Carbon coated monoliths as support material for a lactase from Aspergillus oryzae:: Characterization and design of the carbon carriers

被引:20
作者
de Lathouder, K. M.
Lozano-Castello, D.
Linares-Solano, A.
Kapteijn, F.
Moulijn, J. A.
机构
[1] Delft Univ Technol, Fac Sci Appl, DelftChemTech, NL-2628 BL Delft, Netherlands
[2] Univ Alicante, Dept Inorgan Chem, E-03080 Alicante, Spain
关键词
carbon fibers; catalyst support; chemical treatment; adsorption; surface oxygen complexes;
D O I
10.1016/j.carbon.2006.05.009
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Tunable carbon-coated monoliths as carriers for enzyme adsorption are presented. Depending on enzyme properties and reaction conditions, the carrier can be adjusted to optimize enzyme loading. Carbon-ceramic composites were prepared by sucrose carbonization, polyfurfuryl alcohol (PFA) carbonization, and by growth of carbon nanofibers (CNFs) over deposited Ni. All carbons were treated in air and subsequently in 1 M HNO3, and analyzed with respect to porosity, morphology and surface chemistry. The composites were applied as a carrier for a lactase from Aspergillus oryzae. The CNFs proved to be the best carrier, with respect to enzyme loading. Untreated fibers could adsorb 115 mg lactase/g carbon. After air/HNO3 treatment this value increased to 360 mg/g. Porosity was not affected by air and air/HNO3 treatment, implying that lactase adsorption mainly depends on surface chemistry. A clear trend was observed between oxygen content of,different CNFs and lactase adsorption. Ni could be removed completely from the fiber tips of CNFs by different concentrated acids-nitric acid, hydrochloric acid, and oxalic acid. However, with HCl and HNO3 the porosity and surface chemistry were affected. Treatment in oxalic acid removed Ni from the tips by complexation, without changing the porosity. For these samples, 30% of the Ni remained present in the sample as residual NiC2O4. This was confirmed by TGA-MS and XRD. (c) 2006 Elsevier Ltd. All rights reserved.
引用
收藏
页码:3053 / 3063
页数:11
相关论文
共 37 条
[1]   Determination of the effective diffusion coefficient of phenol in Ca-alginate-immobilized P-putida beads [J].
Aksu, Z ;
Bülbül, G .
ENZYME AND MICROBIAL TECHNOLOGY, 1999, 25 (3-5) :344-348
[2]  
Barros RJ, 1998, BIOTECHNOL BIOENG, V59, P364
[3]   Mesoporous alginate/silica biocomposites for enzyme immobilisation [J].
Coradin, T ;
Livage, J .
COMPTES RENDUS CHIMIE, 2003, 6 (01) :147-152
[4]   Impact of surface characteristics of activated carbon on adsorption of BTEX [J].
Daifullah, AAM ;
Girgis, BS .
COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS, 2003, 214 (1-3) :181-193
[5]   Carbon nanofibers: Catalytic synthesis and applications [J].
De Jong, KP ;
Geus, JW .
CATALYSIS REVIEWS-SCIENCE AND ENGINEERING, 2000, 42 (04) :481-510
[6]   A novel structured bioreactor:: Development of a monolithic stirrer reactor with immobilized lipase [J].
de Lathouder, KM ;
Fló, TM ;
Kapteijn, E ;
Moulijn, JA .
CATALYSIS TODAY, 2005, 105 (3-4) :443-447
[7]   Structured reactors for enzyme immobilization: advantages of tuning the wall morphology [J].
de Lathouder, KM ;
Bakker, J ;
Kreutzer, MT ;
Kapteijn, F ;
Moulijn, JA ;
Wallin, SA .
CHEMICAL ENGINEERING SCIENCE, 2004, 59 (22-23) :5027-5033
[8]   Lactose hydrolysis by immobilized β-galactosidase:: the effect of the supports and the kinetics [J].
Di Serio, M ;
Maturo, C ;
De Alteriis, E ;
Parascandola, P ;
Tesser, R ;
Santacesaria, E .
CATALYSIS TODAY, 2003, 79 (1-4) :333-339
[9]   Enzyme immobilization in MCM-41 molecular sieve [J].
Diaz, JF ;
Balkus, KJ .
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 1996, 2 (2-3) :115-126
[10]   Preparation and properties of lipase immobilized on MCM-36 support [J].
Dumitriu, E ;
Secundo, F ;
Patarin, J ;
Fechete, L .
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 2003, 22 (3-4) :119-133