王静云,马翠丽,包永明.脂肪酶仿生固定化及性质[J].分子催化,2011,(4):341-347
脂肪酶仿生固定化及性质
The immobilization of lipase by biomimetic mineralization and its properties
  
DOI:
中文关键词:  仿生钛化  氧化钛  精蛋白  固定化脂肪酶
英文关键词:Biomimetic mineralization  Titania  Protamine  Encapsulated lipase
基金项目:国家重点基础研究发展计划 “973” 项目(2009CB724706)资助
作者单位
王静云 大连理工大学 生命科学与技术学院 
马翠丽 大连理工大学 生命科学与技术学院 
包永明 大连理工大学 生命科学与技术学院 
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中文摘要:
      温和条件下的生物矿化过程能够合成结构复杂、性能优异的无机材料,为酶固定化提供了重要启示。本文首次将仿生钛化过程用于脂肪酶固定化,研究了该过程中工艺条件对脂肪酶固定化的影响及固定化脂肪酶的性质。结果表明: 0.5 ml 浓度8 mg/ml精蛋白诱导剂、0.5 ml 浓度6 mg/ml脂肪酶与1ml, 0.25M 钛前驱体(Ti-BALDH)在pH 7.5,0.05 mol/L磷酸盐缓冲液为反应介质的条件下,脂肪酶的包埋率达70.1%,酶活回收率为20.3%。固定化脂肪酶的最适pH为8.0,最适温度为45 ℃;与游离酶相比,固定化脂肪酶的pH、温度和储存稳定性都有了较大提高;重复6次使用,固定化脂肪酶仍保持最初酶活的41%。
英文摘要:
      Biomimetic mineralization, which employs biological molecules to induce and drive the formation of inorganic oxides with excellent properties at room temperature, ambient pressure and neutral pH, provides a facile new method for enzyme immobilization. In the present study, for the first time, the biomimetic synthesis of titania was employed for the immobilization of lipase. The optimal encapsulation efficiency (70.1%) and activity recovery (20.3%) of lipase were achieved when 0.5ml protamine solution of 8mg/ml and 0.5ml lipase solution of 6mg/ml were reacted with 1ml Ti-BALDH of 0.25mol/L in phosphate buffer (pH7.5, 0.05 mmol/L). It was found that the optimum pH of free and encapsulated lipase in titania particles were pH 7.0 and 8.0, respectively, while the optimum temperature were 37 ℃and 45 ℃. Additionally, the lipase encapsulated into titania particles exhibited significantly enhanced pH, thermal, and storage stability, still retained 41% of its initial activity after consecutive 6 cycles.
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