We developed a Polyvinyl butyral (PVB)-zirconium alkoxide hybrid hollow tube by air-gap spinning. Enzyme (beta-galactosidase and lipase) was physically entrap-immobilized and disseminated throughout the hollow tube architecture. The enzyme immobilized PVB-Zr hybrid tube shown its stability in phosphate buffer solution, electrolyte solution, and other organic solvents. The apparent Michaelis constant K-m for immobilized beta-galactosidase (I beta G) was 0.079 mol/l compared to 0.067 mol/l for free enzyme. The maximum velocity V-max was 4.9 mu mol.min(-1), whereas it was 11.5 mu mol.min(-1) for free enzyme. The preserved activity of I beta G was found to be 90%, after ten reaction cycles. Moreover, up to 70% conversion for citronellyl acetate after 50 h. was achieved by immobilized lipase (IL) in hexane solution. The activity of IL was found to be 62% after 8 repeated uses where free enzyme retained 15% activity. Overall, it was considered that the enzyme activity employed both in the interior and the vicinity of the hollow tube surface.