Co-immobilization of two enzymes by Sol-gel Encapsulation Improves Production of Lactosucrose

• 1、School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122

Abstract：β-fructofuranosidase was obtained from Arthrobacter sp.10137 and purified by ammonium sulphate precipitation. The purified β-fructofuranosidase and glucose oxidase were co-immobilized by the sol-gel method and characterized by scanning electron microscopy, particle size analysis, Fourier transform infrared spectroscopy, and thermogravimetric analysis. The results showed that the co-immobilized enzymes had a more regular surface and yielded larger particles than the sol-gel matrix. The co-immobilized enzymes retained 85.39% of their activity with a specific activity of 216.57 U/g gel (wet weight). The co-immobilized enzymes exhibited good thermal stability. When the temperature was above 40 C, the free enzyme lost its transfructosylation activity. However, the co-immobilized enzymes showed significantly higher activity than the free enzyme (p<0.01). Moreover, the co-immobilized enzymes displayed good operational stability in that the enzyme retained 82.0% of their original activity after 8 consecutive reuses. The co-immobilized enzymes provide high stability, which increases the production of lactosucrose with low costs.

Keywords： Food science co-immobilization stability β-fructofuranosidase lactosucrose glucose oxidase