Enhanced enzyme thermostability of a family I.3 lipase LipSR1 by T118A mutation at the calcium-binding site
Author:
Funder
National Key R&D Program of China
National Natural Science Foundation of China
Publisher
Springer Science and Business Media LLC
Subject
General Medicine,Biotechnology,Bioengineering,Applied Microbiology and Biotechnology
Link
https://link.springer.com/content/pdf/10.1007/s10529-023-03413-8.pdf
Reference23 articles.
1. Amada K, Haruki M, Imanaka T, Morikawa M, Kanaya S (2000) Overproduction in Escherichia coli, purification and characterization of a family I.3 lipase from Pseudomonas sp. MIS38. Biochim Biophys Acta 1478:201–210. https://doi.org/10.1016/S0167-4838(00)00046-7
2. Bordoli L, Kiefer F, Arnold K, Benkert P, Battey J, Schwede T (2009) Protein structure homology modeling using SWISS-MODEL workspace. Nat Protoc 4:1–13. https://doi.org/10.1038/nprot.2008.197
3. Brocca S, Secundo F, Ossola M, Alberghina L, Carrea G, Lotti M (2003) Sequence of the lid affects activity and specificity of Candida rugosa lipase isoenzymes. Protein Sci 12:2312–2319. https://doi.org/10.1110/ps.0304003
4. Casas-Godoy L, Gasteazoro F, Duquesne S, Bordes F, Marty A, Sandoval G (2018) Lipases: an overview. Methods Mol Biol 1835:3–38. https://doi.org/10.1007/978-1-4939-8672-9_1
5. Chandra P, Singh R, Arora PK (2020) Microbial lipases and their industrial applications: a comprehensive review. Microb Cell Fact 19:169. https://doi.org/10.1186/s12934-020-01428-8
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