08.20.24
Effera, a form of lactoferrin brought to market by Helaina which is a human equivalent, may be more digestible and tolerated than bovine-sourced lactoferrin, according to a new study which tested both types of the colostrum protein in a simulated model of human digestion.
Lactoferrin is an abundant protein found in both human and bovine colostrum, and it is also produced endogenously throughout the body. Lactoferrin is thought to play roles in iron metabolism, providing prebiotic properties, and influencing innate and adaptive immune response.
There are key differences between human and bovine lactoferrin, such as amino acid composition and glycosylation, which may have an influence over its activity.
In the new study, researchers assessed the differences between Effera, the human-equivalent lactoferrin which is produced by yeast, against both bovine lactoferrin and human-sourced lactoferrin, in validated in vitro digestion protocols. Each of the three lactoferrin types was assessed with both high and low levels of iron saturation, to assess how lactoferrin’s iron-binding activity could impact its digestibility.
Researchers were able to determine the extent of intact protein retention, and the profile of peptides released by all three forms across simulated gastric and intestinal digestion through gel electrophoresis, ELISA, and LC-MS.
Intact lactoferrin retention across digestion was similar across all three lactoferrin types, but the human-sourced lactoferrin with high iron saturation had the strongest protein retention in simulated gastric fluid than all other types. Peptides in the digested human lactoferrin had strong similarity to Effera, where digested bovine lactoferrin samples were significantly different.
Because Effera is so much more similar to human lactoferrin than bovine-sourced lactoferrin, it may better mimic the effects of the human variety when digested, the authors of the study noted. However, more research on its safety profile, in vivo digestion, and comparison of peptide activity across digestion will be needed.
Lactoferrin is an abundant protein found in both human and bovine colostrum, and it is also produced endogenously throughout the body. Lactoferrin is thought to play roles in iron metabolism, providing prebiotic properties, and influencing innate and adaptive immune response.
There are key differences between human and bovine lactoferrin, such as amino acid composition and glycosylation, which may have an influence over its activity.
In the new study, researchers assessed the differences between Effera, the human-equivalent lactoferrin which is produced by yeast, against both bovine lactoferrin and human-sourced lactoferrin, in validated in vitro digestion protocols. Each of the three lactoferrin types was assessed with both high and low levels of iron saturation, to assess how lactoferrin’s iron-binding activity could impact its digestibility.
Researchers were able to determine the extent of intact protein retention, and the profile of peptides released by all three forms across simulated gastric and intestinal digestion through gel electrophoresis, ELISA, and LC-MS.
Intact lactoferrin retention across digestion was similar across all three lactoferrin types, but the human-sourced lactoferrin with high iron saturation had the strongest protein retention in simulated gastric fluid than all other types. Peptides in the digested human lactoferrin had strong similarity to Effera, where digested bovine lactoferrin samples were significantly different.
Because Effera is so much more similar to human lactoferrin than bovine-sourced lactoferrin, it may better mimic the effects of the human variety when digested, the authors of the study noted. However, more research on its safety profile, in vivo digestion, and comparison of peptide activity across digestion will be needed.
