Objective To judge the stability and digestibility of human α-lactalbumin derived from recombinant bovine. To compare the digestion time for the recombinant human α-lactalbumin with that for standard human α-lactalbumin in simulated gastric and intestinal fluid or in gastric and intestinal fluid extracted from miniature swine. This would provide basic materials for assessing the allergenicity of recombinant proteins. Methods The recombinant protein and human α-lactalbumin standard substance were digested according to the national standard method Food safety detection of genetically modified organisms and derived products—Method of target protein digestive stability in simulative gastric and intestinal fluid. The samples after digestion were analyzed with sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting. Results The recombinant protein samples were digested completely within 0 s in simulated gastric fluid; 10 min in simulated intestinal fluid; and 20 min in gastric and intestinal fluid of miniature swine. The digestion time was all less than 20 minutes for recombinant protein samples, which was similar for human α-lactalbumin standard substance, although some differences were existed. Conclusion There was no digestion resistance of the recombinant protein in simulated gastric and intestinal fluid or in gastric and intestinal fluid extracted from miniature swine.