SAXS Studies of the Endoglucanase Cel12A from Show Its Monomeric Structure and Reveal the Influence of Temperature on the Structural Stability of the Enzyme

Overview

Journal Materials (Basel)

Publisher MDPI

Date 2017 Aug 10

PMID 28788125

Authors

Lis S Miotto

Caio V Dos Reis

Mario de Oliveira Neto

Igor Polikarpov

Affiliations

Soon will be listed here.

Abstract

Endoglucanases are key enzymes applied to the conversion of biomass aiming for second generation biofuel production. In the present study we obtained the small angle X-ray scattering (SAXS) structure of the -1,4-β-glucanase Cel12A and investigated the influence of an important parameter, temperature, on both secondary and tertiary structure of the enzyme and its activity. The CD analysis for GtCel12A revealed that changes in the CD spectra starts at 55 °C and the calculated from the experimental CD sigmoid curve using the Boltzmann function was 60.2 ± 0.6 °C. SAXS data showed that GtCel12A forms monomers in solution and has an elongated form with a maximum diameter of 60 ± 5 Å and a gyration radius of 19.4 ± 0.1 Å as calculated from the distance distribution function. Kratky analysis revealed that 60 °C is the critical temperature above which we observed clear indications of denaturation. Our results showed the influence of temperature on the stability and activity of enzymes and revealed novel structural features of GtCel12A.

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