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Crosslinked enzyme aggregates in hierarchically‐ordered mesoporous silica: A simple and effective method for enzyme stabilization
Author(s) -
Kim Moon Il,
Kim Jungbae,
Lee Jinwoo,
Jia Hongfei,
Na Hyon Bin,
Youn Jong Kyu,
Kwak Ja Hun,
Dohnalkova Alice,
Grate Jay W.,
Wang Ping,
Hyeon Taeghwan,
Park Hyun Gyu,
Chang Ho Nam
Publication year - 2006
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.21107
Subject(s) - lipase , enzyme , autolysis (biology) , glutaraldehyde , chemistry , immobilized enzyme , mesoporous material , enzyme assay , adsorption , chromatography , mesoporous silica , chemical engineering , biochemistry , organic chemistry , catalysis , engineering
α‐chymotrypsin (CT) and lipase (LP) were immobilized in hierarchically‐ordered mesocellular mesoporous silica (HMMS) in a simple but effective way for the enzyme stabilization, which was achieved by the enzyme adsorption followed by glutaraldehyde (GA) crosslinking. This resulted in the formation of nanometer scale crosslinked enzyme aggregates (CLEAs) entrapped in the mesocellular pores of HMMS (37 nm), which did not leach out of HMMS through narrow mesoporous channels (13 nm). CLEA of α‐chymotrypsin (CLEA‐CT) in HMMS showed a high enzyme loading capacity and significantly increased enzyme stability. No activity decrease of CLEA‐CT was observed for 2 weeks under even rigorously shaking condition, while adsorbed CT in HMMS and free CT showed a rapid inactivation due to the enzyme leaching and presumably autolysis, respectively. With the CLEA‐CT in HMMS, however, there was no tryptic digestion observed suggesting that the CLEA‐CT is not susceptible to autolysis. Moreover, CLEA of lipase (CLEA‐LP) in HMMS retained 30% specific activity of free lipase with greatly enhanced stability. This work demonstrates that HMMS can be efficiently employed as host materials for enzyme immobilization leading to highly enhanced stability of the immobilized enzymes with high enzyme loading and activity. Biotechnol. Bioeng. 2007;96: 210–218. © 2006 Wiley Periodicals, Inc.