Several immobilization techniques have been introduced to increase the industrial utilization of biocatalysis, where the enzymes either are adsorbed and anchored on inherent matrices 1 or are crystallized and cross-linked with glutaraldehyde. 2 These techniques allow one to recover or to reuse the biocatalysts in large-scale industrial production, but still present significant problems in terms of enzyme recycling, stability, and functional activity. In direct comparison to the above existing immobilization techniques, protein monolayer engineering 1,3 has been shown to yield in few model systems 3-10 unmatchable results in terms of both heat stability and lifetime, making this technique quite promising for a wide range of potential applications in industrial biocatalysis.Among available thin film technologies, several modifications 1,3-10 of the technology originally introduced by Langmuir 11,12 appear to be the most promising ones, being capable of engineering enzymes into highly ordered monolayers with a high degree of packing and molecular orientation. Particularly appealing is the possibility to deposit the 2D monolayer onto spherical substrates of desired size, assembly, and chemical composition. 10 In this overview, the recent development in the engineering of enzyme monolayers that are more relevant to industrial biocatalysis 13-15 is summarized, with emphasis on the recycling stability and the cost-effectiveness, along with the outline of a possible emerging bioreactor and the attempt to standardize an optimal procedure that takes into consideration the numerous parameters controlling the structure and the function of enzymes during thin film formation at the air/water interface. [16][17][18][19][20][21][22][23][24][25][26][27] 435 a