Purification of angiotensin I-converting enzyme inhibitory peptides from a cowpea (Vigna unguiculata) enzymatic hydrolysate (original) (raw)

2011, Process Biochemistry

Chuan Sheih et al. 2009). ACE plays an important physiological role in regulating blood pressure by converting angiotensin I into angiotensin II, a vasoconstrictor, and degrading bradykinin, a vasodilator. ACE inhibitory peptides can decrease blood pressure by inhibiting ACE and, have been isolated from enzymatic digest of various food materials, including casein, sake, sour milk, fish proteins, and plant proteins (Hernández-Ledesma et al. 2011). ACE inhibitory peptides derived from food proteins are usually purified using several chromatographic steps that include size exclusion, ionic exchange, and RP-HPLC chromatography. Affinity chromatography is a powerful purification method for protein and bioactive peptides. It is based on the use of specific ligands to absorb the desired substances on solid supports and to elute them from the support (Megías et al. 2006). Recently, the purification of ACE inhibitory peptides using ACE immobilized and immobilized metal ion affinity chromatography (IMAC) have been reported (Megías et al. 2009; Lan et al. 2015). The aim of our work was to obtain ACE inhibitory peptides from casein hydrolysate. The affinity purification of ACE inhibitory peptides using IMAC with immobilized Ni 2+ is described and a novel ACE inhibitory peptide was isolated by further HPLC purification. Materials and methods Materials Papain (with a declared activity of 500,000 U/g) was kindly provided by Nanning Pangbo Biological Engineering Co., Ltd. (China). ACE from rabbit lung (2.0 units/mg of protein) and hippuryl-l-histidyl-l-leucine (HHL) were purchased from the Sigma Chemical Company (USA). Casein,

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