The immobilization of Fusarium solani β-glucosidase (FBgl1) on chitosan was performed to improve biocatalyst performance. Compared with free FBgl1, the immobilized biocatalyst exhibited a shift of the optimal temperature, a conservation of the optimum pH with high residual activity at extreme acidic pH and an improved thermal stability. The immobilized enzyme was reusable up to 12 cycles. The FBgl1 immobilization enhanced its glucose and organic solvent tolerance. The free form of FBgl1 was unable to synthesize alkylglucosides, while the immobilized one was able to react using butanol as alcohol and either cellobiose or glucose as glucoside. The alkylglucosides were characterized by nuclear magnetic resonance as sec-butyl-β-d-glucoside and sec-butyl-β-d-cellobioside. It is worth noting that this last glucomolecule is synthesized for the first time using an enzymatic process. These butylglucosides exhibited a typical surfactant behavior (surface tension 26−35 mN/m and critical micellar concentration 250−1000 mg/L).

进行了枯萎镰刀菌β-葡萄糖苷酶（FBgl1）固定在壳聚糖上，以提高生物催化剂的性能。与游离的FBgl1相比，固定化的生物催化剂表现出最佳温度的变化，最佳pH的保留，在极端酸性pH下的高残留活性以及改善的热稳定性。固定的酶最多可重复使用12个循环。固定化FBgl1增强了葡萄糖和有机溶剂的耐受性。游离形式的FBgl1不能合成烷基葡糖苷，而固定化的FBgl1能够使用丁醇作为醇和纤维二糖或葡萄糖作为葡糖苷反应。烷基葡萄糖苷通过核磁共振表征为仲丁基-β- d-葡萄糖苷和仲丁基-β- d-纤维二糖苷。值得注意的是，该最后的糖分子是使用酶促方法首次合成的。这些丁基葡萄糖苷表现出典型的表面活性剂行为（表面张力26-35 mN / m和临界胶束浓度250-1000 mg / L）。