The combined influence of preheat treatment, mixing with various proteins, and the addition of microbial transglutaminase (MTGase) on the physicochemical properties of bovine collagen-peptide (BCP) gel was investigated. The preheat treatment and the mixing with various proteins contributed to the enhancement of the gel strength and polymerization of BCP. The gel made with 0.1% MTGase showed the highest breaking strength. The melting point of the preheated BCP gel was higher than that of the unheated one (P < 0.05). The gel made with a combination of preheated BCP-casein or preheated BCP-soybean protein showed a higher melting point than that made with preheated BCP alone (P < 0.05). The sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) pattern of the mixture of preheated BCP with casein or soybean protein showed that the protein bands with relatively low molecular weights disappeared and the bands with relatively high molecular weights increased. Observation by a scanning electron microscope revealed that the preheated BCP gel prepared with MTGase had a well-defined cross-linked network and showed some clumps of aggregated proteins. These results show that preheating, mixing with other proteins and MTGase treatment, are effective ways to make BCP a fine biopolymer.