Lipase and cutinase belong to the esterase family and have biological applications in many fields. To develop more efficient biocatalysts that can be used for waste paper deinking, a chimeric lipase-cutinase (Lip-Cut) was constructed and successfully overexpressed in Pichia pastoris. The chimeric Lip-Cut exhibited lipase and cutinase activities that were 127% and 210% higher than their parent enzymes, respectively. Cut was superior to Lip in ink removal and improvement of paper brightness than Lip. The Lip-Cut displayed a better ink removal efficiency and paper brightness than that of the Lip, Cut, and Lip/Cut mixture. When the chimeric Lip-Cut was used, the ink removal efficiencies were 25.8% and 16.2% higher than that of the control-treated laser-printed paper and newspaper, which had sheet brightness values of 88% ISO and 59% ISO, respectively. The results demonstrated that the proper construction of bi-functional Lip-Cut could enhance the catalytic properties through the synergistic action of the two moieties because of the complementary advantages in the substrate specificities and catalysis patterns of both enzymes. This may provide an effective way to engineer more efficient bi-functional lipases and cutinases for deinking waste paper.