〔Abstract〕 Objective To explore the expression and purification of PrtC protein fromPorphyromonas gingivalisand its functionin vitro. Methods The whole gene was used to synthesizeprtC gene in ATCC33277 ofPorphyromonas gingivalis, and the recombinant expression vector p29-prtC was constructed,Bioinformatics analysis, low-temperature induced expression,SDS-PAGE and Western blot identification were performed, and the function of collagenase was detected by enzymatic hydrolysis. Results The prokaryotic expression vector of collagenase protein PrtC was successfully constructed, and the soluble protein expression was obtained in the expression system ofE.coli. The protein PrtC with high purity and stability was purified by affinity chromatography and molecular sieve chromatography, and it was proved to have the ability to degrade collagen. Conclusion PrtC protein expressed by prokaryotic recombinant protein had collagenase activity, which laid a foundation for subsequent analysis of PrtC structure.