Screening and design of immobilized biocatalysts (IMBs) is a time-consuming process. An ideal process should be universal, fast, convenient, precise, and reproducible. Many of these requirements are met by enzymic flow microcalorimeters, also known as enzyme thermistors (ETs) or thermal assay probes (TAPs). Adaptation of ETs to real measurements of reaction rates requires coupling of the mathematical description of the reaction-diffusion phenomena in the ET column with heat balance and, subsequently, experimental verification of the mathematical model. This article presents such a process developed as an adaptation of ETs for the characterization of the microkinetic properties of IMBs and their further application for screening of IMBs. The IMBs characterized were the preparations of invertase, biospecificaly adsorbed on concanavalin A conjugated to activated bead cellulose.