In Vitro Binding Capacity of Bile Acids by Defatted Corn Protein Hydrolysate

Jauricque Ursulla Kongo-Dia-Moukala,Hui Zhang,Pierre Claver Irakoze

doi:10.3390/ijms12021066

Abstract

Defatted corn protein was digested using five different proteases, Alcalase, Trypsin, Neutrase, Protamex and Flavourzyme, in order to produce bile acid binding peptides. Bile acid binding capacity was analyzed in vitro using peptides from different proteases of defatted corn hydrolysate. Some crystalline bile acids like sodium glycocholate, sodium cholate and sodium deoxycholate were individually tested using HPLC to see which enzymes can release more peptides with high bile acid binding capacity. Peptides from Flavourzyme defatted corn hydrolysate exhibited significantly (p < 0.05) stronger bile acid binding capacity than all others hydrolysates tested and all crystalline bile acids tested were highly bound by cholestyramine, a positive control well known as a cholesterol-reducing agent. The bile acid binding capacity of Flavourzyme hydrolysate was almost preserved after gastrointestinal proteases digestion. The molecular weight of Flavourzyme hydrolysate was determined and most of the peptides were found between 500-180 Da. The results showed that Flavourzyme hydrolysate may be used as a potential cholesterol-reducing agent.

Highlights

Protein is a food substance essentially required by the body that cannot be substituted by other compounds in the whole body tissues for its nitrogen contents; it must be provided in food
All the curves showed a high rate of enzymatic hydrolysis during the first 15 min and the rate of hydrolysis gradually declined with time
This study demonstrated that bile acid binding peptides can be generated from defatted corn protein by enzymatic hydrolysis

Summary

Introduction

Protein is a food substance essentially required by the body that cannot be substituted by other compounds in the whole body tissues for its nitrogen contents; it must be provided in food. Each corn variety contains a different amount of protein of differing quality. Protein quality is determined by the protein concentration and its amino acid patterns, and each cereal has a different amino acid composition [2]. A byproduct of the corn oil industry, is rich in proteins, minerals and B-group vitamins, and has a balanced amino acid composition, the content of lysine; sulfur-containing amino acids and tryptophan are equivalent to those proposed by WHO/FAO for reference protein [3,4,5]. Peptides derived from in vivo digestion of whole proteins by hydrolyzation with bacterial proteases before ingestion have been reported to carry specific bioactivities. The identification and synthesis of these bioactive peptides has received considerable attention in recent years [6,7,8]

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