Enhancing immobilization of Aspergillus oryzae ST11 lipase on polyacrylonitrile nanofibrous membrane by bovine serum albumin and its application for biodiesel production

The partially purified lipase from Aspergillus oryzae ST11 was immobilized on the surface-modified electrospun polyacrylonitrile (PAN) nanofibrous membrane. The effects of time and concentrations of glutaraldehyde and bovine serum albumin (BSA) were studied. The immobilized lipase reached the maximum activity at 180 min with the recovered activity of 44.2% (0.22 U/mg-support) in the absence of BSA. After adding 6 mg/mL BSA and 40 mM glutaraldehyde gave the recovered activity at 86.9% (0.43 U/mg-support). It showed the highest stability at pH 7.5 but the soluble lipase was at pH 7.0. In addition, the immobilized lipase was more stable at pH 4.0 and 9.0. The immobilized lipase preserved 56% activity at 70 degrees C but the soluble lipase had 34% activity. It conserved 86% activity while the soluble lipase had 18% activity after 13 days of storage at 4 degrees C. The operating parameters such as biocatalyst concentration, water content, and the molar ratio of methanol and palm oil were optimized for biodiesel production. The highest biodiesel conversion (95%) was obtained with the immobilized lipase 15% (w/w), 40% (w/w) 50 mM Tris-HCl buffer pH 7.0 and methanol/palm oil (3.5:1.0). This immobilized lipase could be reused with 82.9% conversion after 10 cycles of batch production.

Automated summary

The partially purified lipase from Aspergillus oryzae ST11 was immobilized on electrospun polyacrylonitrile (PAN) nanofibrous membrane. The immobilized lipase showed increased stability and activity under optimized pH conditions and specific additives, with significant biodiesel conversion efficiency and reusability.