Fermentation of hemp seed proteins leads to formation of peptides that share sequence similarity with human vitamin D-binding protein

Stefania Pacini,Marco Ruggiero

doi:10.15761/mri.1000170

Abstract

Fermentation of hemp seed proteins leads to formation of peptides that share sequence similarity with human vitamin D-binding protein

Highlights

Vitamin D-binding protein-derived Macrophage Activating Factor (DBP-MAF or Gc-protein-derived MAF) and its conceptual derivative based on microbial chondroitin sulfate, proved effective in a number of conditions characterized by immune system and mitochondrial dysfunction thanks to their effects on the pathogenetic alterations that are common to chronic conditions [1,2,3,4,5,6,7,8,9]
The protein/peptide content from the fermented hemp seed protein extract added to each well containing 2,500 cells was calculated as 0.6 μg/well, an amount that is of the same order of magnitude as that used by Gregory et al to assess the effects of DBP-MAF on transformed prostate cell proliferation and migration [10]
Edestin is an hexameric globular protein that bears striking functional resemblance to the human vitamin D-binding protein that is the precursor of DBP-MAF (Fig. 1)

Summary

Introduction

Vitamin D-binding protein-derived Macrophage Activating Factor (DBP-MAF or Gc-protein-derived MAF) and its conceptual derivative based on microbial chondroitin sulfate, proved effective in a number of conditions characterized by immune system and mitochondrial dysfunction thanks to their effects on the pathogenetic alterations that are common to chronic conditions [1,2,3,4,5,6,7,8,9]. We demonstrate that fermentation of hemp seed proteins utilizing an ad hoc designed microbial formula l eads to formation of peptides endowed with biological activity similar to that of DBP-MAF. The process of fermentation of hemp seed protein extract was performed in Switzerland using the following materials: Mineral water (France).

Results

Conclusion