Production of a novel cold-active lipase from Pichia lynferdii Y-7723.
Lipase (triacylglycerol acylhydrolases, E.C. 3.1.1.3) is one of the most important enzymes applied to a broad range of industrial application fields. Especially, lipases with abnormal functionality such as thermostability and alkaline, acidic, and cold activities gain special attention because of their applicability in the restricted reaction conditions. In this study, 16 yeast strains prescreened for lipase induction were investigated for their actual lipase production, and we found a novel cold-active lipase produced from Pichia lynferdii Y-7723. The activity of lipase Y-7723 was retained by 74 and 70% at 20 and 10 degrees C, respectively, as compared to the maximum value at 35 degrees C. On the basis of an optimization study, the optimal lipase productivity was obtained at 96 h of incubation with 3% oil substrate in a medium composed of sucrose as a carbon source at pH 7.0. Among carbon sources tested, sucrose showed almost twice as high of a lipase production (184%) as the control, while the cell growth was similar (105%). Yeast extract and ammonium salts were effective as individual nitrogen sources for lipase production. This study demonstrated that the cold activity of lipase Y-7723 at 10 degrees C was highest among the cold-active lipases reported so far.
Kim
Hak-Ryul
HR
Department of Animal Science and Biotechnology, Kyungpook National University, Daegu 702-701, Korea. hakrkim@knu.ac.kr
Kim
In-Hwan
IH
Hou
Ching T
CT
Kwon
Kwang-Il
KI
Shin
Beom-Soo
BS
D003080:Cold Temperature; D004789:Enzyme Activation; D004795:Enzyme Stability; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism*; D008049:Lipase / Q000737:chemistry* / Q000378:metabolism*; D010843:Pichia / Q000737:chemistry / Q000201:enzymology*; D015003:Yeasts / Q000737:chemistry / Q000201:enzymology
D005656:Fungal Proteins; D008049:Lipase