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Glucose oxidase (GOX; β-d-glucose:oxygen oxidoreductase) from Aspergillus niger is a dimeric flavoprotein with a molecular mass of 80 kDa/monomer. Thermal denaturation of glucose oxidase has been studied by absorbance, circular dichroism spectroscopy, viscosimetry, and differential scanning calorimetry. Thermal transition of this homodimeric enzyme is irreversible and, surprisingly, independent of GOX concentration (0.2–5.1 mg/ml). It has an apparent transition temperature of 55.8 ± 1.2 °C and an activation energy of ∼280 kJ/mol, calculated from the Lumry-Eyring model. The thermally denatured state of GOX after recooling has the following characteristics. (i) It retains ∼70% of the native secondary structure ellipticity; (ii) it has a relatively low intrinsic viscosity, 7.5 ml/g; (iii) it binds ANS; (iv) it has a low Stern-Volmer constant of tryptophan quenching; and (v) it forms defined oligomeric (dimers, trimers, tetramers) structures. It is significantly different from chemically denatured (6.67 m GdmHCl) GOX. Both the thermal and the chemical denaturation of GOX cause dissociation of the flavin cofactor; however, only the chemical denaturation is accompanied by dissociation of the homodimeric GOX into monomers. The transition temperature is independent of the protein concentration, and the properties of the thermally denatured protein indicate that thermally denatured GOX is a compact structure, a form of molten globule-like apoenzyme. GOX is thus an exceptional example of a relatively unstable mesophilic dimeric enzyme with residual structure in its thermally denatured state. Glucose oxidase (GOX; β-d-glucose:oxygen oxidoreductase) from Aspergillus niger is a dimeric flavoprotein with a molecular mass of 80 kDa/monomer. Thermal denaturation of glucose oxidase has been studied by absorbance, circular dichroism spectroscopy, viscosimetry, and differential scanning calorimetry. Thermal transition of this homodimeric enzyme is irreversible and, surprisingly, independent of GOX concentration (0.2–5.1 mg/ml). It has an apparent transition temperature of 55.8 ± 1.2 °C and an activation energy of ∼280 kJ/mol, calculated from the Lumry-Eyring model. The thermally denatured state of GOX after recooling has the following characteristics. (i) It retains ∼70% of the native secondary structure ellipticity; (ii) it has a relatively low intrinsic viscosity, 7.5 ml/g; (iii) it binds ANS; (iv) it has a low Stern-Volmer constant of tryptophan quenching; and (v) it forms defined oligomeric (dimers, trimers, tetramers) structures. It is significantly different from chemically denatured (6.67 m GdmHCl) GOX. Both the thermal and the chemical denaturation of GOX cause dissociation of the flavin cofactor; however, only the chemical denaturation is accompanied by dissociation of the homodimeric GOX into monomers. The transition temperature is independent of the protein concentration, and the properties of the thermally denatured protein indicate that thermally denatured GOX is a compact structure, a form of molten globule-like apoenzyme. GOX is thus an exceptional example of a relatively unstable mesophilic dimeric enzyme with residual structure in its thermally denatured state. Glucose oxidase (GOX 1The abbreviations used are: GOX, glucose oxidase; DSC, differential scanning calorimetry; ANS, 8-anilino-1-naphthalenesulfonate; Gdm-HCl, guanidinium hydrochloride.1The abbreviations used are: GOX, glucose oxidase; DSC, differential scanning calorimetry; ANS, 8-anilino-1-naphthalenesulfonate; Gdm-HCl, guanidinium hydrochloride.; β-d-glucose:oxygen oxidoreductase, EC 1.1.3.4) is a flavoenzyme that catalyzes oxidation of β-d-glucose by molecular oxygen to δ-gluconolactone, which subsequently hydrolyzes spontaneously to gluconic acid and hydrogen peroxide. The enzyme contains one tightly, noncovalently bound FAD cofactor per monomer and is a homodimer with a molecular mass of 160 kDa, depending on the extent of glycosylation (1Hecht H.J. Kalisz H.M. Hendle J. Schmid R.D. Schomburg D. J. Mol. Biol. 1993; 229: 153-172Crossref PubMed Scopus (634) Google Scholar). Glucose oxidase from Aspergillus niger is glycosylated by neutral sugars (mostly mannose-like sugars) and by amino sugars (2Tsuge H. Natsuaki O. Ohashi K. J. Biochem. (Tokyo). 1975; 78: 835-843Crossref PubMed Scopus (138) Google Scholar). Several reports find that the sugar content may vary from 11 up to 30% (3Swoboda B.E.P. Massey V. J. Biol. Chem. 1965; 240: 2209-2215Abstract Full Text PDF PubMed Google Scholar, 4Nakamura S. Hayashi S. FEBS Lett. 1974; 41: 327-330Crossref PubMed Scopus (26) Google Scholar, 5Kalisz H.M. Hecht H.J. Schomburg D. Schmid R.D. Biochim. Biophys. Acta. 1991; 1080: 138-142Crossref PubMed Scopus (95) Google Scholar). GOX is of considerable commercial importance. The enzyme has applications in the food and fermentation industry, in the textile industry, and as a molecular diagnostic and analytical tool in medical and environmental monitoring applications (6Röhr M. Kubicek C.P. Kominek J. Rehm H.J. Reed G. Biotechnology. 3. Verlag Chemie Weiheim, Munich, Germany1983: 455-456Google Scholar, 7Frew J.E. Hill H.A. Philos. Trans. R. Soc. Lond. B Biol. Sci. 1987; 316: 95-106Crossref PubMed Scopus (34) Google Scholar, 8Turner A.P.F. Karube L. Wilson G.S. Biosensors: Fundamentals and Applications. Oxford University Press, Oxford1987: 770Google Scholar, 9Tzanov T. Costa S.A. Gubitz G.M. Cavaco-Paulo A. J. Biotechnol. 2002; 93: 87-94Crossref PubMed Scopus (116) Google Scholar, 10Wang S. Yoshimoto M. Fukunaga K. Nakao K. Biotechnol. Bioeng. 2003; 83: 444-453Crossref PubMed Scopus (36) Google Scholar). The study of GOX and its applications is limited by its conformational instability. A significant effort has been made to increase the stability of GOX. It is known that both the thermal stability and the dynamic properties of the enzyme depend on its redox state (11Nakamura S. Koga K. Biochem. Biophys. Res. Commun. 1977; 78: 806-810Crossref PubMed Scopus (9) Google Scholar, 12Haouz A. Twist C. Zentz C. Tanc P. Alpert B. Eur. Biophys. J. 1998; 27: 19-25Crossref PubMed Scopus (68) Google Scholar). Protein glycosylation affects the conformational dynamics of the active site and thus the activity of the enzyme (13Kohen A. Jonsson T. Klinman J.P. Biochemistry. 1997; 36: 2603-2611Crossref PubMed Scopus (95) Google Scholar). However, the way in which glycosylation affects the stability of GOX is not known. On the other hand, modification of the glucose oxidase surface by artificial long polyethylene-glycol chains results in an increased melting temperature (14Seymour S.L. Klinman J.P. Biochemistry. 2002; 41: 8747-8758Crossref PubMed Scopus (45) Google Scholar). Externally added polyols like sorbitol significantly increased the melting temperature of glucose oxidase R. Biochem. Mol. Biol. Google Scholar). The activity and conformational stability been studied in the state Biochem. J. PubMed Scopus Google Scholar, 2002; PubMed Scopus Google in the state B. 1977; PubMed Scopus Google and in the of different as and and A. V. Biochemistry. PubMed Scopus Google Scholar, A. V. Biochemistry. 2002; 41: PubMed Scopus Google Scholar, S.A. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). the in the thermal of GOX, the of the irreversible thermally denaturation is not in the the apparent transition temperature of the thermal denaturation of the the thermal denaturation of GOX a of denaturation by and R. H. J. Chem. Scopus Google Scholar, Biophys. J. Full Text PDF PubMed Scopus Google Scholar). results to (i) the thermally denatured (ii) a of thermal and (iii) indicate a of in the that the thermal transition of glucose of from and Glucose oxidase from and the protein The concentration of glucose oxidase calculated the (3Swoboda B.E.P. Massey V. J. Biol. Chem. 1965; 240: 2209-2215Abstract Full Text PDF PubMed Google Scholar). with a with an apparent molecular mass of 80 The of guanidinium from an PubMed Scopus Google Scholar). The of the with a The surface of calculated J. Chem. 2002; PubMed Scopus Google Scholar). on a with glucose oxidase °C in and a concentration of A with a used the and a used the and is the of the of The thermal a constant of and with different of The temperature of the with a on a The in different and in the to of the of the and the The flavin in the of The and the by an thermal The temperature the with a to a The concentration of glucose oxidase in on a and a in the of the and and The protein concentration in in a of of the in to the of glucose oxidase as the in the with and of a m concentration in The with added to the in The after the Stern-Volmer (1Hecht H.J. Kalisz H.M. Hendle J. Schmid R.D. Schomburg D. J. Mol. Biol. 1993; 229: 153-172Crossref PubMed Scopus (634) Google a of Biochem. PubMed Scopus Google is the Stern-Volmer The Stern-Volmer by The Stern-Volmer from the of the The of FAD and an a on a defined of M. Sci. 2003; Scopus Google Scholar). The of the The concentration of glucose oxidase in the and of m used the used as a The thermal with a scanning of The calculated from the is the of protein and is the of the The calculated by the following the concentration of the protein in of the intrinsic viscosity, from the by the of a of the native and thermally and chemically of glucose oxidase by as A. V. Biochemistry. 2002; 41: PubMed Scopus Google with The as (i) concentration of and (ii) of in m and and to °C by a of made in the of in the of the University of on the in a °C The by the of and Scopus Google Scholar). The calculated the on the as A. J. B. J.P. FEBS Lett. PubMed Scopus Google Scholar, A. J. Biochemistry. PubMed Scopus Google Scholar). on GOX The molecular of the GOX calculated from as is the and viscosity, is the is the and is the of the The GOX in S. S. J. Biochem. (Tokyo). PubMed Scopus Google and GOX in with J. Biochemistry. PubMed Scopus Google Scholar). The and of the of made K. C. J. Biol. Chem. Full Text PDF PubMed Google Scholar). The (3Swoboda B.E.P. Massey V. J. Biol. Chem. 1965; 240: 2209-2215Abstract Full Text PDF PubMed Google Scholar). of Thermal thermal transition of glucose oxidase a the and of the native and denatured form is temperature is the constant is the apparent and is the apparent temperature of transition of the is in the native The with a on a and The of The protein concentration the flavin Biochem. PubMed Scopus Google Scholar). The thermal transition of glucose oxidase irreversible in of the the the used to the of the that accompanied the protein thermal The transition temperature and the of the thermal not on the protein and flavin concentration The of the and after the with of Glucose in the of thermally and chemically denatured GOX in the relatively defined in both the and differential in the of the used to the thermally in the active site of the protein protein The transition temperature of the thermal denaturation in the of to the in the GOX irreversible of the thermally denatured protein in of the flavin as by the of the flavin and not the dissociation constant the flavin thermal and the flavin cofactor from the active site as (3Swoboda B.E.P. Massey V. J. Biol. Chem. 1965; 240: 2209-2215Abstract Full Text PDF PubMed Google Scholar, Biotechnol. Bioeng. PubMed Scopus Google Scholar). is in with other reports T. M. Soc. Google Scholar, D. Biochim. Biophys. Acta. PubMed Scopus Google Scholar). the transition temperature of thermal denaturation from the flavin independent of the glucose oxidase concentration It that the the thermal denaturation an apparent concentration to the of in the in the the tryptophan the from the flavin The denaturation from the in apparent a transition The transition temperature of the thermal denaturation in this °C and The of GOX thermal denaturation by circular dichroism a that in secondary The to the melting as in the of spectroscopy, thus that the secondary and the with The of a residual the indicate the of by in the and by is to the of the protein and the The transition temperature from °C thermal denaturation is in of Thermal on Protein and and different used the of different protein The GOX concentration in the this concentration not the denaturation temperature of the protein The of the thermal transition of the homodimeric GOX on its concentration the of the transition of the dimeric with m is a of the melting temperature on the concentration of the protein K. Biochemistry. PubMed Scopus Google Scholar, 1987; PubMed Scopus Google the of the irreversible of the the is as it is the The of this the irreversible transition is to the following Biophys. J. Full Text PDF PubMed Scopus Google is the and is the activation the irreversible the irreversible a of of the transition temperature on the protein concentration that the dissociation of the is not of the irreversible the thermal transition by independent of cofactor a in FAD concentration on the thermal transition the of glucose oxidase The irreversible with the thermal denaturation of the protein to the However, the thermal transition the irreversible the denaturation is independent of the Biophys. J. Full Text PDF PubMed Scopus Google as in the of M. M. M. Biochemistry. PubMed Scopus Google Scholar). The transition temperature of the irreversible thermal denaturation of GOX on the the in an increased melting temperature the to vary the from to an increase in the to an increase in the transition temperature up to a the irreversible not the of the thermal this the transition temperature the a M. B. P. A. Biochemistry. 2002; 41: PubMed Scopus Google Scholar). to the intrinsic of the used in DSC, the in the irreversible thermal transition of glucose oxidase from A. from a of of The of this The by the ± ± The the of the melting temperature on the and the is only to the temperature from to the irreversible M. Biochemistry. 27: PubMed Scopus Google Scholar). the to the activation from the of the The activation energy of the irreversible in the thermal denaturation of GOX is ∼280 structure of the thermally and chemically denatured by may by to form a with Press, Scholar). with the of the results of the of the native and the thermally and chemically denatured GOX. the native GOX the protein of only to GOX with m only protein to in with a study A. V. Biochemistry. 2002; 41: PubMed Scopus Google Scholar). the thermally denatured GOX, protein to trimers, and significant of of the protein of of GOX in different GOX in with of S. The molecular of the native GOX calculated and to a in with (1Hecht H.J. Kalisz H.M. Hendle J. Schmid R.D. Schomburg D. J. Mol. Biol. 1993; 229: 153-172Crossref PubMed Scopus (634) Google Scholar, H. Natsuaki O. Ohashi K. J. Biochem. (Tokyo). 1975; 78: 835-843Crossref PubMed Scopus (138) Google Scholar, J. Biochemistry. PubMed Scopus Google Scholar). of GOX in m an apparent of which to the S. the GOX in is not known and, the molecular not calculated from on GOX in A. V. Biochemistry. 2002; 41: PubMed Scopus Google that the the form of GOX. GOX after temperature The the and which of both and dimeric GOX. to of and oxidase is a flavoprotein that binds one flavin per monomer in the active of the flavin and the tryptophan circular dichroism a tool the study of conformational in the active site of glucose the native glucose oxidase a relatively in the and The a that to the flavin the flavin has its in the to the known in the Biochem. 1974; PubMed Scopus Google Scholar). The in the is the to the of FAD and in the active as in other flavin G. R. M. M. Eur. J. Biochem. 2003; PubMed Scopus (36) Google Scholar). The is by the which is to the of the secondary structure with from the The of native GOX in the is a protein and The thermal transition by the of the residual secondary structure °C the stability of the protein secondary of the in ∼70% a relatively of the protein secondary structure the and the the native and the thermally denatured The thermally denatured state in the in the of to the dissociation of FAD from the The of the protein chemically by m a of in the to the of the Protein Chem. 2002; PubMed Scopus Google Scholar). to the dissociation of in the and the of the the protein denatured by B and The in of the thermally denatured and chemically denatured GOX The in the °C of both the of the residual an increase in the concentration in the a in the of of the denatured GOX contains one in the structure that is not to after thermal denaturation S.A. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). of the protein in the of significant on the of the transition on the of the residual structure not and of the °C The of the thermal denaturation of glucose oxidase made it to the thermally denatured state The tryptophan of glucose oxidase is the of the of per monomer and of the to as by the is and to with an surface of that the protein the of the and thus to a low Stern-Volmer used to the of the to tryptophan Biochem. PubMed Scopus Google Scholar). is a of tryptophan in glucose the on glucose in that the state is and the to the in the thermally denatured state. The native protein has a low Stern-Volmer constant ± the irreversible thermal glucose oxidase is in a state with structure with that to the as by the increased Stern-Volmer ± The of the increased in the of The indicate that the of the tryptophan in from native to the thermally denatured and to the chemically denatured state of glucose A is the and The the of the with a Stern-Volmer and flavin of GOX in its constant is of flavin not ± ± ± ± ± ± ± ± ± ± to the of the in the of ± of FAD by in the of significant from ± ± ± is of flavin not Stern-Volmer to the of the in the of D. M. M. M. M. Schmid Biophys. Chem. 2002; PubMed Scopus Google of FAD by in the of significant from in a The of a of FAD with of the The Stern-Volmer GOX in different the the flavin in the denatured and is to the in the native state of the Stern-Volmer constant of FAD in the thermally denatured state is the chemically denatured state. However, the of the is into the the thermally and chemically denatured is low with to the Stern-Volmer of FAD the m by a of D. M. M. M. M. Schmid Biophys. Chem. 2002; PubMed Scopus Google and this results in the Stern-Volmer both denatured of glucose oxidase However, the flavin is not a denatured FAD is to the in the of chemical and thermal in both denatured FAD is in and is not to different of the active site of GOX. The is FAD in and is in the thermally and chemically denatured GOX. the that the FAD into is to the denaturation of the protein of like molten Biochemistry. PubMed Scopus Google Scholar, 1991; PubMed Scopus Google Scholar). The native and chemically denatured not the On the other hand, the thermally denatured state of GOX binds ANS, as is from the of the increase in the and a of the in the thermally denatured glucose oxidase The of to the thermally denatured glucose oxidase that the protein is in a molten globule-like state. of and and of Glucose intrinsic of a protein the of the protein with The intrinsic of glucose oxidase calculated from the protein The intrinsic of the native protein °C which with the J. Biochemistry. PubMed Scopus Google Scholar, B.E.P. Biochim. Biophys. Acta. PubMed Scopus Google Scholar). The thermally denatured protein °C has an intrinsic of 7.5 and the chemically denatured protein has an intrinsic of the is in with the of the chemically denatured state in m J. Biochemistry. PubMed Scopus Google Scholar). the concentration of the to the temperature in the scanning with the of ± M. Sci. 2003; Scopus Google Scholar). The thermal denaturation of the native different with a constant of not to the of the to the The the used of the the increased of the that the transition and the increased of the °C a of the A to an increase of a The of the and the of m the is that of the thermally denatured state the temperature The thermally denatured state thus compact the state. to the in the with the of a state in the of The the of the thermal and denatured protein and with independent of protein It that the of protein used in the relatively a concentration of glucose a in the of the thermal to of the protein protein the of the thermal transition not The Thermal of GOX to a the different to study the thermal and chemical denaturation of the glucose It that thermal denaturation of glucose oxidase is an irreversible transition to the compact denatured form with a defined oligomeric structure that is significantly different from the chemically denatured state of GOX, by and in the protein in the the secondary GOX is an the in the to the secondary in the in the the amino tryptophan However, the of GOX the protein and the the properties to The used to the properties of the active site in the the that GOX is a relatively dimeric protein the transition temperature of the thermal denaturation of GOX is in a from to °C with the 55.8 apparent on protein concentration that the thermal transition of GOX has a It that dissociation of FAD the thermal denaturation is the the transition the of FAD The transition temperature of GOX, as a homodimeric depend on its concentration Biophys. J. Full Text PDF PubMed Scopus Google the homodimeric structure is to to the thermally a in protein concentration in the transition temperature GOX not its oligomeric state in the of thermal transition it into forms is by the that the thermally denatured state of GOX forms in with a D. Biochim. Biophys. Acta. PubMed Scopus Google Scholar). analytical that the thermally denatured state of GOX forms and an of is to the that dissociation of FAD GOX R. Biochem. Mol. Biol. Google Scholar, B.E.P. Biochim. Biophys. Acta. PubMed Scopus Google Scholar). results indicate that after the dissociation of FAD from the the is not in a state to form S.A. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). of the the of an molten globule-like and analytical results and indicate of oligomeric up to results indicate the of a residual structure the apparent of of the protein results in a of the significantly with a in the of in results the of the by thermal thermally denatured GOX with chemically denatured GOX. The chemically denatured GOX in a way as the state of GOX A. V. Biochemistry. 2002; 41: PubMed Scopus Google Scholar). However, results the denaturation GOX contains secondary and and that from the chemically denatured GOX. the thermal transition of GOX it to thermally denatured GOX after recooling and to it with the chemically denatured state. denatured GOX, after the properties of a molten (i) ∼70% secondary structure with a structure and (ii) the to the the Stern-Volmer the of tryptophan of the thermally denatured significantly that of the chemically denatured state with a structure, to the dynamics of the thermally denatured state after results significant the thermally denatured of GOX, low and and the chemically denatured GOX. is to the of the and chemically denatured in intrinsic viscosity, and in in m to the C. Protein Chem. PubMed Scopus Google Scholar). The of residual structure the in the the temperature and of the with C. K. S. J. Biol. Chem. Full Text PDF PubMed Google Scholar). is C. Protein Chem. PubMed Scopus Google that the of a the of a Glucose oxidase in the thermally denatured state of ± glucose oxidase in m ± that is a significantly of the structure in the thermally denatured state in with the protein in the of m of Thermal of following results to a the thermal denaturation of (i) in the residual the a (ii) the transition temperature by different the protein and (iii) the of the thermal The results indicate that the transition is in with the Lumry-Eyring in by Biophys. J. Full Text PDF PubMed Scopus Google and may by the following is the native homodimeric structure, is the thermally denatured and to an to its low the molten globule-like and the chemically denatured may into the following and of trimers, and of GOX after it is that GOX in oligomeric and in the thermally denatured state is of the oligomeric state of the protein The with a and may not The irreversible and accompanied by dissociation and of the FAD the of the thermal transition not by an of and Protein after the site of flavin cofactor is in the thermally denatured state as by and of circular It is to that the flavin cofactor the of this in of the Lumry-Eyring the that the thermal transition is by the of the the concentration to the increase of the transition flavin cofactor not thermal transition of the glucose oxidase of the thermal transition is not by is in the The results by by of a in the of denaturation and of as irreversible of of apparent melting temperature on concentration that the after the the to the thermal dissociation the thermal transition as is by the this the of to a The apparent transition temperature not by the protein this one that (i) dissociation of oligomeric protein it after the (ii) the irreversible and (iii) flavin dissociation after the flavin and protein dissociation not in the of thermal denaturation of glucose oxidase from A. after in a The made it to in a one of the irreversible in the of denaturation the in the of the transition temperature on the it to the activation of this The the activation ∼280 kJ/mol, a temperature the irreversible in the in the transition of GOX in the the transition of thermal denaturation of GOX to FAD dissociation vary a relatively from °C S.A. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google to °C R. Biochem. Mol. Biol. Google to a of secondary and structure by circular dichroism from °C S.A. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google to °C A. V. Biochemistry. PubMed Scopus Google to °C (11Nakamura S. Koga K. Biochem. Biophys. Res. Commun. 1977; 78: 806-810Crossref PubMed Scopus (9) Google Scholar). The of on the with the relatively the activation the by and Koga (11Nakamura S. Koga K. Biochem. Biophys. Res. Commun. 1977; 78: 806-810Crossref PubMed Scopus (9) Google the relatively of is the of a not of the by different with GOX from different and and the transition by °C and °C the protein from and an apparent on other results in this a that the thermal stability of GOX may on It has been that sugars a on GOX R. Biochem. Mol. Biol. Google and one that sugars an of the of of the residual structure in the thermally denatured state of the protein may the of the The residual structure is with a in the of amino Protein Sci. PubMed Scopus Google that to a of S. M. S. Sci. S. A. 2003; PubMed Scopus Google Scholar). is one of the that the protein stability as the energy of temperature 1987; PubMed Scopus Google and to the denaturation temperature S. M. S. Sci. S. A. 2003; PubMed Scopus Google of the of the protein stability to M. M. M. Biochemistry. PubMed Scopus Google Scholar). the of amino in the protein Protein Sci. PubMed Scopus Google it is that with an of amino the of which the protein is is the structure of GOX, which contains amino per it is that a of the residual structure in GOX is to the temperature which the protein is is in the M. M. M. Biochemistry. PubMed Scopus Google Scholar, S. M. S. Sci. S. A. 2003; PubMed Scopus Google Scholar, C. T. A. Protein PubMed Google and in mesophilic D. C. 1993; Full Text PDF PubMed Scopus Google Scholar, J. V. J. Mol. Biol. PubMed Scopus Google Scholar). Glucose oxidase thus one of the mesophilic homodimeric with a residual structure in its thermally denatured state. and K. in the
Žoldák et al. (Thu,) studied this question.
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