Encapsulation of lipase in mesoporous silica yolk–shell spheres with enhanced enzyme stability

Abstract

Enzyme encapsulation is an attractive method among the different immobilization strategies to improve the reusability and stability of enzymes because it can separate enzymes from a hazardous external environment. However, current encapsulation methods have limitations including enzyme leakage. In this study, a new approach based on a two-step soft templating method has been proposed to encapsulate lipase within substrate permeable mesoporous silica yolk-shell spheres. In the first step, lipase was immobilized onto epoxy functionalized silica nanospheres that serve as the core materials. The core materials were mixed with a fluorocarbon surfactant, FC4, to form a core-vesicle complex. In the second step, a mesoporous silica shell was assembled surrounding the core-vesicle complex to form the yolk-shell structure with the lipase encapsulated. The mesoporous silica shell has a pore size of 2.1 nm, which is permeable to the reactant and product while isolating the enzymes from harmful external conditions. The encapsulated lipase retained 87.5% of its activity after thermal treatment at 70 C for 2 hours while the free enzyme lost 99.5% of its activity under the same treatment. Importantly, the encapsulated lipase shows significantly enhanced resistance to degradation by proteases.

Improved Performance of Lipase Immobilized on Tannic Acid-Templated Mesoporous Silica Nanoparticles

“…These results indicated that the BCL@TA-MSNs showed better thermal stability compared to free BCL, which can be attributed to the microenvironment provided by the TA-MSNs. It means that the major part of the lipase is immobilized inside the pores of the TA-MSNs, which provided a sheltered position that can provide a more rigid external backbone for lipase molecules and thus protect the lipase from thermal damage [25,50].…”

Heterogeneous Asymmetric Oxidation Catalysis Using Hemophore HasApf. Application in the Chemoenzymatic Deracemization of sec-Alcohols with Sodium Borohydride

“…Therefore, although further explorations of the efficiency, turnover number, or enzyme loading in comparison to other known systems for this or similar transformations are being actively pursued in this laboratory, this process would overcome the apparent difficulties in working with pure dehydrogenase enzymatic/redox-cofactor systems for biotransformation. The use of a heme-binding protein (HBP) as a HasA-catalytic system has been proposed for heterogeneous enzyme catalysis [44][45][46], where a redox cofactor is incorporated to perform asymmetric oxidation. In the future, bacterial HasAs are expected to become important biological catalysts for the Therefore, although further explorations of the efficiency, turnover number, or enzyme loading in comparison to other known systems for this or similar transformations are being actively pursued in this laboratory, this process would overcome the apparent difficulties in working with pure dehydrogenase enzymatic/redox-cofactor systems for biotransformation.…”

“…In the future, bacterial HasAs are expected to become important biological catalysts for the Therefore, although further explorations of the efficiency, turnover number, or enzyme loading in comparison to other known systems for this or similar transformations are being actively pursued in this laboratory, this process would overcome the apparent difficulties in working with pure dehydrogenase enzymatic/redox-cofactor systems for biotransformation. The use of a heme-binding protein (HBP) as a HasA-catalytic system has been proposed for heterogeneous enzyme catalysis [44][45][46], where a redox cofactor is incorporated to perform asymmetric oxidation. In the future, bacterial HasAs are expected to become important biological catalysts for the synthesis of optically active alcohols using environmentally friendly systems that promote industrial sustainability.…”

Use of silica supports for enhancing the stability of folates and developing antimicrobial agents

“…Concretely, encapsulation of lipase in mesoporous silica yolk-shell spheres enhanced its thermal stability in a 90%, compared to free lipase that loses its activity after thermal treatment at 70 °C for 2 h (Zhao et al, 2013).…”

“…Among bioactive molecules that have been protected from the environment via the encapsulation in MSPs highlight enzymes (Zhao et al, 2013), or the flavonoid quercetin (Berlier et al, 2013).…”