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Sorbitol counteracts high hydrostatic pressure-induced denaturation of inulin fructotransferase.

Abstract：

:Inulin fructotransferase (IFTase), a novel hydrolase for inulin, was exposed to high hydrostatic pressure (HHP) at 400 and 600 MPa for 15 min in the presence or absence of sorbitol. Sorbitol protected the enzyme against HHP-induced activity loss. The relative residual activity increased nearly 3.1- and 3.8-fold in the presence of 3 mol/L sorbitol under 400 MPa and 600 MPa for 15 min, respectively. Circular dichroism results indicated that the original chaotic unfolding conformation of the enzyme under HHP shifted toward more ordered and impact with 3 mol/L sorbitol. Fluorescence and UV spectra results suggested that sorbitol prevented partially the unfolding of the enzyme and stabilized the conformation under high pressure. These results might be attributed to the binding of sorbitol on the surface of IFTase to rearrange and strengthen intra- and intermolecular hydrogen bonds.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Li Y,Miao M,Liu M,Jiang B,Zhang T,Chen X

doi

10.1016/j.ijbiomac.2014.06.023

subject

Has Abstract

pub_date

2014-09-01 00:00:00

pages

251-6

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(14)00406-1

journal_volume

70

pub_type

杂志文章

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