Covalent immobilization of catalase onto spacer-arm attached modified florisil: Characterization and application to batch and plug-flow type reactor systems


ALPTEKİN Ö., TÜKEL S. S. , YILDIRIM D., ALAGÖZ D.

ENZYME AND MICROBIAL TECHNOLOGY, vol.49, pp.547-554, 2011 (Peer-Reviewed Journal) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 49
  • Publication Date: 2011
  • Doi Number: 10.1016/j.enzmictec.2011.09.002
  • Journal Name: ENZYME AND MICROBIAL TECHNOLOGY
  • Journal Indexes: Science Citation Index Expanded, Scopus
  • Page Numbers: pp.547-554
  • Keywords: Catalase, Covalent immobilization, Reactors, Spacer-arm, ENZYME IMMOBILIZATION, LIVER CATALASE, OXIDASE, ACID, GEL, COIMMOBILIZATION, BIOCATALYST, SURFACE, PHENOL

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 x 10(5) M-1 s(-1)) as compared to that of CIG (2.1 x 10(4) M-1 s(-1)). CIG and CIG-6-AHA retained 67 and 35% of their initial activities at 5 degrees 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 mu mol for CIG-6-AHA in plug-flow type reactor. (C) 2011 Elsevier Inc. All rights reserved.