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| Type |
Poster Presentation |
| Area |
생명화학 |
| Room No. |
포스터발표장 |
| Time |
4월 21일 (금요일) 13:00~14:30 |
| Code |
BIO.P-307 |
| Subject |
Characterization and mutational analysis of a cold-adapted bacterial lipase, SaHSL from Salinisphaera sp. P7-4 [TCI 포스터상] |
| Authors |
유완기, 김부영1, 김두헌2,*
성균관대학교 의과대학, Korea
1숙명여자대학교 화학과, Korea
2숙명여자대학교 이과대학 화학과, Korea
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| Abstract |
Hormone sensitive lipase (HSL) contributes energy metabolism and fatty acid signaling in various tissues. Functional and structural properties of HSL from human have been studied in detail, however, lipase homologues from bacteria are still largely unknown. Previously, a new cold-adapted bacterial lipase, SaHSL was identified and purified. Here, biochemical and biophysical studies of SaHSL were reported. Primary structure analysis of SaHSL revealed that SaHSL was different from human HSL, especially in N terminal region and regulatory domain. Here, SaHSL were investigated with fluorescence analysis, dynamic light scattering (DLS), electron microscopy, and time of flight (TOF) mass spectrometry. Studies of site-directed mutants in regulatory region suggested that the region are critical for structural stability as well as for substrate specificity. Improvement of chemical, thermal resistance and good durability of immobilized SaHSL proposed the potential as a biocatalyst in industries. |
| E-mail |
vlqkshqk61@outlook.kr |
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119th General Meeting of the KCS