Abstract:
:Catalase was covalently immobilized onto florisil via glutaraldehyde (GA) and glutaraldehyde+6-amino hexanoic acid (6-AHA) (as a spacer arm). Immobilizations of catalase onto modified supports were optimized to improve the efficiency of the overall immobilization procedures. The V(max) values of catalase immobilized via glutaraldehyde (CIG) and catalase immobilized via glutaraldehyde+6-amino hexanoic acid (CIG-6-AHA) were about 0.6 and 3.4% of free catalase, respectively. The usage of 6-AHA as a spacer arm caused about 40 folds increase in catalytic efficiency of CIG-6-AHA (8.3 × 10⁵ M⁻¹ s⁻¹) as compared to that of CIG (2.1 × 10⁴ M⁻¹ s⁻¹). CIG and CIG-6-AHA retained 67 and 35% of their initial activities at 5 °C and 71 and 18% of their initial activities, respectively at room temperature at the end of 6 days. Operational stabilities of CIG and CIG-6-AHA were investigated in batch and plug-flow type reactors. The highest total amount of decomposed hydrogen peroxide (TAD-H₂O₂) was determined as 219.5 μmol for CIG-6-AHA in plug-flow type reactor.
journal_name
Enzyme Microb Technoljournal_title
Enzyme and microbial technologyauthors
Alptekin O,Tükel SS,Yildirim D,Alagöz Ddoi
10.1016/j.enzmictec.2011.09.002subject
Has Abstractpub_date
2011-12-10 00:00:00pages
547-54issue
6-7eissn
0141-0229issn
1879-0909pii
S0141-0229(11)00191-8journal_volume
49pub_type
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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