One-dimensional crosslinked enzyme aggregates in SBA-15: Superior catalytic behavior to conventional enzyme immobilization

• Published in: Microporous and mesoporous materials Vol. 111; no. 1; pp. 18 - 23
• Main Authors: Kim, Moon Il, Kim, Jungbae, Lee, Jinwoo, Shin, Sujeong, Na, Hyon Bin, Hyeon, Taeghwan, Park, Hyun Gyu, Chang, Ho Nam
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier Inc 15.04.2008; Elsevier
• Subjects: ADSORPTION; ASPECT RATIO; BASIC BIOLOGICAL SCIENCES; Biological and medical sciences; CAPACITY; Catalysis; Chemistry; CLEAs (crosslinked enzyme aggregates); Colloidal state and disperse state; Environmental Molecular Sciences Laboratory; Enzyme immobilization; ENZYMES; Exact sciences and technology; Fundamental and applied biological sciences. Psychology; GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; General and physical chemistry; INACTIVATION; LEACHING; LIPASES; Mechanisms. Catalysis. Electron transfer. Models; Molecular biophysics; Mucor javanicus lipase; Physical chemistry in biology; PORE STRUCTURE; Porous materials; SBA-15; SILICA; STABILITY; STABILIZATION; Theory of reactions, general kinetics. Catalysis. Nomenclature, chemical documentation, computer chemistry; α-Chymotrypsin; α-Chymotrypsin; Enzyme immobilization; SBA-15; Mucor javanicus lipase; CLEAs (crosslinked enzyme aggregates); Catalytic reaction; Enzyme; Immobilization; Enzymatic catalysis; Porous material; Mesoporosity; Heterogeneous catalysis; Aggregate
• ISSN: 1387-1811; 1873-3093
• DOI: 10.1016/j.micromeso.2007.07.009

α-Chymotrypsin (CT) and lipase (LP) were immobilized in SBA-15 mesoporous silica by crosslinking adsorbed enzymes. This simple approach resulted in one-dimensional crosslinked enzyme aggregates (CLEAs) in the linear pore channels of SBA-15, which was very effective in preventing the enzyme leaching and consequently improving the enzyme stability. Both CLEAs of CT and LP showed negligible activity decrease under harsh shaking condition for one week while the conventional approaches including adsorption and covalent attachment resulted in more than 50–90% enzyme inactivation under the same condition. This effective stabilization results from the bent pore structure of SBA-15 with a high aspect ratio, which prevents the leaching of one-dimensional CLEAs and thereby achieves the higher enzyme loading capacity. Along with the higher specific activity than that of adsorbed enzymes, this CLEA approach is much simpler than that of covalent attachment by obviating the tedious processes for silica functionalization and enzyme attachment.