Enhancement of l-asparaginase production by isolated Bacillus circulans (MTCC 8574) using response surface methodology. Appl Biochem Biotechnol 159:191–198PubMedCrossRefGoogle Scholar
  37. International Agency for Research on Cancer (IARC) (1994) Monographs on the evaluation of carcinogenic risks to humans, some industrial chemicals. Acrylamide. 88:389–433.
  38. Jerlström PG, Bezjak DA, Jennings MP, Beacham IR (1989) Structure and expression in Escherichia coli K-12 of the l-asparaginase I-encoding ansA gene and its flanking regions. Gene 78:37–46PubMedCrossRefGoogle Scholar
  39. Jia M, Xu M, He B, Rao Z (2013) Cloning, expression and characterization of l-asparaginase from a newly isolated Bacillus subtilis B11-06. J Agric Food Chem 61:9428–9434PubMedCrossRefGoogle Scholar
  40. Kavitha A, Vijayalakshmi M (2012) A study on l-asparaginase of Nocardia levis MK-VL_113. Sci World J 2012:160434CrossRefGoogle Scholar
  41. Kenari SLD, Alemzadeh I, Maghsodi V (2011) Production of l-asparaginase from Escherichia coli ATCC 11303: optimization by response surface methodology. Food Bioprod Process 89:315–321CrossRefGoogle Scholar
  42. Kornbrust BA, Stringer MA, Lange NEK, Hendriksen HV, Whitehurst R, Oort Mv (2009) Asparaginase—an enzyme for acrylamide reduction in food products. In: Enzymes in Food Technology, 2nd edn. Wiley-Blackwell, UK, pp 59–87Google Scholar
  43. Kotzia GA, Labrou NE (2007) l-Asparaginase from Erwinia chrysanthemi 3937: cloning, expression and characterization. J Biotechnol 127:657–669PubMedCrossRefGoogle Scholar
  44. Kotzia GA, Labrou NE (2011) Engineering substrate specificity of E. carotovora l-asparaginase for the development of biosensor. J Mol Catal B-Enzym 72:95–101CrossRefGoogle Scholar
  45. Kotzia GA, Lappa K, Labrou NE (2007) Tailoring structure-function properties of l-asparaginase: engineering resistance to trypsin cleavage. Biochem J 404:337–343PubMedCentralPubMedCrossRefGoogle Scholar
  46. Kumar NSM, Manonmani HK (2013) Purification, characterization and kinetic properties of extracellular l-asparaginase produced by Cladosporium sp. World J Microbiol Biotechnol 29:577–587CrossRefGoogle Scholar
  47. Kumar S, Pakshirajan K, Dasu VV (2009) Development of medium for enhanced production of glutaminase-free l-asparaginase from Pectobacterium carotovorum MTCC 1428. Appl Biochem Biotechnol 84:477–486Google Scholar
  48. Kumar S, Dasu VV, Pakshirajan K (2010) Localization and production of novel l-asparaginase from Pectobacterium carotovorum MTCC 1428. Process Biochem 45:223–229CrossRefGoogle Scholar
  49. Kumar S, Dasu VV, Pakshirajan K (2011a) Purification and characterization of glutaminase-free l-asparaginase from Pectobacterium carotovorum MTCC 1428. Bioresour Technol 102:2077–2082PubMedCrossRefGoogle Scholar
  50. Kumar S, Veeranki VD, Pakshirajan K (2011b) Assessment of physical process conditions for enhanced production of novel glutaminase-free l-asparaginase from Pectobacterium carotovorum MTCC 1428. Appl Biochem Biotechnol 163:327–337PubMedCrossRefGoogle Scholar
  51. Kumar NSM, Ramasamy R, Manonmani HK (2013) Production and optimization of l-asparaginase from Cladosporium sp. using agricultural residues in solid state fermentation. Ind Crop Prod 43:150–158CrossRefGoogle Scholar
  52. Kumar NM, Shimray CA, Indrani D, Manonmani H (2014a) Reduction of acrylamide formation in sweet bread with l-asparaginase treatment. Food Bioprocess Technol 7:741–748CrossRefGoogle Scholar
  53. Kumar NSM, Kishore V, Manonmani HK (2014b) Chemical modification of l-asparaginase from Cladosporium sp. for improved activity and thermal stability. Prep Biochem Biotechnol 44:433–450CrossRefGoogle Scholar
  54. Kumari PK, Sankar GG, Prabhakar T, Lakshmi SS (2013) Purification and characterization of l-asparaginase from Streptomyces griseoluteus WS3/1. Int J Pharm Sci Rev Res 23:198–202Google Scholar
  55. Li LZ, Xie TH, Li HJ, Qing C, Zhang GM, Sun MS (2007) Enhancing the thermostability of Escherichia coli l-asparaginase II by substitution with pro in predicted hydrogen-bonded turn structures. Enz Microb Tech 41:523–527CrossRefGoogle Scholar
  56. Martin JF (1989) Molecular genetics of amino acid-producing Corynebacteria. Symp Soc Gen Microbiol 44:25–59Google Scholar
  57. Mashburn LT, Wriston JC Jr (1964) Tumor inhibitory effect of l-asparaginase from Escherichia coli. Arch Biochem Biophys 105:450–453PubMedCrossRefGoogle Scholar
  58. Moreno-Enriquez A, Evangelista-Martinez Z, Gonzalez-Mondragon EG, Calderon-Flores A, Arreguin R, Perez-Ruedas E, Huerta-Saquero A (2012) Biochemical characterization of recombinant l-asparaginase (AnsA) from Rhizobium etli, a member of an increasing Rhizobial-type family of l-asparaginases. J Microbiol Biotechnol 22:292–300PubMedCrossRefGoogle Scholar
  59. Narayana KJP, Kumar KG, Vijayalakshmi M (2008) l-Asparaginase production by Streptomyces albidoflavus. Indian J Microbiol 48:331–336PubMedCentralPubMedCrossRefGoogle Scholar
  60. Narta U, Roy S, Kanwar SS, Azmi W (2011) Improved production of l-asparaginase by Bacillus brevis cultivated in the presence of oxygen-vectors. Bioresour Technol 102:2083–2085PubMedCrossRefGoogle Scholar
  61. Onishi Y, Yano S, Thongsanit J, Takagi K, Yoshimune K, Wakayama M (2011) Expression in Escherichia coli of a gene encoding type II l-asparaginase from Bacillus subtilis, and characterization of its unique properties. Ann Microbiol 61:517–524CrossRefGoogle Scholar
  62. Patil S, Coutsouvelis J, Spencer A (2011) Asparaginase in the management of adult acute lymphoblastic leukaemia: is it used appropriately? Cancer Treat Rev 37:202–207PubMedCrossRefGoogle Scholar
  63. Pedreschi F, Kaack K, Granby K (2008) The effect of asparaginase on acrylamide formation in French fries. Food Chem 109:386–392CrossRefGoogle Scholar
  64. Pedreschi F, Mariotti S, Granby K, Risum J (2011) Acrylamide reduction in potato chips by using commercial asparaginase in combination with conventional blanching. LWT-Food Sci Technol 44:1473–1476CrossRefGoogle Scholar
  65. Pieters R, Hunger SP, Boos J, Rizzari C, Silverman L, Baruchel A, Goekbuget N, Schrappe M, Pui CH (2011) l-Asparaginase treatment in acute lymphoblastic leukemia. Cancer 117:238–249PubMedCentralPubMedCrossRefGoogle Scholar
  66. Pokrovskaya M, Pokrovskiy V, Aleksandrova S, Anisimova NY, Andrianov R, Treschalina E, Ponomarev G, Sokolov N (2012a) Recombinant intracellular Rhodospirillum rubrum l-asparaginase with low l-glutaminase activity and antiproliferative effect. Biochemistry-Moscow 6:123–131Google Scholar
  67. Pokrovskaya MV, Aleksandrova SS, Pokrovsky VS, Omeljanjuk NM, Borisova AA, Anisimova NY, Sokolov NN (2012b) Cloning, expression and characterization of the recombinant Yersinia pseudotuberculosis l-asparaginase. Protein Expres Purif 82:150–154CrossRefGoogle Scholar
  68. Prakasham RS, Rao CS, Rao RS, Lakshmi GS, Sarma PN (2007) l-Asparaginase production by isolated Staphylococcus sp-6A: design of experiment considering interaction effect for process parameter optimization. J Appl Microbiol 102:1382–1391PubMedCrossRefGoogle Scholar
  69. Roth G, Nunes J, Rosado L, Bizarro C, Volpato G, Nunes C, Renard G, Basso L, Santos D, Chies J (2013) Recombinant Erwinia carotovora l-asparaginase II production in Escherichia coli fed-batch cultures. Braz J Chem Eng 30:245–256CrossRefGoogle Scholar
  70. Sahu MK, Sivakumar K, Poorani E, Thangaradjou T, Kannan L (2007) Studies on l-asparaginase enzyme of actinomycetes isolated from estuarine fishes. J Environ Biol 28:465–474PubMedGoogle Scholar
  71. Sanjeeviroyar A, Rajendran A, Muthuraj M, Basha KM, Thangavelu V (2010) Sequential optimization and kinetic modeling of l-asparaginase production by Pectobacterium carotovorum in submerged fermentation. Asia-Pac J Chem Eng 5:743–755Google Scholar
  72. Savitri AN, Azmi W (2003) Microbial l-asparaginase: a potent antitumour enzyme. Indian J Biotechnol 2:184–194Google Scholar
  73. Shibayama K, Takeuchi H, J-i W, Mori S, Arakawa Y (2011) Biochemical and pathophysiological characterization of Helicobacter pylori asparaginase. Microbiol Immunol 55:408–417PubMedCrossRefGoogle Scholar
  74. Shrivastava A, Khan AA, Shrivastav A, Jain SK, Singhal PK (2012) Kinetis studies of l-asparaginase from Penicillium digitatum. Prep Biochem Biotechnol 42:574–581PubMedCrossRefGoogle Scholar
  75. Singh Y, Srivastava S (2012) Statistical and evolutionary optimization for enhanced production of an anti-leukemic enzyme, l-asparaginase, in a protease-deficient Bacillus aryabhattai ITBHU02 isolated from the soil contaminated with hospital waste. Indian J Exp Biol 51:322–335Google Scholar
  76. Singh Y, Srivastava S (2014) Performance improvement of Bacillus aryabhattai ITBHU02 for high-throughput production of a tumor-inhibitory l-asparaginase using a kinetic model based approach. J Chem Technol Biotechnol 89:117–127CrossRefGoogle Scholar
  77. Singh Y, Gundampati RK, Jagannadham MV, Srivastava S (2013) Extracellular l-asparaginase from a protease-deficient Bacillus aryabhattai ITBHU02: purification, biochemical characterization, and evaluation of antineoplastic activity in vitro. Appl Biochem Biotechnol 171:1759–1774PubMedCrossRefGoogle Scholar
  78. Stecher A, Morgantetti de Deus P, Polikarpov I, Abrahao-Neto J (1999) Stability of l-asparaginase: an enzyme used in leukemia treatment. Pharm Acta Helv 74:1–9PubMedCrossRefGoogle Scholar
  79. Sudhir AP, Dave BR, Trivedi KA, Subramanian RB (2012) Production and amplification of an l-asparaginase gene from actinomycete isolate Streptomyces ABR2. Ann Microbiol 62:1609–1614CrossRefGoogle Scholar
  80. Tareke E, Rydberg P, Karlsson P, Eriksson S, Törnqvist M (2002) Analysis of acrylamide, a carcinogen formed in heated foodstuffs. J Agric Food Chem 50:4998–5006PubMedCrossRefGoogle Scholar
  81. Thenmozhi C, Sankar R, Karuppiah V, Sampathkumar P (2011) l-Asparaginase production by mangrove derived Bacillus cereus MAB5: optimization by response surface methodology. Asian Pac J Trop Med 4:486–491PubMedCrossRefGoogle Scholar
  82. Verma N, Kumar K, Kaur G, Anand S (2007a) E. coli K-12 asparaginase-based asparagine biosensor for leukemia. Artif Cell Blood Sub 35:449–456CrossRefGoogle Scholar
  83. Verma N, Kumar K, Kaur G, Anand S (2007b) l-Asparaginase: a promising chemotherapeutic agent. Crit Rev Biotechnol 27:45–62PubMedCrossRefGoogle Scholar
  84. Vidya J, Pandey A (2012) Recombinant expression and characterization of l-asparaginase II from a moderately thermotolerant bacterial isolate. Appl Biochem Biotechnol 167:973–980PubMedCrossRefGoogle Scholar
  85. Vidya J, Vasudevan UM, Soccol CR, Pandey A (2011) Cloning, functional expression and characterization of l-asparaginase II from E. coli MTCC 739. Food Technol Biotechnol 49:286–290Google Scholar
  86. Vidya J, Ushasree MV, Pandey A (2014) Effect of surface charge alteration on stability of l-asparaginase II from Escherichia sp. Enz Microb Tech 56:15–19CrossRefGoogle Scholar
  87. Wink PL, Bogdawa HM, Renard G, Chies JM, Basso LA, Santos DS (2010) Comparison between two Erwinia carotovora l-asparaginase II constructions: cloning, heterologous expression, purification, and kinetic characterization. J Microbial Biochem Technol 2:13–19CrossRefGoogle Scholar
  88. Yano S, Minato R, Thongsanit J, Tachiki T, Wakayama M (2008) Overexpression of type I l-asparaginase of Bacillus subtilis in Escherichia coli, rapid purification and characterisation of recombinant type I l-asparaginase. Ann Microbiol 58:711–716CrossRefGoogle Scholar
  89. Zhang YQ, Xiang RL, Yan HB, Chen XX (2008) Preparation of silk fibroin nanoparticles and their application to immobilization of l-asparaginase. Chem J Chin Univ 29:628–633Google Scholar
  90. Zhang YQ, Wang YJ, Wang HY, Zhu L, Zhou ZZ (2011) Highly efficient processing of silk fibroin nanoparticle-l-asparaginase bioconjugates and their characterization as a drug delivery system. Soft Matter 7:9728–9736CrossRefGoogle Scholar
  91. Zhu JH, Liu J (2008) Improving the extraction of intracellular l-asparaginase by high-pressure homogenization. Asia-Pac J Chem Eng 3:211–216CrossRefGoogle Scholar
  92. Zhu JH, Yan XL, Chen HJ, Wang ZH (2007) In situ extraction of intracellular l-asparaginase using thermoseparating aqueous two-phase systems. J Chromatogra A 1147:127–134CrossRefGoogle Scholar
  93. Zuo S, Xue D, Zhang T, Jiang B, Mu W (2014) Biochemical characterization of an extremely thermostable l-asparaginase from Thermococcus gammatolerans EJ3. J Mol Catal B Enzym 109:122–129CrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  • Shaohua Zuo
    • 1
  • Tao Zhang
    • 1
  • Bo Jiang
    • 1
    • 2
  • Wanmeng Mu
    • 1
    • 2
  1. 1.State Key Laboratory of Food Science and Technology, Ministry of Education Key Laboratory of Carbohydrate Chemistry and BiotechnologyJiangnan UniversityWuxiChina
  2. 2.Synergetic Innovation Center of Food Safety and NutritionJiangnan UniversityWuxiChina

Personalised recommendations