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김용환

Kim, Yong Hwan
Enzyme and Protein Engineering Lab.
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dc.citation.endPage 39 -
dc.citation.startPage 33 -
dc.citation.title JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC -
dc.citation.volume 119 -
dc.contributor.author Park, Saerom -
dc.contributor.author Kim, Sung Hee -
dc.contributor.author Kim, Ji Hyun -
dc.contributor.author Yu, Hyejeong -
dc.contributor.author Kim, Hyung Joo -
dc.contributor.author Yang, Yung-Hun -
dc.contributor.author Kim, Hyungsup -
dc.contributor.author Kim, Yong Hwan -
dc.contributor.author Ha, Sung Ho -
dc.contributor.author Lee, Sang Hyun -
dc.date.accessioned 2023-12-22T00:42:59Z -
dc.date.available 2023-12-22T00:42:59Z -
dc.date.created 2016-09-06 -
dc.date.issued 2015-09 -
dc.description.abstract Lignocellulose-based hydrogels may have many potential applications in biomedical and biotechnological fields owing to their attractive properties including low cost, biodegradability, and biocompatibility. In this study, cellulose/lignin composite hydrogel beads were prepared by co-dissolution of cellulose and lignin in 1-ethyl-3-methylimidazolium acetate and then reconstitution with distilled water. Lipase from Candida rugosa was immobilized on various cellulose/lignin hydrogel beads. The results showed that lipase immobilized on cellulose/lignin beads showed higher activity and stability than those of lipase immobilized on pure cellulose beads. The activity and stability of immobilized lipase increased with the increase in the lignin content in the cellulose/lignin beads. The activity, protein loading, and specific activity of lipase immobilized on the optimal cellulose/lignin beads were 2.6, 2.2, and 1.2 times higher than those of lipase immobilized on cellulose beads, respectively. The effect of lignin on the activity of lipase immobilized on cellulose/lignin beads was statistically well predicted. The residual activity of lipase immobilized on the optimal cellulose/lignin beads after incubation for 12 h at 40 degrees C was 3.2 and 1.9 times higher than that of free lipase and lipase immobilized on cellulose beads, respectively. Interestingly, the half-life time of lipase immobilized on cellulose/lignin beads at pH 3.0 was 24 and 3 times higher than that of free lipase and that of lipase immobilized on cellulose beads, respectively. These results show that cellulose/lignin hydrogels may offer many potential applications in the biocatalytic, biomedical, and bioelectronic fields owing to their high biocompatibility, biodegradability, and controllable properties. -
dc.identifier.bibliographicCitation JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, v.119, pp.33 - 39 -
dc.identifier.doi 10.1016/j.molcatb.2015.05.014 -
dc.identifier.issn 1381-1177 -
dc.identifier.scopusid 2-s2.0-84934950440 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/20326 -
dc.identifier.url http://www.sciencedirect.com/science/article/pii/S1381117715300047 -
dc.identifier.wosid 000359027000005 -
dc.language 영어 -
dc.publisher ELSEVIER SCIENCE BV -
dc.title Application of cellulose/lignin hydrogel beads as novel supports for immobilizing lipase -
dc.type Article -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordAuthor Cellulose -
dc.subject.keywordAuthor Lignin -
dc.subject.keywordAuthor Ionic liquid -
dc.subject.keywordAuthor Lipase -
dc.subject.keywordAuthor Immobilization -
dc.subject.keywordPlus IONIC LIQUID SOLUTION -
dc.subject.keywordPlus ENZYME IMMOBILIZATION -
dc.subject.keywordPlus SYNTHETIC WOOD -
dc.subject.keywordPlus LIGNIN -
dc.subject.keywordPlus ENTRAPMENT -
dc.subject.keywordPlus LIGNOCELLULOSE -
dc.subject.keywordPlus MICROSPHERES -
dc.subject.keywordPlus SPECTROSCOPY -
dc.subject.keywordPlus HYDROLYSIS -
dc.subject.keywordPlus ADSORPTION -

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