Protein engineering for thermostabilisation of proteins: Some theoretical rules and application to a ß-glucanase

E. Querol; J. Pons; J. Cedano; M. Vallmitjana; F. García; C. Bonet; J. Pérez-Pons; A. Planas; A. Mozo-Villarías

doi:10.1016/S0921-0423(98)80045-2

Protein engineering for thermostabilisation of proteins: Some theoretical rules and application to a ß-glucanase

E. Querol^*, J. Pons, J. Cedano, M. Vallmitjana, F. García, C. Bonet, J. Pérez-Pons, A. Planas, A. Mozo-Villarías

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Protein thermostability has been investigated by two approaches. (A) Computational. To study the relationship between thermostability and conformational characteristics of proteins, 195 single amino acid residue replacements have been analysed for several protein conformational characteristics. From the analyses, some general rules arise which suggest where amino acid substitutions can be made to enhance protein thermostability. (B) Experimental. Glucohydrolases are biotechnologically important enzymes. We are analysing by site directed mutagenesis the structure/function relationship of two bacterial glucohydrolases, a 1,3-1,4-β-glucanase and a β-glucosidase. We have determined the key residues for catalysis and substrate binding, and redesigned the stability and specificity of the glucanase. A glucanase thermorresistant mutant (N57A) has been obtained.

Idioma original	Anglès
Títol de la publicació	Stability and Stabilization of Biocatalysts
Editors	A. Ballesteros, F.J. Plou, J.L. Iborra, P.J. Halling
Editor	Elsevier Science Publishers
Pàgines	303-310
Nombre de pàgines	8
Edició	1
ISBN (electrònic)	9780080541655
ISBN (imprès)	9780444829702
DOIs	https://doi.org/10.1016/S0921-0423(98)80045-2
Estat de la publicació	Publicada - 10 de nov. 1998

Sèrie de publicacions

Nom	Progress in Biotechnology
Volum	15
ISSN (imprès)	0921-0423

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10.1016/S0921-0423(98)80045-2

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Querol, E., Pons, J., Cedano, J., Vallmitjana, M., García, F., Bonet, C., Pérez-Pons, J., Planas, A., & Mozo-Villarías, A. (1998). Protein engineering for thermostabilisation of proteins: Some theoretical rules and application to a ß-glucanase. In A. Ballesteros, F. J. Plou, J. L. Iborra, & P. J. Halling (Ed.), Stability and Stabilization of Biocatalysts (1 ed., pàg. 303-310). (Progress in Biotechnology; Vol. 15). Elsevier Science Publishers. https://doi.org/10.1016/S0921-0423(98)80045-2

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title = "Protein engineering for thermostabilisation of proteins: Some theoretical rules and application to a {\ss}-glucanase",

abstract = "Protein thermostability has been investigated by two approaches. (A) Computational. To study the relationship between thermostability and conformational characteristics of proteins, 195 single amino acid residue replacements have been analysed for several protein conformational characteristics. From the analyses, some general rules arise which suggest where amino acid substitutions can be made to enhance protein thermostability. (B) Experimental. Glucohydrolases are biotechnologically important enzymes. We are analysing by site directed mutagenesis the structure/function relationship of two bacterial glucohydrolases, a 1,3-1,4-β-glucanase and a β-glucosidase. We have determined the key residues for catalysis and substrate binding, and redesigned the stability and specificity of the glucanase. A glucanase thermorresistant mutant (N57A) has been obtained.",

author = "E. Querol and J. Pons and J. Cedano and M. Vallmitjana and F. Garc{\'i}a and C. Bonet and J. P{\'e}rez-Pons and A. Planas and A. Mozo-Villar{\'i}as",

year = "1998",

month = nov,

day = "10",

doi = "10.1016/S0921-0423(98)80045-2",

language = "English",

isbn = "9780444829702",

series = "Progress in Biotechnology",

publisher = "Elsevier Science Publishers",

pages = "303--310",

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Querol, E, Pons, J, Cedano, J, Vallmitjana, M, García, F, Bonet, C, Pérez-Pons, J, Planas, A & Mozo-Villarías, A 1998, Protein engineering for thermostabilisation of proteins: Some theoretical rules and application to a ß-glucanase. in A Ballesteros, FJ Plou, JL Iborra & PJ Halling (ed.), Stability and Stabilization of Biocatalysts. 1 ed., Progress in Biotechnology, vol. 15, Elsevier Science Publishers, pàg. 303-310. https://doi.org/10.1016/S0921-0423(98)80045-2

Protein engineering for thermostabilisation of proteins: Some theoretical rules and application to a ß-glucanase. / Querol, E.; Pons, J.; Cedano, J. et al.
Stability and Stabilization of Biocatalysts. ed. / A. Ballesteros; F.J. Plou; J.L. Iborra; P.J. Halling. 1. ed. Elsevier Science Publishers, 1998. pàg. 303-310 (Progress in Biotechnology; Vol. 15).

Producció científica: Capítol de llibre › Contribució a congrés/conferència › Avaluat per experts

TY - GEN

T1 - Protein engineering for thermostabilisation of proteins

T2 - Some theoretical rules and application to a ß-glucanase

AU - Querol, E.

AU - Pons, J.

AU - Cedano, J.

AU - Vallmitjana, M.

AU - García, F.

AU - Bonet, C.

AU - Pérez-Pons, J.

AU - Planas, A.

AU - Mozo-Villarías, A.

PY - 1998/11/10

Y1 - 1998/11/10

N2 - Protein thermostability has been investigated by two approaches. (A) Computational. To study the relationship between thermostability and conformational characteristics of proteins, 195 single amino acid residue replacements have been analysed for several protein conformational characteristics. From the analyses, some general rules arise which suggest where amino acid substitutions can be made to enhance protein thermostability. (B) Experimental. Glucohydrolases are biotechnologically important enzymes. We are analysing by site directed mutagenesis the structure/function relationship of two bacterial glucohydrolases, a 1,3-1,4-β-glucanase and a β-glucosidase. We have determined the key residues for catalysis and substrate binding, and redesigned the stability and specificity of the glucanase. A glucanase thermorresistant mutant (N57A) has been obtained.

AB - Protein thermostability has been investigated by two approaches. (A) Computational. To study the relationship between thermostability and conformational characteristics of proteins, 195 single amino acid residue replacements have been analysed for several protein conformational characteristics. From the analyses, some general rules arise which suggest where amino acid substitutions can be made to enhance protein thermostability. (B) Experimental. Glucohydrolases are biotechnologically important enzymes. We are analysing by site directed mutagenesis the structure/function relationship of two bacterial glucohydrolases, a 1,3-1,4-β-glucanase and a β-glucosidase. We have determined the key residues for catalysis and substrate binding, and redesigned the stability and specificity of the glucanase. A glucanase thermorresistant mutant (N57A) has been obtained.

UR - https://www.scopus.com/pages/publications/77957039565

U2 - 10.1016/S0921-0423(98)80045-2

DO - 10.1016/S0921-0423(98)80045-2

M3 - Conference contribution

AN - SCOPUS:77957039565

SN - 9780444829702

T3 - Progress in Biotechnology

SP - 303

EP - 310

BT - Stability and Stabilization of Biocatalysts

A2 - Ballesteros, A.

A2 - Plou, F.J.

A2 - Iborra, J.L.

A2 - Halling, P.J.

PB - Elsevier Science Publishers

ER -

Querol E, Pons J, Cedano J, Vallmitjana M, García F, Bonet C et al. Protein engineering for thermostabilisation of proteins: Some theoretical rules and application to a ß-glucanase. In Ballesteros A, Plou FJ, Iborra JL, Halling PJ, editors, Stability and Stabilization of Biocatalysts. 1 ed. Elsevier Science Publishers. 1998. pàg. 303-310. (Progress in Biotechnology). doi: 10.1016/S0921-0423(98)80045-2

Protein engineering for thermostabilisation of proteins: Some theoretical rules and application to a ß-glucanase

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