Discovery Sagaサイレントキーワード俯瞰

In this research, an enzyme will be immobilized inside the chemically modified mesoporous silica, MCM-41, to enhance both its stability and reactivity. The enzyme of interest in this work is protocatechuate 3,4-dioxygenase, which can selectively cleave a strong C-C bond in the catechol aromatic ring.
In year 2021, preparation of mesoporous silica and modification of its surface using silane coupling agent were achieved. As a choice of mesoporous silica, SBA-15 was synthesized, instead of MCM-41. This was due to the fact that (1) the protocol of its synthesis was well-established in the Ogura lab, the group where this research was carried out and (2) SBA-15 has a similar pore structure as MCM-41 with controlled pore size. The synthesized SBA-15 with average pore size of 8 nm was then subjected to surface modification by silane coupling to obtain the modified SBA-15, m-SBA-15.
To prove the stabilizing effect of the unstable enzyme via immobilization into mesoporous silica, a more commonly and widely used enzyme compared to protocatechuate 3,4-dioxygenase, lipase, was immobilized first into m-SBA-15. As a result, the increase in stability of lipase was successfully observed through immobilization into m-SBA-15. Moreover, methods to measure and quantify the amount of active lipase were explored and established.
In addition, SBA-15 with pore size of 10 nm and 12 nm that are commercially available were also purchased, and subjected to surface modification to compare the amount of active, immobilized lipase.