The　salt-induced　gelation　behavior　of　soy　protein　isolate　(SPI)　emulsions　was　markedly　influenced　by　microbial　transglutaminase　(TGase)　pre-crosslinking.　Rheological　data　showed　that　when　SPI　emulsions　were　incubated　with　TGase　at　low　concentrations　(1　and　3　U/g　protein)　at　50　degrees　C　for　30　min　prior　to　gelation,　no　change　in　storage　modulus　(G＇),　but　enhanced　resistance　to　deformation　of　the　gels　was　observed.　Extensive　crosslinking　by　TGase　(5　U/g　protein)　resulted　in　severe　decreases　in　gel　firmness　and　fracture　properties　(yielding　stress　and　strain),　likely　due　to　the　impairment　of　hydrophobic　bonds　and　the　formation　of　coarse　networks.　The　water-holding　capacity　of　the　gels　was　significantly　enhanced　by　increased　concentrations　of　TGase.　Interactive　force　analysis　indicated　that　non-covalent　interactions　and　disulfide　bonds　are　the　primary　forces　involved　in　CaSO4-induced　SPI　emulsion　gel,　but　TGase　treatment　may　limit　hydrophobic　interactions　within　the　gel　network.　These　results　are　of　great　potential　value　for　the　application　of　TGase　in　the　food　industry.