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김용환

Kim, Yong Hwan
Enzyme and Protein Engineering Lab.
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dc.citation.endPage 178 -
dc.citation.startPage 170 -
dc.citation.title JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC -
dc.citation.volume 122 -
dc.contributor.author Kim, Hyun Jung -
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 Kan, Eunsung -
dc.contributor.author Kim, Yong Hwan -
dc.contributor.author Lee, Sang Hyun -
dc.date.accessioned 2025-06-30T09:30:04Z -
dc.date.available 2025-06-30T09:30:04Z -
dc.date.created 2025-06-29 -
dc.date.issued 2015-12 -
dc.description.abstract Cellulose nanocrystals (CNCs) are rod-like cellulose nanomaterials that can be economically prepared from various cellulosic materials by the elimination of amorphous regions of cellulose. CNCs can be used as supports to immobilize enzymes because of their inherent biocompatibility, high specific-surface area, and exceptional mechanical properties. In this study, CNCs obtained from cotton linter cellulose (CLC) and bacterial cellulose (BC) were used as supports to immobilize Candida nigosa lipase. The protein loading and immobilization yield of the lipase immobilized onto the CNC obtained from CLC (CNC CLC) were 1.8 and 2.2 times higher, respectively, than those of the lipase immobilized onto CLC. The lipase immobilized onto CNC CLC showed significantly enhanced thermal stability. The half-life time of the immobilized lipase during incubation at 60 degrees C was 27 times higher than that of free lipase. The lipase immobilized onto CNC CLC also showed increased pH stability at an alkaline pH. The residual activity of the immobilized lipase after 5 h incubation at pH 10 was 8.8 times higher than that of free lipase. In addition, the lipase immobilized onto CNC CLC was able to perform homogeneous-like biocatalysis without shaking or agitation because the immobilized lipase remained well-dispersed during the aqueous reaction. The CNCs as enzyme supports have many potential applications in the biomedical, bioelectronic, and biocatalytic fields. (C) 2015 Elsevier B.V. All rights reserved. -
dc.identifier.bibliographicCitation JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, v.122, pp.170 - 178 -
dc.identifier.doi 10.1016/j.molcatb.2015.09.007 -
dc.identifier.issn 1381-1177 -
dc.identifier.scopusid 2-s2.0-84942909507 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/87256 -
dc.identifier.wosid 000366078800021 -
dc.language 영어 -
dc.publisher ELSEVIER SCIENCE BV -
dc.title Biocompatible cellulose nanocrystals as supports to immobilize lipase -
dc.type Article -
dc.description.isOpenAccess FALSE -
dc.type.docType Article -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -

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