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

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dc.contributor.author Aishah Suhaimi
dc.date.accessioned 2019-11-27T02:42:03Z
dc.date.available 2019-11-27T02:42:03Z
dc.date.issued 2017-05
dc.identifier.uri http://umt-ir.umt.edu.my:8080/xmlui/handle/123456789/14228
dc.description.abstract iii 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.language.iso en en_US
dc.publisher Universiti Malaysia Terengganu en_US
dc.subject Angiotensin-converting enzyme en_US
dc.subject QP 609 .A53 A3 2017 en_US
dc.title Optimization and characterization of angiotensin converting enzyme (ACE) inhibitory peptide from blood cockle (anadara granosa) hydrolysate en_US
dc.type Thesis en_US


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