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

International Journal of Molecular Sciences

Jauricque Ursulla Kongo-Dia-Moukala²  Hui Zhang¹ 

[1] State Key Laboratory of Food Science and Technology, Jiangnan University, Lihu Road 1800, Wuxi 214122, Jiangsu, China;

关键词: defatted corn protein;    enzymatic hydrolysis;    Flavourzyme hydrolysate;    bile acid binding capacity;   

DOI  :  10.3390/ijms12021066

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2011 by the authors; licensee MDPI, Basel, Switzerland.