Abstract：
Heterogeneous biocatalysts were prepared by adsorbing T. lanuginosus lipase (TLL) onto uncalcined (SBAUC-TLL) and calcined (SBAC-TLL) SBA-15, using ammonium fluoride as a pore expander to facilitate TLL immobilization. At an enzyme load of 1 mg/g, high immobilization yields (>90 %) and recovered activities (>80 % for SBAUC-TLL and 70 % for SBAC-TLL) were achieved. When increasing the enzyme load to 5 mg/g, the immobilization yield of SBAUC-TLL was 80 %, and the recovered activity was 50 %, while SBAC-TLL had a yield of 100 % and a recovered activity of 36 %. Crosslinking with glutaraldehyde (GA) was conducted to improve stability (SBAUC-TLL-GA and SBAC-TLL-GA). Although SBAC-TLL-GA lost 25 % of initial activity after GA modifications, it exhibited the highest thermal (t1/2 = 5.7 h at 65 °C), when compared to SBAC-TLL (t1/2 = 12 min) and the soluble enzyme (t1/2 = 36 min), and operational stability (retained 100 % activity after 5 cycles). Both biocatalysts presented high storage stability since they retained 100 % of initial activity for 30 days. These results highlight SBA-15\'s potential as an enzyme support and the protocol\'s efficacy in enhancing stability, with implications for industrial applications in the food, chemical, and pharmaceutical sectors.
摘要：
通过使用氟化铵作为扩孔剂以促进TLL固定，将毛藻木霉脂肪酶（TLL）吸附到未煅烧（SBAUC-TLL）和煅烧（SBAC-TLL）SBA-15上，制备了非均相生物催化剂。在1mg/g的酶负荷下，实现了高固定化产率(>90%)和回收活性(SBAUC-TLL>80%和SBAC-TLL>70%)。当将酶负荷增加到5mg/g时，SBAUC-TLL的固定化产率为80%，恢复的活性为50%，而SBAC-TLL具有100%的产率和36%的恢复活性。进行与戊二醛(GA)的交联以改善稳定性(SBAUC-TLL-GA和SBAC-TLL-GA)。虽然SBAC-TLL-GA在GA修饰后失去了25%的初始活性，它表现出最高的热量（t1/2=5.7小时，在65°C），与SBAC-TLL（t1/2=12分钟）和可溶性酶（t1/2=36分钟）相比，和操作稳定性(5个循环后保持100%活性)。两种生物催化剂均呈现高储存稳定性,因为它们保持100%的初始活性持续30天。这些结果突出了SBA-15作为酶支持的潜力和方案在增强稳定性方面的功效，对食品工业应用的影响，化学,和制药部门。
