Characterization and properties of catalase immobilized onto controlled pore glass and its applicati.pdf
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Characterization and properties of catalase immobilized onto controlled pore glass and its applicati
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dJournal of Molecular Catalysis B: Enzymatic 58 (2009) 124–131
Contents lists available at ScienceDirect
Journal of Molecular Catalysis B: Enzymatic
journa l homepage: www.e lsev ier .com/ locate /molcatb
haracterization and properties of catalase immobilized onto controlled pore
lass and its application in batch and plug-flow type reactors
zlem Alptekin ?, S. Seyhan Tükel, Deniz Y?ld?r?m, Dilek Alag?z
niversity of Cukurova, Faculty of Arts Sciences, Department of Chemistry, 01330 Adana, Turkey
r t i c l e i n f o
rticle history:
eceived 18 July 2008
eceived in revised form
3 November 2008
ccepted 9 December 2008
vailable online 24 December 2008
a b s t r a c t
Bovine liver catalase was covalently immobilized onto controlled pore glass (CPG) beads modified with
3-aminopropyltriethoxysilane (3-APTES) followed by treatment with glutaraldehyde. Coupling of cata-
lase onto CPG was optimized to improve the efficiency of the overall immobilization procedure. The
optimum coupling conditions: pore diameter of CPG, pH, buffer concentration, temperature, coupling
time and initial catalase amount per grams of carrier were determined as 70nm, 6.0, 75mM, 5 ?C, 7heywords:
atalase
ontrolled pore glass
ovalent immobilization
and 6mg catalase, respectively. Catalytic efficiencies (kcat/Km) and thermal inactivation rate constants
(ki) of ICPG1 were determined and compared with that of free catalase. Suitability of ICPG1 was also
investigated by using it in batch and plug-flow type reactors. When the remaining activity of ICPG1
retained was about 50% of its initial activity the highest total productivity of ICPG1 was determined as
7.6×106 Ug immobilized catalase?1 in plug-flow type reactor. However, the highest total productivity of
5 mob ?1
tion
eactors
roductivity
ICPG1 was 6.2×10 Ug im
biocatalyst for the applica
. Introduction
Catalases (H2O2:H2O2 oxidoreductase; EC ) are abundant
nzymes in nature that decompose hydr
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