Journal
KOREAN JOURNAL OF CHEMICAL ENGINEERING
Volume 28, Issue 3, Pages 853-859Publisher
KOREAN INSTITUTE CHEMICAL ENGINEERS
DOI: 10.1007/s11814-010-0412-3
Keywords
Immobilized Trypsin; Covalent Modification; Crowding Environment; Accessible Transmission
Funding
- National High Technology Research and Development Program of China (863 Program) [2009AA05Z313, 2006AA02Z211]
- National Natural Science Foundation of China [50872052, 20376034]
- Natural Science Foundation of Jiangsu Province of China [BK2006181]
- Foundation of Jiangsu Province of China for College Postgraduate Students in Innovation Engineering
- Foundation of Nanjing University of technology of China for College Postgraduate Students in Innovation Engineering [BSCX200910]
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Chemically modified macromolecules were assembled with adsorptive trypsin in mesoporous silica foams (MCFs) to establish covalent linkage. Effects of catalytic properties and stability of immobilized trypsin were examined. The addition of chemically modified protein (BSA) and polysaccharide (ficoll) to the immobilized trypsin exhibited high coupled yield (above 90%) and relative activities (174.5% and 175.9%, respectively), showing no protein leaching after incubating for 10 h in buffers. They showed broader pH and temperature profiles, while the half life of thermal stability of BSA-modified preparation at 50 degrees C increased to 1.3 and 2.3 times of unmodified and free trypsin, respectively. The modified trypsin in aqueous-organic solvents exhibited 100% activity after 6 h at 50 C. The kinetic parameters of trypsin preparations and suitable pore diameter of MCFs warranted compatibility of covalent modification for substrate transmission. The covalent crowding modification for immobilized trypsin in nanopores establishes suitable and accessible microenvironment and renders possibility of biological application.
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