Study of Trypsin Behavior into Functionalized Nano-Engineered SBA-15: Loading and Stability of Enzyme

سال انتشار: 1388
نوع سند: مقاله کنفرانسی
زبان: انگلیسی
مشاهده: 1,655

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شناسه ملی سند علمی:

CNS03_233

تاریخ نمایه سازی: 21 دی 1388

چکیده مقاله:

Immobilization of trypsin enzyme (37×37×42A°) into inorganic host materials has attracted considerable attention over the past few years. Hexagonal mesoporous SBA-15-type molecular sieves with thiol, amin, phenyl, sulfonic acid functional groups and pore size in the range of 55-65A° have been prepared non-ionic block copolymers and used for immobilization of the trypsin enzyme. Trypsin immobilization on unfunctionalized SBA-15 showed the maximum amount of loading and activity at 25 °C, PH 8 and lowest amount of medium ionic strength. Though about the functionalized SBA-15, we see that each function has a specific effect on trypsin behavior. The XRD and pore symmetry result indicated that SBA-15 with thiol function has a maximum amount of loading due to our experimental data. However, in this report in temperature over than 40°C, could not be achieved a good activity from immobilized trypsin although stability of adsorbed trypsin in comparison to free one was totally considerable. Our focus in this study is on SBA-15 with thiol and sulfonic acid functions, because of the maximum activity and highly amount of loading could be accomplished in this condition.

نویسندگان

S Emadi

Institute of Advance Studies in Basic Science, Zanjan, Iran