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.
Original language | English |
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Pages (from-to) | 19-25 |
Number of pages | 7 |
Journal | Biocatalysis and Agricultural Biotechnology |
Volume | 11 |
DOIs | |
Publication status | Published - 2017 Jul |
Keywords
- Cloning
- Cold-active
- Lipase
- Pichia lynferdii
ASJC Scopus subject areas
- Biotechnology
- Food Science
- Bioengineering
- Applied Microbiology and Biotechnology
- Agronomy and Crop Science