Japanese Journal of Water Treatment Biology
Online ISSN : 1881-0438
Print ISSN : 0910-6758
ISSN-L : 0910-6758
ORIGINALS
Adsorption and Enzymatic Activity of Immobilized Catalase on Calcined Montmorillonite and Pillared Interlayer Clays
MITSUAKI SUZUKIYUTAKA MATSUMOTOTAKAHIRO SEKIKAWAKEISUKE IWAHORI
Author information
JOURNAL FREE ACCESS

2008 Volume 44 Issue 3 Pages 161-167

Details
Abstract
The application of the enzyme catalase in the textile bleaching process requires the use of catalase under high-temperature, alkaline conditions. We therefore investigated the immobilization of catalase on calcined montmorillonite and pillared interlayer clays (PILCs) as a means of increasing the enzyme’s temperature and pH stabilities. SiO2-PILCs and Al2O3-PILCs were prepared from montmorillonite and were calcined at 400 or 600 ℃. The temperature stability of catalase immobilized on the clays was higher than that of free catalase up to 55 ℃. Additionally, the pH at which the catalase immobilized on the two PILCs was stable was shifted to more alkaline values compared to the pH values for free catalase. In particular, the relative activity (with 100% activity being defined as that observed at pH 7) of catalase immobilized on Al2O3-PILCs was higher than that of free catalase at pH 8–12. Furthermore, the relative activity at pH 10–11 of catalase immobilized on Al2O3-PILCs calcined at 600 ℃ was only 40–60% of that observed at pH 7 for the same PILC. However, the relative activity of catalase immobilized on calcined montmorillonite was almost the same as that of free catalase at pH >7.
Content from these authors
© 2008 by Japanese Society of Water Treatment Biology
Previous article Next article
feedback
Top