Structural and functional characterization of a thermostable secretory phospholipase A2 from Sciscionella marina and its application in liposome
biotransformation
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Title
- Structural and functional characterization of a thermostable secretory phospholipase A2 from Sciscionella marina and its application in liposome
biotransformation
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Author(s)
- Kang, Bu-Gyeong; Kwon, Seung-Yeon; Lee, Hyo-Ran; Hwang, Yeji; Youn, So-Yeon; Oh, Chul Hong; Park, Jin-Byung; Cha, Sun-Shin
- KIOST Author(s)
- Oh, Chul Hong(오철홍)
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Alternative Author(s)
- 오철홍
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Publication Year
- 2023-02
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Abstract
- Secretory phospholipase A2 (sPLA2), which hydrolyzes the sn-2 acyl bond of lecithin in a Ca2+-dependent manner, is an important enzyme in the oil and oleochemical industries. However, most sPLA2s are not stable under process conditions. Therefore, a thermostable sPLA2 was investigated in this study. A marine bacterial sPLA2 isolated from Sciscionella marina (Sm-sPLA2) was catalytically active even after 5 h of incubation at high temperatures of up to 50°C, which is outstanding compared with a representative bacterial sPLA2 (i.e. sPLA2 from Streptomyces violaceoruber; Sv-sPLA2). Consistent with this, the melting temperature of Sm-sPLA2 was measured to be 7.7°C higher than that of Sv-sPLA2. Furthermore, Sm-sPLA2 exhibited an improved biotransformation performance compared with Sv-sPLA2 in the hydrolysis of soy lecithin to lysolecithin and free fatty acids at 50°C. Structural and mutagenesis studies revealed that the Trp41-mediated anchoring of a Ca2+-binding loop into the rest of the protein body is directly linked to the thermal stability of Sm-sPLA2. This finding provides a novel structural insight into the thermostability of sPLA2 and could be applied to create mutant proteins with enhanced industrial potential.
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ISSN
- 2059-7983
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URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/43917
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DOI
- 10.1107/S2059798323000384
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Bibliographic Citation
- Acta Crystallographica Section D-structural Biology, v.D79, pp.188 - 197, 2023
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Publisher
- INT UNION CRYSTALLOGRAPHY
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Keywords
- phospholipase A2; Sciscionella marina; thermostability; crystal structure; loop anchoring; liposome biotransformation.
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Type
- Article
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Language
- English
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Document Type
- Article
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