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DC Field | Value | Language |
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dc.citation.endPage | 1187 | - |
dc.citation.number | 8 | - |
dc.citation.startPage | 1181 | - |
dc.citation.title | PROCESS BIOCHEMISTRY | - |
dc.citation.volume | 48 | - |
dc.contributor.author | Jun, Chanha | - |
dc.contributor.author | Jeon, Byoung Wook | - |
dc.contributor.author | Joo, Jeong Chan | - |
dc.contributor.author | Quang Anh Tuan Le | - |
dc.contributor.author | Gu, Sol-A. | - |
dc.contributor.author | Byun, Sungmin | - |
dc.contributor.author | Cho, Dae Haeng | - |
dc.contributor.author | Kim, Dukki | - |
dc.contributor.author | Sang, Byoung-In | - |
dc.contributor.author | Kim, Yong Hwan | - |
dc.date.accessioned | 2023-12-22T03:39:10Z | - |
dc.date.available | 2023-12-22T03:39:10Z | - |
dc.date.created | 2016-09-06 | - |
dc.date.issued | 2013-08 | - |
dc.description.abstract | A large improvement in the thermostability of Candida antarctica lipase B (CALB) was achieved through double immobilization, i.e., physical adsorption and R1 silaffin-mediated biosilicification. The C-terminus of CALB was fused with the R1 silaffin peptide for biosilicification. The CALB-R1 fusion protein was adsorbed onto a macroporous polyacrylate carrier and then subsequently biosilicified with tetramethyl orthosilicate (TMOS). After R1 silaffin-mediated biosilicification, the double-immobilized CALB-R1 exhibited remarkable thermostability. The T-50(60) of the double-immobilized CALB-R1 increased dramatically from 45 to 72 degrees C and that was 27, 13.8, 9.8 and 9.9 degrees C higher than the T-50(60) values of free CALB-R1, CALB-R1 adsorbed onto a resin, commercial Novozym 435, and Novozym 435 treated with TMOS, respectively. In addition, the time required for the residual activity to be reduced to half (t(1/2)) of the double immobilized CALB-R1 elevated from 12.2 to 385 min, which is over 30 times longer life time compared free CALB-R1. The optimum pH for biosilicification was determined to be 5.0, and the double-immobilized enzyme showed much better reusability than the physically adsorbed enzyme even after 6 repeated reuses. This R1-mediated biosilicification approach for CALB thermostabilization is a good basis for the thermostabilization of industrial enzymes that are only minimally stabilized by protein engineering. | - |
dc.identifier.bibliographicCitation | PROCESS BIOCHEMISTRY, v.48, no.8, pp.1181 - 1187 | - |
dc.identifier.doi | 10.1016/j.procbio.2013.06.010 | - |
dc.identifier.issn | 1359-5113 | - |
dc.identifier.scopusid | 2-s2.0-84881132106 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/20355 | - |
dc.identifier.url | http://www.sciencedirect.com/science/article/pii/S1359511313002808 | - |
dc.identifier.wosid | 000323690700009 | - |
dc.language | 영어 | - |
dc.publisher | ELSEVIER SCI LTD | - |
dc.title | Thermostabilization of Candida antarctica lipase B by double immobilization:. Adsorption on a macroporous polyacrylate carrier and R1 silaffin-mediated biosilicification | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | Candida antarctica lipase B | - |
dc.subject.keywordAuthor | Silaffin | - |
dc.subject.keywordAuthor | R1 peptide | - |
dc.subject.keywordAuthor | Biosilicification | - |
dc.subject.keywordAuthor | Immobilization | - |
dc.subject.keywordAuthor | Thermostability | - |
dc.subject.keywordPlus | BACILLUS-CIRCULANS XYLANASE | - |
dc.subject.keywordPlus | DIRECTED EVOLUTION | - |
dc.subject.keywordPlus | SILICA PARTICLES | - |
dc.subject.keywordPlus | PICHIA-PASTORIS | - |
dc.subject.keywordPlus | ENZYME-ACTIVITY | - |
dc.subject.keywordPlus | ENCAPSULATION | - |
dc.subject.keywordPlus | STABILITY | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | DESIGN | - |
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