Purification and characterisation of angiotensin I converting enzyme (ACE) inhibitory peptide from blood cockle (Anadara granosa) meat hydrolysate
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) inhi...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Penerbit Universiti Kebangsaan Malaysia
2020
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| Online Access: | http://journalarticle.ukm.my/15695/ http://journalarticle.ukm.my/15695/1/49_01_02.pdf |
| _version_ | 1848813861921095680 |
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| author | Aishah Suhaimi, Amiza Mat Amin, Norizah Mhd Sarbon, Mohd Effendy Abd. Wahid, Zaliha Harun, |
| author_facet | Aishah Suhaimi, Amiza Mat Amin, Norizah Mhd Sarbon, Mohd Effendy Abd. Wahid, Zaliha Harun, |
| author_sort | Aishah Suhaimi, |
| building | UKM Institutional Repository |
| collection | Online Access |
| description | 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. |
| first_indexed | 2025-11-15T00:24:55Z |
| format | Article |
| id | oai:generic.eprints.org:15695 |
| institution | Universiti Kebangasaan Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T00:24:55Z |
| publishDate | 2020 |
| publisher | Penerbit Universiti Kebangsaan Malaysia |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | oai:generic.eprints.org:156952020-11-16T11:08:58Z http://journalarticle.ukm.my/15695/ 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, 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. Penerbit Universiti Kebangsaan Malaysia 2020 Article PeerReviewed application/pdf en http://journalarticle.ukm.my/15695/1/49_01_02.pdf Aishah Suhaimi, and Amiza Mat Amin, and Norizah Mhd Sarbon, and Mohd Effendy Abd. Wahid, and Zaliha Harun, (2020) Purification and characterisation of angiotensin I converting enzyme (ACE) inhibitory peptide from blood cockle (Anadara granosa) meat hydrolysate. Malaysian Applied Biology, 49 (1). pp. 13-21. ISSN 0126-8643 http://www.mabjournal.com/index.php?option=com_content&view=article&id=981&catid=59:current-view&Itemid=56 |
| spellingShingle | Aishah Suhaimi, Amiza Mat Amin, Norizah Mhd Sarbon, Mohd Effendy Abd. Wahid, Zaliha Harun, Purification and characterisation of angiotensin I converting enzyme (ACE) inhibitory peptide from blood cockle (Anadara granosa) meat hydrolysate |
| title | Purification and characterisation of angiotensin I converting enzyme (ACE) inhibitory peptide from blood cockle (Anadara granosa) meat hydrolysate |
| title_full | Purification and characterisation of angiotensin I converting enzyme (ACE) inhibitory peptide from blood cockle (Anadara granosa) meat hydrolysate |
| title_fullStr | Purification and characterisation of angiotensin I converting enzyme (ACE) inhibitory peptide from blood cockle (Anadara granosa) meat hydrolysate |
| title_full_unstemmed | Purification and characterisation of angiotensin I converting enzyme (ACE) inhibitory peptide from blood cockle (Anadara granosa) meat hydrolysate |
| title_short | Purification and characterisation of angiotensin I converting enzyme (ACE) inhibitory peptide from blood cockle (Anadara granosa) meat hydrolysate |
| title_sort | purification and characterisation of angiotensin i converting enzyme (ace) inhibitory peptide from blood cockle (anadara granosa) meat hydrolysate |
| url | http://journalarticle.ukm.my/15695/ http://journalarticle.ukm.my/15695/ http://journalarticle.ukm.my/15695/1/49_01_02.pdf |