Study of the thermal stability of D-amino acid oxidase from Trigonopsis variabilis reveals enzyme inactivation via multiple steps

Biocatalysis and Biotransformation

Volumn 24, Issue 6, 2006, Pages 426-436

  Slavica, Anita ^a   Ačai, Pavel ^a,b   Riethorst, Waander ^c   Nidetzky, Bernd ^a  

^a GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

^b SLOVAK UNIVERSITY OF TECHNOLOGY   (Slovakia)

^c NOVARTIS PHARMA AG   (Switzerland)

Author keywords

(D amino acid) oxidase; Multistep inactivation mechanism; Stability; Stabilization

Indexed keywords

ACTIVATION ENERGY; ENZYME KINETICS; ION EXCHANGE; OXIDATION; PROTEINS; RATE CONSTANTS; THERMODYNAMIC STABILITY;

INACTIVATION KINETICS; MULTISTEP INACTIVATION MECHANISM; PROTEIN CONCENTRATIONS; TRIGONOPSIS VARIABILIS; UNFOLDING REACTION;

AMINO ACIDS;

5,5' DITHIOBIS(2 NITROBENZOIC ACID); CYSTEINE; DEXTRO AMINO ACID OXIDASE; DITHIOTHREITOL; FUNGAL ENZYME; POTASSIUM DIHYDROGEN PHOSPHATE; PROTEIN SUBUNIT;

ARTICLE; CHEMICAL MODIFICATION; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; DENATURATION; ENZYME BINDING; ENZYME INACTIVATION; ENZYME KINETICS; ENZYME POLYMORPHISM; ENZYME PURIFICATION; ENZYME STRUCTURE; FUNGAL STRAIN; ION EXCHANGE CHROMATOGRAPHY; NONHUMAN; OXYGENATION; PH; PROTEIN AGGREGATION; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE; THERMOSTABILITY; TRIGONOPSIS VARIABILIS;

TRIGONOPSIS VARIABILIS;

EID: 33845517037     PISSN: 10242422     EISSN: 10292446     Source Type: Journal    
DOI: 10.1080/10242420601034025     Document Type: Article

References (31)

1. Betancor, L and Hidalgo, A and Fernández-Lorente, G and Mateo, C and Rodriguez, V and Fuentes, M and Lopez-Gallego, F and Fernández-Lafuente, R and Guisan, JM. (2003) Use of physicochemical tools to determine the choice of optimal enzyme: stabilization of D-amino acid oxidase Biotechnol Prog, 19, pp. 784-788.
2. Dib, I and Slavica, A and Riethorst, W and Nidetzky, B. (2006) Thermal inactivation of D-amino acid oxidase from Trigonopsis variabilis occurs via three parallel paths of irreversible denaturation Biotechnol Bioeng, 94, pp. 645-654.
3. D'Souza, SF and Desphande, A. (2001) Simultaneous purification and reversible immobilization of D-amino acid oxidase from Trigonopsis variabilis on a hydrophobic support Appl Biochem Biotechnol, 95, pp. 83-92.
4. Eschrich, K and van Berkel, WJH and Westphal, AH and de Kok, A and Mattevi, A and Obmolova, G and Kalk, KH and Hol, WGJ. (1990) Engineering of microheterogeneity-resistant p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens FEBS Lett, 277, pp. 197-199.
5. Fernández-Lafuente, R and Rodriguez, V and Mateo, C and Fernández-Lorente, G and Arminsen, P and Sabaquillo, P and Guisan, P. (1999a) Stabilization of enzymes (D-amino acid oxidase) against hydrogen peroxide via immobilization and post-immobilization techniques J Mol Catal, B Enzym, 7, pp. 173-179.
6. Fernández-Lafuente, R and Rodriguez, V and Mateo, C and Penzol, G and Hernandez-Justiz, O and Irazoqui, G and Villarino, A and Ovsejevi, K and Batista, F and Guisan, JM. (1999b) Stabilization of multimeric enzymes via immobilization and post-immobilization techniques J Mol Catal, B Enzym, 7, pp. 181-189.
7. Habeeb, AFSA. (1972) Reaction of protein sulfhydryl groups with Ellman's reagent Methods Enzymol, 25, pp. 457-464.
8. Joke M, Kajiyama, N. Kokai T.K. 2004. Preparation of heat stable D-amino acid oxidase by mutagenesis. JP 2004180624.
9. Ju, SS and Lin, LL and Chien, HR and Hsu, WH. (2000) Substitution of the critical methionine residues in Trigonopsis variabilis D-amino acid oxidase with leucine enhances its resistance to hydrogen peroxide FEMS Microbiol Lett, 186, pp. 215-219.
10. Khang, YH and Kim, IW and Hah, YR and Hwangbo, JH and Kang, KK. (2003) Fusion protein of Vitreoscilla hemoglobin with D-amino acid oxidase enhances activity and stability of biocatalyst in the bioconversion process of cephalosporin C Biotechnol Bioeng, 82, pp. 480-488.
11. Kim JW, Shin SK, Hwang HY, Choi SY, Yun JC. 2003. Immobilization of D-amino acid oxidase or glutaryl-7-aminocephalosporanic acid acylase on silica gel or composite silica gel carrier. WO 2003031610.
12. Lemanique, A and Braun, J and LeGoffic, F. (1988) Influence de la polymérysation de la D-amino acid oxidase sur le comportement de l'enzyme imobilisée sur chitosane par fixation covalente Eur J Biochem, 174, pp. 171-176.
13. Lopez-Gallego, F and Batencor, L and Hidalgo, A and Mateo, C and Fernandez-Lafuente, R and Guisan, JM. (2005) One-pot conversion of cephalosporin C to 7-aminocephalosporanic acid in the absence of hydrogen peroxide Adv Synth Catal, 347, pp. 1804-1810.
14. Matsuyama, N and Yamaguchi, M and Toyosato, M and Takayama, M and Mizuno, K. (2001) New enzymatic colorimetric assay for total homocysteine Clin Chem, 47, pp. 2155-2157.
15. Moreno, JA and Ruiz, CA and Catalan, J and Galan, MA. (2004) Thermal deactivation and inhibition of D-amino acid oxidase in permeabilized cells of the yeast Trigonopsis variabilis J Chem Technol Biotechnol, 79, pp. 321-326.
16. Patel, RN. (2001) Enzymatic synthesis of chiral intermediates for Omapatrilat, an antihypertensive drug Biomol Eng, 17, pp. 167-182.
17. Pilone, MS. (2000) D-amino acid oxidase: New findings Cell Mol Life Sci, 57, pp. 1732-1747.
18. Pilone, MS and Pollegioni, L. (2002) D-amino acid oxidase as an industrial biocatalyst Biocatal Biotrans, 20, pp. 145-159.
19. Pollegioni, L and Caldinelli, L and Molla, G and Sacchi, S and Pilone, MS. (2004) Catalytic properties of D-amino acid oxidase in cephalosporin C bioconversion: A comparison between proteins from different sources Biotechnol Prog, 20, pp. 467-473.
20. Pollegioni, L and Lorenzi, S and Rosini, E and Marcone, GL and Molla, G and Verga, R and Cabri, W and Pilone, MS. (2005) Evolution of an acylase active on cephalosporin C Protein Sci, 14, pp. 3064-3076.
21. Riethorst, W and Reichert, A. (1999) An industrial view on enzymes for the cleavage of cephalosporin C Chimia, 53, pp. 600-607.
22. Sadana, A. (1993) Models of enzyme inactivation. Berlin: Springer-Verlag.
23. Schräder, T and Andreesen, JR. (1993) Evidence for the functional importance of Cys298 in D-amino acid oxidase from Trigonopsis variabilis Eur J Biochem, 218, pp. 735-744.
24. Schräder, T and Andreesen, JR. (1996) Studies on the inactivation of the flavoprotein D-amino acid oxidase from Trigonopsis variabilis Appl Microbiol Biotechnol, 45, pp. 458-464.
25. Slavica, A and Dib, I and Nidetzky, B. (2005) Single-site oxidation, cysteine 108 to cysteine sulfinic acid, in D-amino acid oxidase from Trigonopsis variabilis and its structural and functional consequences Appl Environ Microbiol, 71, pp. 8061-8068.
26. Tishkov, VI and Khoronenkova, SV. (2005) D-Amino acid oxidase: Structure, catalytic mechanism, and practical application Biochemistry (Moscow), 70, pp. 40-54.
27. Trampitsch, C and Slavica, A and Riethorst, W and Nidetzky, B. (2005) Reaction of Trigonopsis variabilis D-amino acid oxidase with 2,6-dichloroindophenol: Kinetic characterization and development of an oxygen-independent assay of the enzyme activity J Mol Catal B: Enzym, 32, pp. 271-278.
28. Trost, EM and Fischer, L. (2002) Minimization of by-product formation during D-amino acid oxidase catalyzed racemate resolution of D/L-amino acids J Mol Catal B: Enzym, 19-20, pp. 189-195.
29. van Berkel, WJH and Müller, F. (1987) The elucidation of the microheterogeneity of highly purified p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens by various biochemical techniques Eur J Biochem, 167, pp. 35-46.
30. van der Bolt, FJ and Drijfhout, MC and Eppink, MH and Hagen, WR and van Berkel, WJ. (1994) Selective cysteine→serine replacements in p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens allow the unambiguous assignment of Cys211 as the site of modification by spin-labeled p-chloromercuribenzoate Protein Eng, 7, pp. 801-804.
31. van der Laan, JM and Swarte, MBA and Groendijk, H and Hol, WGJ and Drenth, J. (1989) The influence of purification and protein heterogeneity on the crystallization of p-hydroxybenzoate hydroxylase Eur J Biochem, 179, pp. 715-724.