The first characterized asparaginase from a basidiomycete, Flammulina velutipes

Bioresource Technology

Volumn 102, Issue 3, 2011, Pages 3316-3321

  Eisele, Nadine ^a   Linke, Diana ^a   Bitzer, Katrin ^b   Na'amnieh, Shukry ^b   Nimtz, Manfred ^c   Berger, Ralf G ^a  

^a LEIBNIZ UNIVERSITY HANNOVER   (Germany)

^b X Zyme GmbH   (Germany)

^c HELMHOLTZ CENTRE FOR INFECTION RESEARCH   (Germany)

Author keywords

Asparaginase; Basidiomycete; Escherichia coli; Flammulina velutipes; Heterologous expression

Indexed keywords

ASPARAGINASE; BASIDIOMYCETE; CHLORIDE CONCENTRATIONS; CODING SEQUENCES; CRUDE EXTRACT; DEAMIDATION; E. COLI; EDIBLE MUSHROOM; ELECTROPHORETIC HOMOGENEITY; ELEVATED TEMPERATURE; FLAMMULINA VELUTIPES; HETEROLOGOUS EXPRESSION; HYDROLYZING ACTIVITY; L-GLUTAMINE; NUTRIENT MEDIA; PAGE ANALYSIS; PEPTIDE FRAGMENTS;

ENZYMES; ESCHERICHIA COLI; FUNGI; HYDROLYSIS; SODIUM; SODIUM CHLORIDE;

AMINO ACIDS;

ASPARAGINASE; NITROGEN; PROTEIN SUBUNIT; SODIUM CHLORIDE;

CATALYSIS; CONCENTRATION (COMPOSITION); EDIBLE SPECIES; ENZYME ACTIVITY; FECAL COLIFORM; GENE EXPRESSION; HOMOGENEITY; HOMOLOGY; HYDROLYSIS; MUSHROOM; PH; PROTEIN; RECOMBINATION; SECRETION; SODIUM CHLORIDE; TOLERANCE;

AMINO ACID SEQUENCE; ARTICLE; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME STABILITY; ENZYME SYNTHESIS; ESCHERICHIA COLI; FLAMMULINA; FOAMING; FUNGAL GENE; GENE OVEREXPRESSION; HIGH TEMPERATURE; HYDROLYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; ASPARAGINASE; CLONING, MOLECULAR; ENZYME ACTIVATION; ENZYME STABILITY; FLAMMULINA; MOLECULAR SEQUENCE DATA;

BASIDIOMYCOTA; ESCHERICHIA COLI; FLAMMULINA VELUTIPES;

EID: 78650808076     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2010.10.098     Document Type: Article

References (27)

1. Altschul S.F., Gish W., Miller W., Myers E.W., Lipman D.J. Basic local alignment search tool. Journal of Molecular Biology 1990, 215:403-410.
2. Bendtsen J.D., Nielsen H., Von Heijne G., Brunak S. Improved prediction of signal peptides: SignalP 3.0. Journal of Molecular Biology 2004, 340:783-795.
3. Borek D., Jaskólski M. Sequence analysis of enzymes with asparaginase activity. Acta Biochimica Polonica 2001, 48:893-902.
4. Curthoys N.P., Lowry O.H. The distribution of glutaminase isoenzymes in the various structures of the nephron in normal, acidotic, and alkalotic rat kidney. Journal of Biological Chemistry 1973, 248:162-168.
5. Friedman M. Chemistry, biochemistry, and safety of acrylamide. A review. Journal of Agricultural and Food Chemistry 2003, 51:4504-4526.
6. Fu C.H., Sakamoto K.M. PEG-asparaginase. Expert Opinion on Pharmacotherapy 2007, 8:1977-1984.
7. Halpern Y.S., Grossowicz N. Hydrolysis of amides by extracts from mycobacteria. Biochemical Journal 1957, 65:716-720.
8. Hecker K.H., Roux K.H. High and low annealing temperatures increase both specificity and yield in touchdown and stepdown PCR. BioTechniques 1996, 20:478-485.
9. Ho P.P.K., Frank B.H., Burck P.J. Crystalline l-asparaginase from Escherichia coli B. Science 1969, 165:510-512.
10. Jackson R.C., Handschumacher R.E. Escherichia coli l-asparaginase. Catalytic activity and subunit nature. Biochemistry 1970, 9:3585-3590.
11. Laan, V.D.J.M., Stor, M.C., Lange, D.I., Mohrmann, L., 2008. Aspergillus niger asparaginase variants and their commercial uses. WO 2008128974.
12. Lindsay R.C., Jang S. Chemical intervention strategies for substantial suppression of acrylamide formation in fried potato products. Advances in Experimental Medicine and Biology 2005, 393-404.
13. Linke, D., Berger, R.G., in press. Foaming of proteins: new prospects for enzyme purification processes. Journal of Biotechnology, doi:10.1016/j.jbiotec.2010.07.022.
14. Maloney K.W. Erwinia asparaginase: coming closer to an understanding of its use in pediatric acute lymphoblastic leukemia?. Pediatric Blood and Cancer 2010, 54:189-190.
15. Matsui, T., Friis, E.P., Yamagishi, A., 2008. Design of thermostable asparaginases and their use for reduction of acrylamide in foods. WO 2008110513.
16. Moriguchi M., Sakai K., Tateyama R., Furuta Y., Wakayama M. Isolation and characterization of salt-tolerant glutaminases from marine Micrococcus luteus K-3. Journal of Fermentation and Bioengineering 1994, 77:621-625.
17. Mottram D.S., Wedzicha B.L., Dodson A.T. Food chemistry: acrylamide is formed in the Maillard reaction. Nature 2002, 419:448-449.
18. Nandakumar R., Yoshimune K., Wakayama M., Moriguchi M. Microbial glutaminase: biochemistry, molecular approaches and applications in the food industry. Journal of Molecular Catalysis B: Enzymatic 2003, 23:87-100.
19. Racusen D. Glycoprotein detection in polyacrylamide gel with thymol and sulfuric acid. Analytical Biochemistry 1979, 99:474-476.
20. Soda K., Ohshima M., Yamamoto T. Purification and properties of isozymes of glutaminase from Pseudomonas aeruginosa. Biochemical and Biophysical Research Communications 1972, 46:1278-1284.
21. Stadler R.H., Blank I., Varga N., Robert F., Hau J., Guy P.A., Robert M.C., Riediker S. Food chemistry: acrylamide from Maillard reaction products. Nature 2002, 419:449-450.
22. Suld H.M., Herbut P.A. Guinea pig serum and liver l-asparaginases. Comparison of serum and papain-digested liver l-asparaginases. Journal of Biological Chemistry 1970, 245:2797-2801.
23. Tareke E., Rydberg P., Karlsson P., Eriksson S., Törnqvist M. Analysis of acrylamide, a carcinogen formed in heated foodstuffs. Journal of Agricultural and Food Chemistry 2002, 50:4998-5006.
24. Wakayama M., Yamagata T., Kamemura A., Bootim N., Yano S., Tachiki T., Yoshimune K., Moriguchi M. Characterization of salt-tolerant glutaminase from Stenotrophomonas maltophilia NYW-81 and its application in Japanese soy sauce fermentation. Journal of Industrial Microbiology and Biotechnology 2005, 32:383-390.
25. Weißhaar R. Acrylamide in bakery products - results from model experiments. Deutsche Lebensmittelrundschau 2004, 100:93-97+i.
26. Yano T., Ito M., Tomita K., Kumagai H. Purification and properties of glutaminase from Aspergillus oryzae. Journal of Fermentation Technology 1988, 66:137-143.
27. 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., Villagran M.D. Acrylamide formation mechanism in heated foods. Journal of Agricultural and Food Chemistry 2003, 51:4782-4787.