that are generally added to protein/antibody formulations to improve its stability. I do not think that there is a universal agent, since it depends from the kind of interaction (charge to charge, hydrofobic interactions)
also the addiction of cofactors (eg sugars, metals) can sometimes improve a lot the enzime stability
DSF is a good and simple approach to screen it.
For example in the past I used it to check the thermal stability induced by binding of UDP-glucose and Mn to an Glucosil transferases
Article The structure of Clostridium difficile toxin A glucosyltrans...
as well as the binding of Zn to a Zinc metalloproteases
Article Identification of a Novel Zinc Metalloprotease through a Glo...
Of course in some cases, when the protein instability is due to non correct protein folding (eg due to the non correct formation of an S-S bond) the formulation cannot be able to solve the problem and you need to go back to optimize the protein domain, perform mutagensys or change expression host (eg using mammalian instead bacteria) or conditions.
Rather than using an additive, you can try to immobilize the enzyme on some inorganic material. This can improve the enzyme thermal stability by 20°C to 30°C.