fulltext.study @t Gmail

Immobilization of β-galactosidase from Kluyveromyces lactis onto a polysiloxane–polyvinyl alcohol magnetic (mPOS–PVA) composite for lactose hydrolysis

Paper ID Volume ID Publish Year Pages File Format Full-Text
51755 46853 2008 6 PDF Available
Title
Immobilization of β-galactosidase from Kluyveromyces lactis onto a polysiloxane–polyvinyl alcohol magnetic (mPOS–PVA) composite for lactose hydrolysis
Abstract

β-Galactosidase from Kluyveromyces lactis was covalently immobilized onto a mPOS–PVA, using glutaraldehyde as activating agent and its properties were evaluated. The enzymatic water insoluble derivative displayed the same optimum pH (6.5) and optimum temperature (50 °C) of the soluble enzyme. The apparent Kmapp and activation energy for both soluble and immobilized enzyme derivative were found to be not significantly different. The mPOS–PVA β-galactosidase preparation presented a higher operational and thermal stability than the soluble enzyme. This immobilized β-galactosidase also was effective in hydrolyzing lactose from milk. Hence, one can conclude that mPOS–PVA is an attractive and efficient support for β-galactosidase immobilization.

Keywords
β-Galactosidase; Kluyveromyces lactis; Covalent immobilization; Polysiloxane; Polyvinyl alcohol; Magnetic support
First Page Preview
Immobilization of β-galactosidase from Kluyveromyces lactis onto a polysiloxane–polyvinyl alcohol magnetic (mPOS–PVA) composite for lactose hydrolysis
Publisher
Database: Elsevier - ScienceDirect
Journal: Catalysis Communications - Volume 9, Issue 14, 30 August 2008, Pages 2334–2339
Authors
, , , , ,
Subjects
Physical Sciences and Engineering Chemical Engineering Catalysis