Nutritional composition and angiotensin-converting enzyme inhibitory activity of blue lupin (Lupinus angustifolius L.)

Angiotensin-converting enzyme (ACE) plays a dominant role in blood pressure regulating system. Synthetic ACE inhibitor is designed as an antihypertensive drug to restrict ACE activity. However, the usage of synthetic drug may cause several adverse effects. Hence, a natural food protein with ACE i...

Full description

Saved in:

Bibliographic Details
Main Author:	Chin, Ying Yee
Format:	Thesis
Language:	English
Published:	2017
Subjects:	Angiotensin - Converting Enzyme Inhibitors Enzyme Activators
Online Access:	http://psasir.upm.edu.my/id/eprint/79334/1/FPSK%28m%29%202019%2014%20ir.pdf
Tags:	Add Tag No Tags, Be the first to tag this record!

id	my-upm-ir.79334
record_format	uketd_dc
spelling	my-upm-ir.793342022-01-12T02:32:25Z Nutritional composition and angiotensin-converting enzyme inhibitory activity of blue lupin (Lupinus angustifolius L.) 2017-09 Chin, Ying Yee Angiotensin-converting enzyme (ACE) plays a dominant role in blood pressure regulating system. Synthetic ACE inhibitor is designed as an antihypertensive drug to restrict ACE activity. However, the usage of synthetic drug may cause several adverse effects. Hence, a natural food protein with ACE inhibitory activity may be promising as a safer alternative to the synthetic drug. Blue lupin (Lupinus angustifolius) is one of the legumes that rich in protein. It has the potential to be a good source of ACE inhibitory peptides. However, blue lupin is usually served as an animal feed and consumption by human is rare. Therefore, this study was carried out to investigate the nutritional, protein and amino acid composition of blue lupin flour, and to evaluate the ACE inhibitory activity of its protein hydrolysates. The results revealed that the lupin flour was abundant in protein (43.3 g/100 g) and dietary fibre (33.5 g/100 g). According to the Osborne classification, plant storage protein was characterised into four categories based on their solubility in different solvents. Results from sequential Osborne extraction procedure showed that lupin protein comprised of 46% salt-soluble globulin, 27% water-soluble albumin, 18% alkaline-soluble glutelin and 7% alcohol-soluble prolamin fractions. Furthermore, lupin protein was rich in lysine but limiting in methionine. In this study, Alcalase and Flavourzyme were used to hydrolyse the lupin protein isolate for different hydrolysis times (4, 10 and 16 h). Gel electrophoresis analysis demonstrated that protein hydrolysis catalysed by Alcalase was more effective compared with Flavourzyme as evidenced by the lower molecular weight peptides presented in the hydrolysates prepared using Alcalase. The ACE inhibitory activity of hydrolysates was determined using an in vitro method. Hydrolysates prepared using Alcalase exhibited higher ACE inhibitory activities compared with those prepared using Flavourzyme, showing IC50 values ranging from 0.10 to 0.21 mg/mL. However, there was no significant difference in IC50 values between the hydrolysates prepared using Alcalase for 4, 10 and 16 h of hydrolysis times. The results suggested that globulin was the major contributing protein fraction on ACE inhibitory effect in lupin protein. In addition, the information obtained in this study is important to reveal the nutritional values and health benefits of blue lupin protein and to recognise the lupin protein hydrolysates as nutraceuticals or functional foods. The lupin protein hydrolysates with potent ACE inhibitory activities can be incorporated into the daily diet to prevent hypertension. They can also be consumed by hypertensive patients to reduce the dosage of antihypertensive drugs needed, thereby lowering the risk of side effects. Angiotensin - Converting Enzyme Inhibitors Enzyme Activators 2017-09 Thesis http://psasir.upm.edu.my/id/eprint/79334/ http://psasir.upm.edu.my/id/eprint/79334/1/FPSK%28m%29%202019%2014%20ir.pdf text en public masters Universiti Putra Malaysia Angiotensin - Converting Enzyme Inhibitors Enzyme Activators Ismail, Amin
institution	Universiti Putra Malaysia
collection	PSAS Institutional Repository
language	English
advisor	Ismail, Amin
topic	Angiotensin - Converting Enzyme Inhibitors Enzyme Activators
spellingShingle	Angiotensin - Converting Enzyme Inhibitors Enzyme Activators Chin, Ying Yee Nutritional composition and angiotensin-converting enzyme inhibitory activity of blue lupin (Lupinus angustifolius L.)
description	Angiotensin-converting enzyme (ACE) plays a dominant role in blood pressure regulating system. Synthetic ACE inhibitor is designed as an antihypertensive drug to restrict ACE activity. However, the usage of synthetic drug may cause several adverse effects. Hence, a natural food protein with ACE inhibitory activity may be promising as a safer alternative to the synthetic drug. Blue lupin (Lupinus angustifolius) is one of the legumes that rich in protein. It has the potential to be a good source of ACE inhibitory peptides. However, blue lupin is usually served as an animal feed and consumption by human is rare. Therefore, this study was carried out to investigate the nutritional, protein and amino acid composition of blue lupin flour, and to evaluate the ACE inhibitory activity of its protein hydrolysates. The results revealed that the lupin flour was abundant in protein (43.3 g/100 g) and dietary fibre (33.5 g/100 g). According to the Osborne classification, plant storage protein was characterised into four categories based on their solubility in different solvents. Results from sequential Osborne extraction procedure showed that lupin protein comprised of 46% salt-soluble globulin, 27% water-soluble albumin, 18% alkaline-soluble glutelin and 7% alcohol-soluble prolamin fractions. Furthermore, lupin protein was rich in lysine but limiting in methionine. In this study, Alcalase and Flavourzyme were used to hydrolyse the lupin protein isolate for different hydrolysis times (4, 10 and 16 h). Gel electrophoresis analysis demonstrated that protein hydrolysis catalysed by Alcalase was more effective compared with Flavourzyme as evidenced by the lower molecular weight peptides presented in the hydrolysates prepared using Alcalase. The ACE inhibitory activity of hydrolysates was determined using an in vitro method. Hydrolysates prepared using Alcalase exhibited higher ACE inhibitory activities compared with those prepared using Flavourzyme, showing IC50 values ranging from 0.10 to 0.21 mg/mL. However, there was no significant difference in IC50 values between the hydrolysates prepared using Alcalase for 4, 10 and 16 h of hydrolysis times. The results suggested that globulin was the major contributing protein fraction on ACE inhibitory effect in lupin protein. In addition, the information obtained in this study is important to reveal the nutritional values and health benefits of blue lupin protein and to recognise the lupin protein hydrolysates as nutraceuticals or functional foods. The lupin protein hydrolysates with potent ACE inhibitory activities can be incorporated into the daily diet to prevent hypertension. They can also be consumed by hypertensive patients to reduce the dosage of antihypertensive drugs needed, thereby lowering the risk of side effects.
format	Thesis
qualification_level	Master's degree
author	Chin, Ying Yee
author_facet	Chin, Ying Yee
author_sort	Chin, Ying Yee
title	Nutritional composition and angiotensin-converting enzyme inhibitory activity of blue lupin (Lupinus angustifolius L.)
title_short	Nutritional composition and angiotensin-converting enzyme inhibitory activity of blue lupin (Lupinus angustifolius L.)
title_full	Nutritional composition and angiotensin-converting enzyme inhibitory activity of blue lupin (Lupinus angustifolius L.)
title_fullStr	Nutritional composition and angiotensin-converting enzyme inhibitory activity of blue lupin (Lupinus angustifolius L.)
title_full_unstemmed	Nutritional composition and angiotensin-converting enzyme inhibitory activity of blue lupin (Lupinus angustifolius L.)
title_sort	nutritional composition and angiotensin-converting enzyme inhibitory activity of blue lupin (lupinus angustifolius l.)
granting_institution	Universiti Putra Malaysia
publishDate	2017
url	http://psasir.upm.edu.my/id/eprint/79334/1/FPSK%28m%29%202019%2014%20ir.pdf
_version_	1747813317051678720

Nutritional composition and angiotensin-converting enzyme inhibitory activity of blue lupin (Lupinus angustifolius L.)

Similar Items