fulltext.study @t Gmail

Kinetic study of the colloidal and enzymatic stability of β-galactosidase, for designing its encapsulation route through sol–gel route assisted by Triton X-100 surfactant

Paper ID Volume ID Publish Year Pages File Format Full-Text
3304 163 2013 7 PDF Available
Title
Kinetic study of the colloidal and enzymatic stability of β-galactosidase, for designing its encapsulation route through sol–gel route assisted by Triton X-100 surfactant
Abstract

•DLS and zeta-potential data may help to explain the β-galactosidase deactivation.•Triton X-100 at 1 × 10–3 M concentration delays the β-galactosidase deactivation.•Preliminary conditions for sol–gel encapsulation of β-galactosidase are suggested.

The kinetic study of the colloidal and enzymatic stability for the β-galactosidase of Bacillus circulans was carried out in function of the presence of Triton X-100 surfactant, under orbital agitation and varying the pH and temperature. The correlation between the Dynamic Light Scattering and enzyme assay data, supported by z-potential and Differential Scanning Calorimetry analyses, gave insights about the mechanism of the protective role of the surfactant against the enzyme deactivation during its incubation. The best conditions for preserving the enzymatic activity, under orbital agitation, were: presence of 1 × 10−3M Triton X-100, at pH 6.0 and 25 °C or 40 °C during less than 24 h, even in the presence of 0.1 M sodium cations or 4% ethanol. As these conditions also affect the polycondensation of the siliceous species and the enzyme-silica interactions, these could be considered as primary information for designing and optimizing an encapsulation route of β-galactosidase in silica, by a sol–gel process assisted by surfactant.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slide

Keywords
β-galactosidase deactivation; Colloidal stability; Biocatalysis; Sol–gel conditions; Non-ionic surfactant Triton X-100 (β-galactosidases (β-gal))
First Page Preview
Kinetic study of the colloidal and enzymatic stability of β-galactosidase, for designing its encapsulation route through sol–gel route assisted by Triton X-100 surfactant
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us
Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 75, 15 June 2013, Pages 32–38
Authors
, , ,
Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us