A comparative study between tilapia (Oreochromis niloticus) by-product and tilapia protein hydrolysate on angiotensin I-converting enzyme (ACE) inhibition activities and functional properties
Tilapia is a popular freshwater fish and among the important cultured fish grown worldwide. In this study, fish protein hydrolysate was produced from tilapia (Oreochromis niloticus) by-product (TB) and tilapia muscle (TM) through enzymatic hydrolysis using alcalase. The TB and TM protein hydrolysate...
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| Format: | Article |
| Language: | English |
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Penerbit Universiti Kebangsaan Malaysia
2018
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| Online Access: | http://psasir.upm.edu.my/id/eprint/60475/1/A%20comparative%20study%20between%20tilapia%20%28Oreochromis%20niloticus%29%20by-product%20and%20tilapia%20protein%20hydrolysate%20on%20angiotensin%20I-converting%20enzyme%20%28ACE%29%20inhibition%20activities%20and%20functional%20properties.pdf |
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| author | Roslan, Jumardi Mustapa Kamal, Siti Mazlina Md. Yunos, Khairul Faezah Abdullah, Norhafizah |
| author_facet | Roslan, Jumardi Mustapa Kamal, Siti Mazlina Md. Yunos, Khairul Faezah Abdullah, Norhafizah |
| author_sort | Roslan, Jumardi |
| collection | UPM |
| description | Tilapia is a popular freshwater fish and among the important cultured fish grown worldwide. In this study, fish protein hydrolysate was produced from tilapia (Oreochromis niloticus) by-product (TB) and tilapia muscle (TM) through enzymatic hydrolysis using alcalase. The TB and TM protein hydrolysates were evaluated for its characteristics in terms of angiotensin I-converting enzyme (ACE) inhibition activity, peptide size distribution, and functional properties. Hydrolysis for 1 h for TB and TM successfully produced low molecular weight peptides (<14.2kDa) with the highest ACE inhibitory activities. The findings also demonstrated that both samples have high nitrogen solubility (>80% at pH2-9) and good emulsifying, water and oil holding capacities. The study indicated that tilapia protein hydrolysates have the potential to be used as functional food products. |
| first_indexed | 2024-03-06T09:38:17Z |
| format | Article |
| id | upm.eprints-60475 |
| institution | Universiti Putra Malaysia |
| language | English |
| last_indexed | 2024-03-06T09:38:17Z |
| publishDate | 2018 |
| publisher | Penerbit Universiti Kebangsaan Malaysia |
| record_format | dspace |
| spelling | upm.eprints-604752018-05-21T03:51:05Z http://psasir.upm.edu.my/id/eprint/60475/ A comparative study between tilapia (Oreochromis niloticus) by-product and tilapia protein hydrolysate on angiotensin I-converting enzyme (ACE) inhibition activities and functional properties Roslan, Jumardi Mustapa Kamal, Siti Mazlina Md. Yunos, Khairul Faezah Abdullah, Norhafizah Tilapia is a popular freshwater fish and among the important cultured fish grown worldwide. In this study, fish protein hydrolysate was produced from tilapia (Oreochromis niloticus) by-product (TB) and tilapia muscle (TM) through enzymatic hydrolysis using alcalase. The TB and TM protein hydrolysates were evaluated for its characteristics in terms of angiotensin I-converting enzyme (ACE) inhibition activity, peptide size distribution, and functional properties. Hydrolysis for 1 h for TB and TM successfully produced low molecular weight peptides (<14.2kDa) with the highest ACE inhibitory activities. The findings also demonstrated that both samples have high nitrogen solubility (>80% at pH2-9) and good emulsifying, water and oil holding capacities. The study indicated that tilapia protein hydrolysates have the potential to be used as functional food products. Penerbit Universiti Kebangsaan Malaysia 2018 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/60475/1/A%20comparative%20study%20between%20tilapia%20%28Oreochromis%20niloticus%29%20by-product%20and%20tilapia%20protein%20hydrolysate%20on%20angiotensin%20I-converting%20enzyme%20%28ACE%29%20inhibition%20activities%20and%20functional%20properties.pdf Roslan, Jumardi and Mustapa Kamal, Siti Mazlina and Md. Yunos, Khairul Faezah and Abdullah, Norhafizah (2018) A comparative study between tilapia (Oreochromis niloticus) by-product and tilapia protein hydrolysate on angiotensin I-converting enzyme (ACE) inhibition activities and functional properties. Sains Malaysiana, 47 (2). pp. 309-318. ISSN 0126-6039 http://www.ukm.my/jsm/english_journals/vol47num2_2018/contentsVol47num2_2018.html 10.17576/jsm-2018-4702–13 |
| spellingShingle | Roslan, Jumardi Mustapa Kamal, Siti Mazlina Md. Yunos, Khairul Faezah Abdullah, Norhafizah A comparative study between tilapia (Oreochromis niloticus) by-product and tilapia protein hydrolysate on angiotensin I-converting enzyme (ACE) inhibition activities and functional properties |
| title | A comparative study between tilapia (Oreochromis niloticus) by-product and tilapia protein hydrolysate on angiotensin I-converting enzyme (ACE) inhibition activities and functional properties |
| title_full | A comparative study between tilapia (Oreochromis niloticus) by-product and tilapia protein hydrolysate on angiotensin I-converting enzyme (ACE) inhibition activities and functional properties |
| title_fullStr | A comparative study between tilapia (Oreochromis niloticus) by-product and tilapia protein hydrolysate on angiotensin I-converting enzyme (ACE) inhibition activities and functional properties |
| title_full_unstemmed | A comparative study between tilapia (Oreochromis niloticus) by-product and tilapia protein hydrolysate on angiotensin I-converting enzyme (ACE) inhibition activities and functional properties |
| title_short | A comparative study between tilapia (Oreochromis niloticus) by-product and tilapia protein hydrolysate on angiotensin I-converting enzyme (ACE) inhibition activities and functional properties |
| title_sort | comparative study between tilapia oreochromis niloticus by product and tilapia protein hydrolysate on angiotensin i converting enzyme ace inhibition activities and functional properties |
| url | http://psasir.upm.edu.my/id/eprint/60475/1/A%20comparative%20study%20between%20tilapia%20%28Oreochromis%20niloticus%29%20by-product%20and%20tilapia%20protein%20hydrolysate%20on%20angiotensin%20I-converting%20enzyme%20%28ACE%29%20inhibition%20activities%20and%20functional%20properties.pdf |
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