Purification and characterisation of a novel angiotensin-I converting enzyme (ACE)-inhibitory peptide derived from the enzymatic hydrolysate of Enteromorpha clathrata protein

Saikun Pan; Shujun Wang; Lingling Jing; Dongrui Yao

doi:10.1016/j.foodchem.2016.05.087

Purification and characterisation of a novel angiotensin-I converting enzyme (ACE)-inhibitory peptide derived from the enzymatic hydrolysate of Enteromorpha clathrata protein

Food Chem. 2016 Nov 15:211:423-30. doi: 10.1016/j.foodchem.2016.05.087. Epub 2016 May 13.

Authors

Saikun Pan¹, Shujun Wang², Lingling Jing³, Dongrui Yao⁴

Affiliations

¹ Jiangsu Marine Resources Development Research Institute, Lianyungang, Jiangsu 222005, China; School of Marine Science and Technology, Huaihai Institute of Technology, 59 Cangwu Road, Xinpu 222005, China; Jiangsu Key Laboratory of Marine Pharmaceutical Compound Screening, Huaihai Institute of Technology, Lianyungang 222005, China; Co-Innovation Center of Jiangsu Marine Bio-industry Technology, Huaihai Institute of Technology, Lianyungang 222005, China. Electronic address: pskgx@yahoo.com.cn.
² Jiangsu Marine Resources Development Research Institute, Lianyungang, Jiangsu 222005, China; School of Marine Science and Technology, Huaihai Institute of Technology, 59 Cangwu Road, Xinpu 222005, China; Jiangsu Key Laboratory of Marine Pharmaceutical Compound Screening, Huaihai Institute of Technology, Lianyungang 222005, China; Co-Innovation Center of Jiangsu Marine Bio-industry Technology, Huaihai Institute of Technology, Lianyungang 222005, China.
³ School of Marine Science and Technology, Huaihai Institute of Technology, 59 Cangwu Road, Xinpu 222005, China.
⁴ Institute of Botany, Jiangsu Province and Chinese Academy of Sciences, 1 Qianhu Houcun, Zhongshanmen Wai, Nanjing 210014, China.

PMID: 27283651
DOI: 10.1016/j.foodchem.2016.05.087

Abstract

Hydrolysates containing angiotensin-I converting enzyme (ACE)-inhibitory peptide were prepared from Enteromorpha clathrata protein using alcalase. The hydrolysates were fractionated into two molecular-weight ranges (below and above 10kDa) by ultrafiltration. The below-10kDa fraction showed higher ACE-inhibitory activity and was subsequently purified by Sephadex G-15 gel filtration chromatography. The structure of active peptide was identified as Pro-Ala-Phe-Gly by HPLC-Q-TOF-MS and its IC50 value was 35.9μM. The yield of this peptide from E. clathrata protein was 0.82%. Lineweaver-Burk plots demonstrated that the inhibitory kinetic mechanism of this peptide was non-competitive. Stability study revealed that the purified peptide showed resistance against gastrointestinal proteases. Thus, E. clathrata protein hydrolysate treated with alcalase is a beneficial ingredient of nutraceuticals and pharmaceuticals against hypertension and related diseases.

Keywords: ACE-inhibitory peptide; Enteromorpha clathrata; Protein hydrolysate; Purification and characterisation.

MeSH terms

Angiotensin-Converting Enzyme Inhibitors / chemistry
Angiotensin-Converting Enzyme Inhibitors / isolation & purification*
Chromatography, Gel
Inhibitory Concentration 50
Molecular Weight
Oligopeptides / chemistry
Oligopeptides / isolation & purification
Peptide Hydrolases / metabolism
Plant Proteins / chemistry
Plant Proteins / isolation & purification*
Protein Hydrolysates / chemistry
Protein Hydrolysates / isolation & purification*
Ulva / chemistry*

Substances

Angiotensin-Converting Enzyme Inhibitors
Oligopeptides
Plant Proteins
Protein Hydrolysates
Peptide Hydrolases