Bacterial Hormone-Sensitive Lipases (bHSLs): Emerging Enzymes for Biotechnological Applications
DC Field | Value | Language |
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dc.contributor.author | Kim, T. Doohun | - |
dc.date.available | 2021-02-22T10:46:42Z | - |
dc.date.issued | 2017-11 | - |
dc.identifier.issn | 1017-7825 | - |
dc.identifier.issn | 1738-8872 | - |
dc.identifier.uri | https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/5086 | - |
dc.description.abstract | Lipases are important enzymes with biotechnological applications in dairy, detergent, food, fine chemicals, and pharmaceutical industries. Specifically, hormone-sensitive lipase (HSL) is an intracellular lipase that can be stimulated by several hormones, such as catecholamine, glucagon, and adrenocorticotropic hormone. Bacterial hormone-sensitive lipases (bHSLs), which are homologous to the C-terminal domain of HSL, have alpha/beta-hydrolase fold with a catalytic triad composed of His, Asp, and Ser. These bHSLs could be used for a wide variety of industrial applications because of their high activity, broad substrate specificity, and remarkable stability. In this review, the relationships among HSLs, the microbiological origins, the crystal structures, and the biotechnological properties of bHSLs are summarized. | - |
dc.format.extent | 9 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | 한국미생물·생명공학회 | - |
dc.title | Bacterial Hormone-Sensitive Lipases (bHSLs): Emerging Enzymes for Biotechnological Applications | - |
dc.type | Article | - |
dc.publisher.location | 대한민국 | - |
dc.identifier.doi | 10.4014/jmb.1708.08004 | - |
dc.identifier.scopusid | 2-s2.0-85035099319 | - |
dc.identifier.wosid | 000416681000002 | - |
dc.identifier.bibliographicCitation | Journal of Microbiology and Biotechnology, v.27, no.11, pp 1907 - 1915 | - |
dc.citation.title | Journal of Microbiology and Biotechnology | - |
dc.citation.volume | 27 | - |
dc.citation.number | 11 | - |
dc.citation.startPage | 1907 | - |
dc.citation.endPage | 1915 | - |
dc.type.docType | Review | - |
dc.identifier.kciid | ART002284715 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |
dc.relation.journalResearchArea | Microbiology | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.relation.journalWebOfScienceCategory | Microbiology | - |
dc.subject.keywordPlus | MYCOBACTERIUM-TUBERCULOSIS H37RV | - |
dc.subject.keywordPlus | OIL-DEGRADING BACTERIUM | - |
dc.subject.keywordPlus | PSYCHROBACTER SP TA144 | - |
dc.subject.keywordPlus | ALICYCLOBACILLUS-ACIDOCALDARIUS | - |
dc.subject.keywordPlus | SEQUENCE SIMILARITY | - |
dc.subject.keywordPlus | THERMOPHILIC ESTERASE | - |
dc.subject.keywordPlus | THERMOSTABLE ESTERASE | - |
dc.subject.keywordPlus | METAGENOMIC LIBRARY | - |
dc.subject.keywordPlus | KINETIC RESOLUTION | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordAuthor | Hormone-sensitive lipase | - |
dc.subject.keywordAuthor | cap domain | - |
dc.subject.keywordAuthor | promiscuity | - |
dc.subject.keywordAuthor | substrate specificities | - |
dc.subject.keywordAuthor | industrial applications | - |
dc.identifier.url | http://www.jmb.or.kr/journal/view.html?doi=10.4014/jmb.1708.08004 | - |
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