Hydrolysis of sucrose by invertase immobilized onto novel magnetic polyvinylalcohol microspheres

Yükleniyor...
Küçük Resim

Tarih

2001

Dergi Başlığı

Dergi ISSN

Cilt Başlığı

Yayıncı

Elsevier Sci Ltd

Erişim Hakkı

info:eu-repo/semantics/closedAccess

Özet

The magnetic polyvinylalcohol (PVAL) microspheres were prepared by crosslinking glutaraldehyde. 1,1 ' -Carbonyldiimidazole (CDI), a carbonylating agent was used for the activation of hydroxyl groups of polyvinylalcohol, and invertase immobilized onto the magnetic PVAL microspheres by covalent bonding through the amino group. The retained activity of the immobilized invertase was 74%. Kinetic parameters were determined for immobilized invertase, as well as for the free enzyme. The K-m values for immobilized invertase (55 mM sucrose) were higher than that of the free enzyme (24 mM sucrose), whereas V-max values were smaller for the immobilized invertase. The optimum operational temperature was 5 degreesC higher for immobilized enzyme than that of the free enzyme. The operational inactivation rate constant (k(opi)) of the immobilized invertase at 35 degreesC with 200 mM sucrose was 5.83 x 10(-5) min(-1). Thermal and storage stabilities were found to increase with immobilization. (C) 2001 Elsevier Science Ltd. All rights reserved.

Açıklama

Akgol, Sinan/0000-0002-8528-1854; Kacar, Yasemin/0000-0002-8682-9228; AKGOL, Sinan/0000-0003-2836-7181

Anahtar Kelimeler

polyvinylalcohol, magnetite, microspheres, covalent bonding, enzyme immobilization, invertase

Kaynak

Food Chemistry

WoS Q Değeri

Q1

Scopus Q Değeri

Q1

Cilt

74

Sayı

3

Künye

closedAccess