Immobilization of xylanase and xylanase–β-cyclodextrin complex in polyvinyl alcohol via electrospinning improves enzyme activity at a wide pH and temperature range

Abstract

Xylanase (EC 3.2.1.8) is a key enzyme for degradation of xylan. A limitation of xylanase application in food and beverage industries is the low enzyme activity and stability at a wide pH and temperature range. In the present study, different levels of pure xylanase (XY) and xylanase–β-cyclodextrin (XY–β-CD) inclusion complex were immobilized in polyvinyl alcohol (PVA) via electrospinning. Morphological and structural characteristics of obtained fibers were investigated by Fourier-transformed infrared spectroscopy (FTIR), scanning electron microscopy (SEM), and X–ray diffraction (XRD) analyzes. Inclusion complex formation was evaluated by FTIR, XRD, and differential scanning calorimetry (DSC) analyzes. Obtained electrospun fibers showed a smooth surface with average diameter from around 200 to 600 nm. Greater diameters were observed at higher xylanase levels. In addition, inclusion complex provided thicker fibers than pure xylanase. Optimum xylanase activity changed from 60 to 70 °C when enzyme was immobilized in PVA. FTIR results suggest a more efficient enzyme conformation after immobilization. The greatest xylanase efficiency of immobilization was achieved at 0.5%-XY, with specific activity of 59.73 μM/min/mg of immobilized xylanase. Xylanase immobilized in PVA fibers exhibited higher activity at extremer pH conditions (4, 5, 7, and 8), as compared to free xylanase.