Identification of angiotensin I converting enzyme inhibitory and radical scavenging bioactive peptides from sea cucumber (Stichopus vastus) collagen hydrolysates through optimization

The sea cucumber (Stichopus vastus) is an underutilized species, as most of its parts, including the integument (high collagen content) are thrown away during processing. The aim of this study was to investigate the effects of different hydrolysis conditions (substrate to enzyme ratio (S/E), re...

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Main Authors: Abedin, Md. Zainul, Karim, A. A., Gan, Chee-Yuen, Ghazali, F. C., Barzideh, Z., Zzaman, Wahidu, Sarker, Md. Zaidul Islam
Format: Article
Language:English
Published: Faculty of Food Science and Technology, Universiti Putra Malaysia 2015
Subjects:
Online Access:http://irep.iium.edu.my/43605/
http://irep.iium.edu.my/43605/
http://irep.iium.edu.my/43605/1/%2828%29.pdf
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spelling iium-436052015-07-03T08:09:48Z http://irep.iium.edu.my/43605/ Identification of angiotensin I converting enzyme inhibitory and radical scavenging bioactive peptides from sea cucumber (Stichopus vastus) collagen hydrolysates through optimization Abedin, Md. Zainul Karim, A. A. Gan, Chee-Yuen Ghazali, F. C. Barzideh, Z. Zzaman, Wahidu Sarker, Md. Zaidul Islam Q Science (General) T Technology (General) The sea cucumber (Stichopus vastus) is an underutilized species, as most of its parts, including the integument (high collagen content) are thrown away during processing. The aim of this study was to investigate the effects of different hydrolysis conditions (substrate to enzyme ratio (S/E), reaction temperature, and hydrolysis time) on the angiotensin I converting enzyme (ACE) inhibitory and radical scavenging (RSc) activities of the hydrolysates produced from trypsin hydrolysis of S. vastus collagen. Optimal conditions predicted by Box-Behnken Design modelling for producing ACE inhibitory and RSc hydrolysates were found to be S/E ratio (15), reaction temperature (55°C), and hydrolysis time (1 h). Under optimal conditions, ACE inhibitory and RSc activities were estimated to be as high as 67.8% and 77.9%, respectively. Besides, some novel bioactive peptides were identified through mass spectrometry analysis. These results indicate that S. vastus hydrolysates might be used as a functional ingredient in food and nutraceutical products. Faculty of Food Science and Technology, Universiti Putra Malaysia 2015 Article PeerReviewed application/pdf en http://irep.iium.edu.my/43605/1/%2828%29.pdf Abedin, Md. Zainul and Karim, A. A. and Gan, Chee-Yuen and Ghazali, F. C. and Barzideh, Z. and Zzaman, Wahidu and Sarker, Md. Zaidul Islam (2015) Identification of angiotensin I converting enzyme inhibitory and radical scavenging bioactive peptides from sea cucumber (Stichopus vastus) collagen hydrolysates through optimization. International Food Research Journal, 22 (3). pp. 1074-1082. ISSN 19854668 (P), 22317546 (O) http://www.ifrj.upm.edu.my/22%20%2803%29%202015/%2828%29.pdf
repository_type Digital Repository
institution_category Local University
institution International Islamic University Malaysia
building IIUM Repository
collection Online Access
language English
topic Q Science (General)
T Technology (General)
spellingShingle Q Science (General)
T Technology (General)
Abedin, Md. Zainul
Karim, A. A.
Gan, Chee-Yuen
Ghazali, F. C.
Barzideh, Z.
Zzaman, Wahidu
Sarker, Md. Zaidul Islam
Identification of angiotensin I converting enzyme inhibitory and radical scavenging bioactive peptides from sea cucumber (Stichopus vastus) collagen hydrolysates through optimization
description The sea cucumber (Stichopus vastus) is an underutilized species, as most of its parts, including the integument (high collagen content) are thrown away during processing. The aim of this study was to investigate the effects of different hydrolysis conditions (substrate to enzyme ratio (S/E), reaction temperature, and hydrolysis time) on the angiotensin I converting enzyme (ACE) inhibitory and radical scavenging (RSc) activities of the hydrolysates produced from trypsin hydrolysis of S. vastus collagen. Optimal conditions predicted by Box-Behnken Design modelling for producing ACE inhibitory and RSc hydrolysates were found to be S/E ratio (15), reaction temperature (55°C), and hydrolysis time (1 h). Under optimal conditions, ACE inhibitory and RSc activities were estimated to be as high as 67.8% and 77.9%, respectively. Besides, some novel bioactive peptides were identified through mass spectrometry analysis. These results indicate that S. vastus hydrolysates might be used as a functional ingredient in food and nutraceutical products.
format Article
author Abedin, Md. Zainul
Karim, A. A.
Gan, Chee-Yuen
Ghazali, F. C.
Barzideh, Z.
Zzaman, Wahidu
Sarker, Md. Zaidul Islam
author_facet Abedin, Md. Zainul
Karim, A. A.
Gan, Chee-Yuen
Ghazali, F. C.
Barzideh, Z.
Zzaman, Wahidu
Sarker, Md. Zaidul Islam
author_sort Abedin, Md. Zainul
title Identification of angiotensin I converting enzyme inhibitory and radical scavenging bioactive peptides from sea cucumber (Stichopus vastus) collagen hydrolysates through optimization
title_short Identification of angiotensin I converting enzyme inhibitory and radical scavenging bioactive peptides from sea cucumber (Stichopus vastus) collagen hydrolysates through optimization
title_full Identification of angiotensin I converting enzyme inhibitory and radical scavenging bioactive peptides from sea cucumber (Stichopus vastus) collagen hydrolysates through optimization
title_fullStr Identification of angiotensin I converting enzyme inhibitory and radical scavenging bioactive peptides from sea cucumber (Stichopus vastus) collagen hydrolysates through optimization
title_full_unstemmed Identification of angiotensin I converting enzyme inhibitory and radical scavenging bioactive peptides from sea cucumber (Stichopus vastus) collagen hydrolysates through optimization
title_sort identification of angiotensin i converting enzyme inhibitory and radical scavenging bioactive peptides from sea cucumber (stichopus vastus) collagen hydrolysates through optimization
publisher Faculty of Food Science and Technology, Universiti Putra Malaysia
publishDate 2015
url http://irep.iium.edu.my/43605/
http://irep.iium.edu.my/43605/
http://irep.iium.edu.my/43605/1/%2828%29.pdf
first_indexed 2023-09-18T21:02:08Z
last_indexed 2023-09-18T21:02:08Z
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