Gene Cloning, Purification, and Characterization of a Cold-Active Alkaline Lipase from <i>Bacillus cereus</i> U2
Baoxiang He | Ning Li | Yan Qin | Liang Xian | Jin Zhou | Sijia Liu | Jing Zhang | Jingtao Wu | Qingyan Wang | Xinquan Liang
Lipases are important industrial enzymes with a wide range of applications across various sectors. Cold-active lipases are particularly well suited for industrial processes that operate at low temperatures (such as food processing and environmental remediation) due to their high catalytic efficiency and energy-saving benefits. In this study, a novel lipase—LipU (GenBank accession: PV094892)—was heterologously expressed from <i>Bacillus cereus</i> U2 and characterized for its low-temperature adaptability and alkaline resistance. LipU belongs to the lipase Subfamily I.5 and shares the highest amino acid sequence identity (53.32%) with known homologs. Enzymatic assays revealed that LipU exhibits optimal activity at 20 °C and pH 11. It retained 95% of its initial activity after 24 h of incubation at 4 °C and pH 11.0. Furthermore, the activity of LipU was enhanced by Ca<sup>2</sup>⁺, Na⁺, Tween 20, and Tween 80, whereas it was inhibited by Cu<sup>2</sup>⁺, Zn<sup>2</sup>⁺, Mn<sup>2</sup>⁺, and sodium dodecyl sulfate (SDS). LipU demonstrated tolerance to various organic solvents of differing polarity; after 1 h of exposure to 15% (<i>v</i>/<i>v</i>) ethanol, n-butanol, isoamyl alcohol, dimethyl sulfoxide, or glycerol, it retained over 78.6% of its activity. These properties make LipU a promising candidate for industrial applications, including for leather degreasing, alkaline wastewater treatment, and low-temperature biocatalysis.
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