Optimization and characterization of angiotensin converting enzyme (ACE) inhibitory peptide from blood cockle (anadara granosa) hydrolysate

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dc.contributor.authorAishah Suhaimi
dc.date.accessioned2019-11-27T02:42:03Z
dc.date.available2019-11-27T02:42:03Z
dc.date.issued2017-05
dc.description.abstractiii Abstract of thesis presented to the Senate of Universiti Malaysia Terengganu in fulfilment of the requirement for the degree of Master of Science. OPTIMIZATION AND CHARACTERIZATION OF ANGIOTENSIN CONVERTING ENZYME (ACE) INHIBITORY PEPTIDE FROM BLOOD COCKLE (Anadara granosa) HYDROLYSATE AISHAH BINTI SUHAIMI May 2017 Main Supervisor : Associate Professor Amiza Mat Amin, Ph.D. Co-Supervisor : Norizah Mhd Sarbon, Ph.D. : Professor Mohd Effendy Abd. Wahid, Ph.D. School : School of Food Science and Technology This study reported on the optimization and characterization of angiotensin converting enzyme (ACE) inhibitory peptide from blood cockle hydrolysate. Firstly, preliminary screening of commercial proteinases was carried out to select the most appropriate proteinase and hydrolysis time (0-8 hrs) to prepare the highest ACE inhibitory activity. It was found that ProtamexTM gave the highest ACE inhibitory activity at 6 hours hydrolysis time as compared to Alcalase®, Neutrase®, pepsin, papain, trypsin and α-chymotrypsin. Next, further optimization of enzymatic hydrolysis condition (i.e. hydrolysis time, pH, hydrolysis temperature and enzyme to substrate (E/S) ratio) of blood cockle with ProtamexTM using a central composite design (face-centered) was employed to obtain maximum ACE inhibitory activity.en_US
dc.identifier.urihttps://umt-ir.umt.edu.my/xmlui/handle/123456789/14228
dc.language.isoenen_US
dc.publisherUniversiti Malaysia Terengganuen_US
dc.subjectAngiotensin-converting enzymeen_US
dc.subjectQP 609 .A53 A3 2017en_US
dc.titleOptimization and characterization of angiotensin converting enzyme (ACE) inhibitory peptide from blood cockle (anadara granosa) hydrolysateen_US
dc.typeThesisen_US
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