dc.creator | Burgos, Martha Ines | |
dc.creator | Ochoa, Aylen | |
dc.creator | Perillo, Maria Angelica | |
dc.date.accessioned | 2019-09-04T17:19:49Z | |
dc.date.accessioned | 2022-10-15T10:05:00Z | |
dc.date.available | 2019-09-04T17:19:49Z | |
dc.date.available | 2022-10-15T10:05:00Z | |
dc.date.created | 2019-09-04T17:19:49Z | |
dc.date.issued | 2019-01-01 | |
dc.identifier | Burgos, Martha Ines; Ochoa, Aylen; Perillo, Maria Angelica; β-sheet to α-helix conversion and thermal stability of β-Galactosidase encapsulated in a nanoporous silica gel; Academic Press Inc Elsevier Science; Biochemical and Biophysical Research Communications; 508; 1; 1-1-2019; 270-274 | |
dc.identifier | 0006-291X | |
dc.identifier | http://hdl.handle.net/11336/82881 | |
dc.identifier | CONICET Digital | |
dc.identifier | CONICET | |
dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/4373650 | |
dc.description.abstract | The effect on protein conformation and thermal stability was studied for β-Galactosidase (β-Gal) encapsulated in the nanopores of a silicate matrix (Eβ-Gal). Circular dichroism spectra showed that, compared with the enzyme in buffer (Sβ-Gal), Eβ-Gal exhibited a higher content of α-helix structure. Heating Eβ-Gal up to 75 °C caused a decrease in the content of β-sheet structure and additional augments on Eβ-Gal components attributed to helical content, instead of the generalized loss of the ellipticity signal observed with Sβ-Gal. Steady state fluorescence spectroscopy analysis evidenced an Eβ-Gal structure less compact and more accessible to solvent and also less stable against temperature increase. While for Sβ-Gal the denaturation midpoint (Tm) was 59 °C, for Eβ-Galit was 48 °C. The enzymatic activity assays at increasing temperatures showed that in both conditions, the enzyme lost most of its hydrolytic activity against ONPG at temperatures above 65 °C and Eβ-Gal did it even at lower T values. Concluding, confinement in silica nanopores induced conformational changes on the tertiary/cuaternary structure of Eβ-Gal leading to the loss of thermal stability and enzymatic activity. | |
dc.language | eng | |
dc.publisher | Academic Press Inc Elsevier Science | |
dc.relation | info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0006291X18324859 | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bbrc.2018.11.077 | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/restrictedAccess | |
dc.subject | Biomaterials | |
dc.subject | Catalytic Activity | |
dc.subject | Circular Dichroism | |
dc.subject | Encapsulation | |
dc.subject | Silicate Matrix | |
dc.subject | Steady State Intrinsic Fluorescence | |
dc.title | β-sheet to α-helix conversion and thermal stability of β-Galactosidase encapsulated in a nanoporous silica gel | |
dc.type | info:eu-repo/semantics/article | |
dc.type | info:ar-repo/semantics/artículo | |
dc.type | info:eu-repo/semantics/publishedVersion | |