PMID- 22142730 OWN - NLM STAT- MEDLINE DCOM- 20120417 LR - 20141120 IS - 1879-0909 (Electronic) IS - 0141-0229 (Linking) VI - 49 IP - 6-7 DP - 2011 Dec 10 TI - Covalent immobilization of catalase onto spacer-arm attached modified florisil: characterization and application to batch and plug-flow type reactor systems. PG - 547-54 LID - 10.1016/j.enzmictec.2011.09.002 [doi] AB - 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-H(2)O(2)) was determined as 219.5 mumol for CIG-6-AHA in plug-flow type reactor. CI - Copyright (c) 2011 Elsevier Inc. All rights reserved. FAU - Alptekin, Ozlem AU - Alptekin O AD - Department of Chemistry, Faculty of Arts & Sciences, University of Cukurova, 01330 Adana, Turkey. FAU - Tukel, S Seyhan AU - Tukel SS FAU - Yildirim, Deniz AU - Yildirim D FAU - Alagoz, Dilek AU - Alagoz D LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't DEP - 20110921 PL - United States TA - Enzyme Microb Technol JT - Enzyme and microbial technology JID - 8003761 RN - 0 (Enzymes, Immobilized) RN - 0 (Magnesium Silicates) RN - 1343-88-0 (Florisil) RN - EC 1.11.1.6 (Catalase) RN - T3C89M417N (Glutaral) RN - U6F3787206 (Aminocaproic Acid) SB - IM MH - Aminocaproic Acid/chemistry MH - Animals MH - *Bioreactors MH - *Catalase/metabolism MH - Cattle MH - Enzyme Stability MH - *Enzymes, Immobilized/metabolism MH - Glutaral/chemistry MH - In Vitro Techniques MH - Kinetics MH - Magnesium Silicates/chemistry MH - Microscopy, Electron, Scanning MH - Surface Properties EDAT- 2011/12/07 06:00 MHDA- 2012/04/18 06:00 CRDT- 2011/12/07 06:00 PHST- 2011/01/13 00:00 [received] PHST- 2011/07/29 00:00 [revised] PHST- 2011/09/09 00:00 [accepted] PHST- 2011/12/07 06:00 [entrez] PHST- 2011/12/07 06:00 [pubmed] PHST- 2012/04/18 06:00 [medline] AID - S0141-0229(11)00191-8 [pii] AID - 10.1016/j.enzmictec.2011.09.002 [doi] PST - ppublish SO - Enzyme Microb Technol. 2011 Dec 10;49(6-7):547-54. doi: 10.1016/j.enzmictec.2011.09.002. Epub 2011 Sep 21.