Oral iron salts are commonly used as supplements and fortificants to treat iron deficiency and anemia, but they are often poorly absorbed and cause gastrointestinal side effects, highlighting the need for more efficient and better-tolerated alternatives. Bovine lactoferrin (LF), a natural iron-binding glycoprotein, offers a promising option for iron supplementation, as it can deliver iron via receptor-mediated uptake in the small intestine. However, its efficacy may be compromised by proteolytic degradation during gastrointestinal digestion. In this study, we systematically evaluated novel LF-based formulations designed to resist gastric conditions. We focused on complexes with succinylated sodium caseinate, low-methoxyl pectin, and whey protein hydrolysate, each combined with varying iron loadings. Static in vitro digestion was performed using the INFOGEST 2.0 protocol, and LF integrity was assessed by SDS-PAGE and LC-MS/MS. Unprotected LF was extensively hydrolyzed under these conditions. By contrast, ternary complexes of LF with sodium caseinate and pectin at high iron saturation, as well as binary LF-caseinate complexes with high levels of extrinsic iron, showed the highest stability. During intestinal digestion, highly iron-saturated ternary complexes of LF with sodium caseinate released the greatest amount of potential iron-binding peptides. These results indicated that specific LF-protein-polysaccharide-iron combinations are promising next-generation iron supplements and fortificants with improved tolerability and bioavailability.