PURIFICATION AND CHARACTERISATION OF ANGIOTENSIN I CONVERTING ENZYME (ACE) INHIBITORY PEPTIDE FROM BLOOD COCKLE (Anadara granosa) MEAT HYDROLYSATE

AISHAH  SUHAIMI; AMIZA  MAT AMIN; NORIZAH  MHD SARBON; MOHD EFFENDY  ABD. WAHID; ZALIHA HARUN

doi:10.55230/mabjournal.v49i1.1649

Authors

AISHAH SUHAIMI School of Food Science and Technology, Universiti Malaysia Terengganu, 21030 Kuala Nerus, Terengganu, Malaysia
AMIZA MAT AMIN
ama@umt.edu.my
School of Food Science and Technology, Universiti Malaysia Terengganu, 21030 Kuala Nerus, Terengganu, Malaysia
NORIZAH MHD SARBON School of Food Science and Technology, Universiti Malaysia Terengganu, 21030 Kuala Nerus, Terengganu, Malaysia
MOHD EFFENDY ABD. WAHID School of Fisheries and Aquaculture Sciences, Universiti Malaysia Terengganu, 21030 Kuala Nerus, Terengganu, Malaysia
ZALIHA HARUN School of Food Science and Technology, Universiti Malaysia Terengganu, 21030 Kuala Nerus, Terengganu, Malaysia

Keywords:

Blood cockle, angiotensin converting enzyme, peptide, hydrolysis

Abstract

Blood cockle (Anadara granosa) is the most abundant and available bivalves in Malaysia. Blood cockles meat has high protein content and has potential to generate bioactive peptides. To date, no study has been reported on purification and identification of angiotensin I converting enzyme (ACE) inhibitory peptides from blood cockle meat. Thus, the objectives of this study were to purify and characterize ACE inhibitory peptide from blood cockle meat hydrolysate. ACE inhibitory peptides from blood cockle meat hydrolysate (CMH) were prepared by enzymatic protein hydrolysis using Protamex®. Crude CMH was characterized for its stability against gastrointestinal proteases, at varying pH (2–11) and temperature (4–90°C). Next, crude CMH was purified by ultrafiltration, ion exchange chromatography and reverse-phase chromatography and its amino acid sequence was identified. It was found that crude CMH was highly stable at low pH and temperature, and was resistant to gastrointestinal proteases (pepsin and trypsin). A three-step purification increased the inhibitory activity of CMH, reducing its IC₅₀ from 0.35 mg/ml to 0.0094 mg/ml. The amino acid sequence of the purified peptide was determined as VNDLLSGSFKHFLY, with a molecular weight of 1621.88 Da. This study suggested the potential of ACE inhibitory peptide derived from cockle meat as a nutraceutical ingredient in functional food

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