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Taking Advantage of Promiscuity of Cold-Active Enzymes

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Cited 1 time in scopus
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dc.contributor.authorNandanwar, Sondavid K.-
dc.contributor.authorBorkar, Shweta Bharat-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorKim, Hak Jun-
dc.date.accessioned2021-05-04T06:00:50Z-
dc.date.available2021-05-04T06:00:50Z-
dc.date.issued2020-11-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/11817-
dc.description.abstractCold-active enzymes increase their catalytic efficiency at low-temperature, introducing structural flexibility at or near the active sites. Inevitably, this feat seems to be accompanied by lower thermal stability. These characteristics have made cold-active enzymes into attractive targets for the industrial applications, since they could reduce the energy cost in the reaction, attenuate side-reactions, and simply be inactivated. In addition, the increased structural flexibility could result in broad substrate specificity for various non-native substrates, which is called substrate promiscuity. In this perspective, we deal with a less addressed aspect of cold-active enzymes, substrate promiscuity, which has enormous potential for semi-synthesis or enzymatic modification of fine chemicals and drugs. Further structural and directed-evolutional studies on substrate promiscuity of cold-active enzymes will provide a new workhorse in white biotechnology.en_US
dc.languageEnglishen_US
dc.language.isoen_USen_US
dc.subjectChemistryen_US
dc.subjectEngineeringen_US
dc.subjectMaterials Scienceen_US
dc.subjectPhysicsen_US
dc.subject.classificationDasan Stationen_US
dc.titleTaking Advantage of Promiscuity of Cold-Active Enzymesen_US
dc.title.alternative생명공학적 활용에서의 장점을 가지는 저온성 효소의 특성인 기질 유연성en_US
dc.typeArticleen_US
dc.identifier.bibliographicCitationNandanwar, Sondavid K., et al. 2020. "Taking Advantage of Promiscuity of Cold-Active Enzymes". <em>APPLIED SCIENCES-BASEL</em>, 10(22): 8128-8145.en_US
dc.citation.titleAPPLIED SCIENCES-BASELen_US
dc.citation.volume10en_US
dc.citation.number22en_US
dc.identifier.doi10.3390/app10228128-
dc.citation.startPage8128en_US
dc.citation.endPage8145en_US
dc.description.articleClassificationSCIE-
dc.description.jcrRateJCR 2018:45.27en_US
dc.subject.keywordcold-active enzymeen_US
dc.subject.keywordcatalytic efficiencyen_US
dc.subject.keywordbroad substrate specificityen_US
dc.subject.keywordsubstrate promiscuityen_US
dc.subject.keywordpsychrophileen_US
dc.identifier.localId2020-0192-
dc.identifier.scopusid2-s2.0-85096113550-
dc.identifier.wosid000594218100001-
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