Protein engineering for thermostabilisation of proteins: some theoretical rules and application to a β-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 β-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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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. © 1998 Elsevier B.V. All rights reserved.

Original language	English
Title of host publication	Progress in Biotechnology
Pages	303-310
Number of pages	7
Volume	15
DOIs	https://doi.org/10.1016/S0921-0423(98)80045-2
Publication status	Published - 1 Jan 1998

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title = "Protein engineering for thermostabilisation of proteins: some theoretical rules and application to a β-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. {\textcopyright} 1998 Elsevier B.V. All rights reserved.",

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",

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

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TY - CHAP

T1 - Protein engineering for thermostabilisation of proteins: some theoretical rules and application to a β-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 - 1998/1/1

Y1 - 1998/1/1

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. © 1998 Elsevier B.V. All rights reserved.

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. © 1998 Elsevier B.V. All rights reserved.

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

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

M3 - Chapter

SN - 0921-0423

VL - 15

SP - 303

EP - 310

BT - Progress in Biotechnology

ER -

Protein engineering for thermostabilisation of proteins: some theoretical rules and application to a β-glucanase

Abstract

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