DC Field | Value | Language |
---|---|---|
dc.contributor.author | Park, Tae Gwan | ko |
dc.contributor.author | Hoffman, Allan S. | ko |
dc.date.accessioned | 2009-10-16T01:30:25Z | - |
dc.date.available | 2009-10-16T01:30:25Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 1990-10 | - |
dc.identifier.citation | JOURNAL OF BIOMEDICAL MATERIALS RESEARCH, v.24, no.1, pp.21 - 38 | - |
dc.identifier.issn | 0021-9304 | - |
dc.identifier.uri | http://hdl.handle.net/10203/11824 | - |
dc.description.abstract | β-Galactosidase has been immobilized within thermally reversible hydrogel beads and has been studied in batch and packed bed reactor systems. The enzyme was entrapped in a copolymer hydrogel of N-isopropylacrylamide (NIPAAm) and acrylamide (AAm) as beads were formed in an inverse suspension polymerization. The optimum temperature for maximum activity of the immobilized enzyme-gel bead system was found to be 30-35°C in a batch mode and 40°C in a packed bed reactor, which were both below the 50°C optimum for the free enzyme. It was also found that when the operational temperature in the packed bed reactor was cycled between temperatures below (35°C) and above (45°C) the copolymer gel LCST, the activity of the immobilized enzyme almost fully recovered after each cycle. | - |
dc.language | English | - |
dc.language.iso | en_US | en |
dc.publisher | JOHN WILEY & SONS INC | - |
dc.title | Immobilization and characterization of β-galactosidase in thermally reversible hydrogel beads | - |
dc.type | Article | - |
dc.type.rims | ART | - |
dc.citation.volume | 24 | - |
dc.citation.issue | 1 | - |
dc.citation.beginningpage | 21 | - |
dc.citation.endingpage | 38 | - |
dc.citation.publicationname | JOURNAL OF BIOMEDICAL MATERIALS RESEARCH | - |
dc.embargo.liftdate | 9999-12-31 | - |
dc.embargo.terms | 9999-12-31 | - |
dc.contributor.localauthor | Park, Tae Gwan | - |
dc.contributor.nonIdAuthor | Hoffman, Allan S. | - |
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