| アイテムタイプ |
共通アイテムタイプ(1) |
| 公開日 |
2025-02-27 |
| タイトル |
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タイトル |
Investigation of the Contribution of Late Embryogenesis Abundant (LEA) K Peptide in Enhancing the Expression of Lipase from Sphingobacterium sp.: In vitro and in Silico Studies |
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言語 |
en |
| その他のタイトル |
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その他のタイトル |
Investigation of the Contribution of Late Embryogenesis Abundant (LEA) K Peptide in Enhancing the Expression of Lipase from #ISphingobacterium#IR sp.: #IIn vitrao#IR and #Iin Silico#IR Studies |
|
言語 |
en |
| 著者 |
Ibrahim Muhammad,
Ng, Siau Ning
Nurul Izza Ismail,
Arsad, Hasni
池野, 慎也
Rahim, Rashidah Abdul
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| 著作権関連情報 |
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権利情報Resource |
https://creativecommons.org/licenses/by/4.0/ |
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権利情報 |
Copyright (c) 2024 Ibrahim Muhammad, Ng Siau Ning, Nurul Izza Ismail, Hasni Arsad, Shinya Ikeno and Rashidah Abdul Rahim.
This open-access article is distributed under a Creative Commons Attribution (CC-BY) 4.0 license. |
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言語 |
en |
| 抄録 |
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内容記述タイプ |
Abstract |
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内容記述 |
Sphingobacterium sp. AB3 lipase is a psychrophilic enzyme with optimal lipolytic activity at pH 7 and 15°C. The cold-adapted properties of the lipase render it suitable for various low-temperature industrial applications such as biodiesel production, detergent formulation, and non-thermal food processing. Recent studies have shown that co-expression of LEA K peptide with AB3 lipase resulted in enhanced protein expression in Escherichia coli. In this study, the purified AB3 lipase was characterized by substrate specificity, followed by tertiary structure prediction of the lipase and LEA K peptide using SWISS-MODEL and PEP-FOLD 3.5, respectively. Molecular docking studies were conducted to study the lipase-LEA K interactions using ClusPro and lipase-olive oil interactions with and without LEA K using Autodock Vina. Based on the findings, AB3 lipase showed the highest preference for olive oil with a lipase-specific activity of 153.3 U/mg. In the presence of LEA K, the binding affinity of AB3 lipase with olive oil improved from -4.7 to -7.0, kcal/moL with increased hydrophobic interactions and hydrogen bonding with catalytic residues of the lipase. Overall, understanding the interaction between the AB3 lipase and LEA K peptide offers valuable insights into the mechanisms underlying the improved stability and affinity of the protein-peptide complex. |
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言語 |
en |
| 書誌情報 |
en : American Journal of Biochemistry and Biotechnology
巻 20,
号 4,
p. 385-395,
発行日 2024-11-21
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| 出版社 |
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出版者 |
Science Publications |
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言語 |
en |
| 言語 |
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|
言語 |
eng |
| 資源タイプ |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
| 出版タイプ |
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出版タイプ |
VoR |
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出版タイプResource |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
| DOI |
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識別子タイプ |
DOI |
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|
関連識別子 |
https://doi.org/10.3844/ajbbsp.2024.385.395 |
| ISSN |
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収録物識別子タイプ |
PISSN |
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収録物識別子 |
1553-3468 |
| ISSN |
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収録物識別子タイプ |
EISSN |
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収録物識別子 |
1558-6332 |
| 研究者情報 |
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|
URL |
https://hyokadb02.jimu.kyutech.ac.jp/html/331_ja.html |
| 論文ID（連携） |
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|
値 |
10448782 |
| 連携ID |
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|
値 |
13052 |
10448782.pdf (1.1 MB)
