Summary: This communication describes an enzyme stabilization method that allows the use of enzymes irrespective of environmental factors, especially heat, while maintaining their activity for a long time. We have designed enzyme microcapsules that consist of papain enzyme cores, poly(propylene glycol) interlayers, and poly(ε‐caprolactone) walls. By confocal laser scanning microscopy measurements and the thermal stability of papain‐loaded microcapsules, it is demonstrated that the papain is surrounded by a hydrophobic polyol layer and stabilized by the exclusive volume effect. In our study, improved thermal stability can be obtained by using more hydrophobic long‐chained polyols, which is understood to be attributed to the effective formation of a hydrophobic polyol layer between the papain and the polymer wall by means of conformational anchoring in the interface.
(A) A CLSM image of a PCL microcapsule containing FITC‐labeled papain and RBITC‐labeled PPG at the same time. (B) A scheme of the role of hydrophobic polyols in the interface of enzyme and polymer.
