High-level expression and characterization of a novel aspartic protease from Talaromyces leycettanus JCM12802 and its potential application in juice clarification

•TlAP was highly expressed in P. pastoris with a specific activity of 1795.4 U/mg.•It was acido-mesophilic, showing optimal activities at pH 3.0 and 55 °C.•It retained highly stable (>70% activity) at pH 3.0–6.0 and at 45 °C and below.•It was highly resistant against most metal ions and chemical reagents.•It showed ability to decrease juice turbidity and disintegrate haze-forming proteins.