A gel model for the functioning of luciferase in cells has been constr
ucted using bacterial NADH:FMN-oxidoreductase and luciferase immobiliz
ed in starch gel disks. The characteristics of the immobilized lucifer
ase depend on the duration of drying, the amount and concentration of
the gel, the nature of the support used for drying, and the properties
of the initial enzyme preparation. Functionally important enzyme grou
ps remain intact in the immobilized preparation, and luciferase retain
s its high specificity with respect to aldehydes. The gel microenviron
ment appears to be optimal for luciferase, judging from its high activ
ity and increased stability. Conditions allowing repeated use of the p
reparation have been found. The approach permits co-immobilization of
luciferase with other enzymes and their substrates. The error in biolu
minescence measurements using the disks is 5-10%. A procedure for stab
ilization of the immobilized luciferase during repeated use has been d
evised.