Molecular cloning and characterization of a novel cold-active lipase from Pichia lynferdii NRRL Y-7723
- Authors
- Bae, Jae-Han; Kim, In-Hwan; Lee, Ki-Teak; Hou, Ching T.; Kim, Hak-Ryul
- Issue Date
- 7월-2017
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- Lipase; Cold-active; Cloning; Pichia lynferdii
- Citation
- BIOCATALYSIS AND AGRICULTURAL BIOTECHNOLOGY, v.11, pp.19 - 25
- Indexed
- SCOPUS
- Journal Title
- BIOCATALYSIS AND AGRICULTURAL BIOTECHNOLOGY
- Volume
- 11
- Start Page
- 19
- End Page
- 25
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/82958
- DOI
- 10.1016/j.bcab.2017.05.008
- ISSN
- 1878-8181
- Abstract
- Lipase is one of the widely used biocatalysts, which is well studied for its application in industrial production. Recently, lipases with special characteristics such as thermo-stability, alkaline-, acidic nature, and cold-activity, have gained attention for effective applications in specific purposes. Previously, Pichia lynferdii NRRL Y-7723 was reported to produce high amounts of extracellular cold-active lipase (Kim et al., 2010). In this study, we report the identification of lip1 gene that encodes an extracellular cold-active lipase from P. lynferdii NRRL Y-7723. The open reading frame of the gene consisted of 1122 bp of nucleotides that encoded a protein with 373 amino acids. The deduced molecular weight and isoelectric point were 41.8 kDa and pH 5.82, respectively. The lip1 gene was cloned into a bacterial expression vector, and the recombinant lipase was successfully expressed and purified. Several parameters of the recombinant lipase were analyzed, and Lip1 showed high activity at low temperature.
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Collections - College of Health Sciences > School of Biosystems and Biomedical Sciences > 1. Journal Articles
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