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http://dx.doi.org/10.7852/ijie.2013.27.2.329

Activity and Stability of Immobilized Enzyme on Silk Sericin Bead  

Oh, Hanjin (National Instrumentation Center for Environmental Management, Seoul National University)
Lee, Ki Hoon (Department of Biosystems & Biomaterials Science and Engineering, Seoul National University)
Publication Information
International Journal of Industrial Entomology and Biomaterials / v.27, no.2, 2013 , pp. 329-332 More about this Journal
Abstract
In present preliminary report, we showed the possibility of silk sericin (SS) in enzyme immobilization. SS beads were prepared and enzymes were immobilized on it. The specific activity of immobilized a-chymotrypsin retained more than 87% compared to the free enzyme. The immobilized a-chymotrypsin has better stability against ethanol especially those immobilized on SS beads coagulated in methanol. Immobilized trypsin and lipase had also comparable apparent activity compared to free enzyme. Our result indicates that SS could be a good candidate for enzyme immobilization support due to its hydrophilicity.
Keywords
Silk Sericn; Enzyme Immobilization; Hydrophilicity;
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Times Cited By KSCI : 2  (Citation Analysis)
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