fulltext.study @t Gmail

Preparation and characterization of Rhizopus amyloglucosidase immobilized on poly(o-toluidine)

Paper ID Volume ID Publish Year Pages File Format Full-Text
35013 45067 2010 5 PDF Available
Title
Preparation and characterization of Rhizopus amyloglucosidase immobilized on poly(o-toluidine)
Abstract

The starch hydrolyzing enzyme amyloglucosidase (AMG) from Rhizopus was immobilized onto the protonated salt (TS) and basic (TB) forms of chemically synthesized poly(o-toluidine) (POT) using adsorption and covalent binding. The polymers were activated with glutaraldehyde prior to covalent bonding. The immobilization efficiency was affected by the pH of the immobilization medium, contact time and amount of enzyme. After immobilization, the pH and temperature were changed to conditions under which the enzyme is most active. Immobilized AMG was more stable with respect to changes in pH and increases in temperature compared to free AMG. The immobilized enzyme retained high catalytic activity after multiple uses and showed enhanced stability with storage compared to free enzyme.

Keywords
Amyloglucosidase; Immobilization; Poly(o-toluidine); Starch; Glucose
First Page Preview
Preparation and characterization of Rhizopus amyloglucosidase immobilized on poly(o-toluidine)
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: Process Biochemistry - Volume 45, Issue 8, August 2010, Pages 1422–1426
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