Purification and characterization of glutaminase-free l-asparaginase from Pectobacterium carotovorum MTCC 1428

Bioresource Technology

Volumn 102, Issue 2, 2011, Pages 2077-2082

  Kumar, Sanjay ^a   Venkata Dasu, V ^a   Pakshirajan, K ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY GUWAHATI   (India)

Author keywords

Anti leukemic enzyme; L Asparaginase; N terminal sequence; Pectobacterium carotovorum; Purification

Indexed keywords

2-MERCAPTOETHANOL; ANTI-CANCER THERAPIES; ANTI-LEUKEMIC ENZYME; DIVALENT CATION; GLUTAMINASE; GLUTATHIONES; HOMOTETRAMERS; ISO-ELECTRIC POINTS; L-ASPARAGINASE; L-CYSTINE; L-HISTIDINE; MALDI TOF MS; MONOCATIONS; N-TERMINALS; NATURAL SUBSTRATES; OPTIMUM PH; OPTIMUM TEMPERATURE; PECTOBACTERIUM CAROTOVORUM; SIDE EFFECT; THIOL GROUPS;

AMINO ACIDS; ENZYMES; POSITIVE IONS;

PURIFICATION;

ASPARAGINASE; CYSTINE; GLUTAMINASE; GLUTATHIONE; HISTIDINE; MERCAPTOETHANOL;

BACTERIUM; CATION; ENZYME ACTIVITY; PH; SUBSTRATE; TEMPERATURE GRADIENT; THIOL;

ARTICLE; BACTERIAL STRAIN; ENZYME ACTIVITY; ENZYME PURIFICATION; HYDROLYSIS; KINETICS; MOLECULAR WEIGHT; NONHUMAN; PECTOBACTERIUM CAROTOVORUM; PH; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ASPARAGINASE; ENZYME STABILITY; GLUTAMINASE; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PECTOBACTERIUM CAROTOVORUM; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, PROTEIN; SUBSTRATE SPECIFICITY; TEMPERATURE;

PECTOBACTERIUM CAROTOVORUM;

EID: 78650705940     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2010.07.114     Document Type: Article

References (23)

1. Abakumova O.Yu., Podobed O.V., Borisova A.A., Sidoruk K.V., Alexandrova S.S., Omelyanuk N.M., Pokrovskaya M.V., Kondakova L.I., Sokolov N.N. Antitumor activity of l-asparaginase from Yersinia pseudotuberculosis. Biochem. (Mosc.) Suppl. B: Biomed. Chem. 2009, 3:198-201.
2. Aghaiypour K., Wlodawer A., Lubkowski J. Do bacterial l-asparaginases utilize a catalytic triad Thr-Tyr-Glu?. Biochim. Biophy. Acta. 2001, 1550:117-128.
3. Andrew P. Estimation of the molecular weights of proteins by Sephadex gel-filtration. Biochem. J. 1964, 91:222-233.
4. Aung H.P., Bocola M., Schleper S., Röhm K.H. Dynamics of a mobile loop at the active site of Escherichia coli asparaginase. Biochem. Biophy. Acta. 2000, 1481:349-359.
5. Deutscher M.P. Guide to protein purification. Methods Enzymol. 1990, 182:430-431.
6. Gallagher M.P., Marshall R.D., Wilson R. Asparaginase as a drug for the treatment of acute lymphoblastic leukemia. Essays Biochem. 1989, 24:1-40.
7. Gallagher S.R. One-dimensional electrophoresis using nondenaturing conditions. Curr. Protoc. Mol. Biol. 1999, 47. 10.2B.1-10.2B.11.
8. Kotzia G.A., Labrou N.E. Cloning, expression and characterization of Erwinia carotovora l-asparaginase. J. Biotechnol. 2005, 119:309-323.
9. Kotzia G.A., Labrou N.E. l-Asparaginase from Erwinia chrysanthemi 3937: cloning, expression and characterization. J. Biotechnol. 2007, 127:657-669.
10. Kozak M., Jurga J. A comparison between the crystal and solution structures of Escherichia coli asparaginase II. Acta Biochim. Pol. 2002, 49:509-513.
11. Kumar S., Pakshirajan K., Venkata Dasu V. Development of medium for enhanced production of glutaminase free l-asparaginase from Pectobacterium carotovorum MTCC 1428. Appl. Microb. Biotechnol. 2009, 84:477-486.
12. Kumar S., Pakshirajan K., Venkata Dasu V. Localization and production of novel l-asparaginase from Pectobacterium carotovorum MTCC 1428. Process Biochem. 2010, 45:223-229.
13. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
14. Leatherbarrow R.J. GraFit (Version 6.0.11) 1998, Erythacus Software Ltd., Staines, UK.
15. Manna S., Sinha A., Sadhukhan R., Chakrabarty S.L. Purification, characterization and antitumor activity of l-asparaginase isolated from Pseudomonas stutzeri MB-405. Curr. Microbiol. 1995, 30:291-298.
16. Mashburn L.T., Wriston J.C. Tumor inhibitory effect of l-asparaginase from Escherichia coli. Arch. Biochem. Biophys. 1964, 105:450-452.
17. Muller H.J., Boos J. Use of l-asparaginase in childhood ALL. Crit. Rev. Oncol./Hematol. 1998, 28:97-113.
18. Narta U.K., Kanwar S.S., Azmi W. Pharmacological and clinical evaluation of l-asparaginase in the treatment of leukemia. Crit. Rev. Oncol./Hematol. 2007, 61:208-221.
19. Pedreschi F., Kaack K., Granby K. The effect of asparaginase on acrylamide formation in French fries. Food Chem. 2008, 109:386-392.
20. Prakasham R.S., Hymavathi M., Rao C.S., Arepalli S.K., Rao J.V., Kennady P.K., Nasaruddin K., Vijayakumar J.B., Sarma P.N. Evaluation of antineoplastic activity of extracellular asparaginase produced by isolated Bacillus circulans. Appl. Biochem. Biotechnol. 2010, 160:72-80.
21. Verma N., Kumar K., Kaur G., Anand S.E. E. coli K-12 asparaginase-based asparagine biosensor for leukemia. Artif. Cell. Blood Substit. Immobil. Biotechnol. 2007, 35:449-456.
22. Warangkar S.C., Khobragade C.N. Purification, characterization, and effect of thiol compounds on activity of the Erwinia carotovora l-asparaginase. Enzyme Res. 2010 (Article ID 165878) 2010, 1-10.
23. Willis R.C., Woolfolk C.A. Asparagine utilization in Escherichia coli. J. Bacteriol. 1974, 118:231-241.