Purification and characterisation of angiotensin i converting enzyme (ACE) inhibitory peptides derived from enzymatic hydrolysate of ovotransferrin

Kaustav Majumder; Jianping Wu

doi:10.1016/j.foodchem.2010.12.039

Purification and characterisation of angiotensin i converting enzyme (ACE) inhibitory peptides derived from enzymatic hydrolysate of ovotransferrin

Kaustav Majumder, Jianping Wu

Research output: Contribution to journal › Article › peer-review

68 Scopus citations

Abstract

Three novel peptides, IQW, IRW and LKP, were predicted in our previous study in the thermolysin-pepsin ovotransferrin hydrolysate. The aims of the present study were to purify the peptides, and determine if the predicted peptides purified from the hydrolysate would have the same activity as the synthetic ones. We also determined the stability of the peptides under simulated gastrointestinal condition. IQW, IRW and LKP were then successfully purified from crude ovotransferrin hydrolysate through multi-step chromatographic purification comprising of cation exchange chromatography followed by three-step reverse-phase high performance liquid chromatography (RP-HPLC), and their sequences were analysed by UPLC-MS/MS. Our results showed that their activities were comparable to the synthetic ones. Simulated gastrointestinal incubation showed that IRW was degraded into a dipeptide of IR and a free amino acid of W by pancreatin, LKP was degraded into a dipeptide of KP and a free amino acid of L by mucosal peptidase, while IQW was stable against the digestive enzymes.

Original language	English (US)
Pages (from-to)	1614-1619
Number of pages	6
Journal	Food Chemistry
Volume	126
Issue number	4
DOIs	https://doi.org/10.1016/j.foodchem.2010.12.039
State	Published - Jun 15 2011
Externally published	Yes

Keywords

ACE inhibitory peptides
Inhibitory kinetics
Ovotransferrin
Purification
Stability

ASJC Scopus subject areas

Analytical Chemistry
Food Science

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title = "Purification and characterisation of angiotensin i converting enzyme (ACE) inhibitory peptides derived from enzymatic hydrolysate of ovotransferrin",

abstract = "Three novel peptides, IQW, IRW and LKP, were predicted in our previous study in the thermolysin-pepsin ovotransferrin hydrolysate. The aims of the present study were to purify the peptides, and determine if the predicted peptides purified from the hydrolysate would have the same activity as the synthetic ones. We also determined the stability of the peptides under simulated gastrointestinal condition. IQW, IRW and LKP were then successfully purified from crude ovotransferrin hydrolysate through multi-step chromatographic purification comprising of cation exchange chromatography followed by three-step reverse-phase high performance liquid chromatography (RP-HPLC), and their sequences were analysed by UPLC-MS/MS. Our results showed that their activities were comparable to the synthetic ones. Simulated gastrointestinal incubation showed that IRW was degraded into a dipeptide of IR and a free amino acid of W by pancreatin, LKP was degraded into a dipeptide of KP and a free amino acid of L by mucosal peptidase, while IQW was stable against the digestive enzymes.",

keywords = "ACE inhibitory peptides, Inhibitory kinetics, Ovotransferrin, Purification, Stability",

author = "Kaustav Majumder and Jianping Wu",

note = "Funding Information: This work was supported by grants from Natural Sciences and Engineering Research Council of Canada (NSERC) and Alberta Livestock Industry Development Fund Inc., (ALIDF, now Alberta Livestock Meat Agency) to J. Wu and a Poultry Research Centre Graduate Assistant Scholarship to K. Majumder. We are thankful to Neova Technologies Inc., (Abbotsford, BC, Canada) for providing ovotransferrin.",

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doi = "10.1016/j.foodchem.2010.12.039",

language = "English (US)",

volume = "126",

pages = "1614--1619",

journal = "Food Chemistry",

issn = "0308-8146",

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T1 - Purification and characterisation of angiotensin i converting enzyme (ACE) inhibitory peptides derived from enzymatic hydrolysate of ovotransferrin

AU - Majumder, Kaustav

AU - Wu, Jianping

N1 - Funding Information: This work was supported by grants from Natural Sciences and Engineering Research Council of Canada (NSERC) and Alberta Livestock Industry Development Fund Inc., (ALIDF, now Alberta Livestock Meat Agency) to J. Wu and a Poultry Research Centre Graduate Assistant Scholarship to K. Majumder. We are thankful to Neova Technologies Inc., (Abbotsford, BC, Canada) for providing ovotransferrin.

PY - 2011/6/15

Y1 - 2011/6/15

N2 - Three novel peptides, IQW, IRW and LKP, were predicted in our previous study in the thermolysin-pepsin ovotransferrin hydrolysate. The aims of the present study were to purify the peptides, and determine if the predicted peptides purified from the hydrolysate would have the same activity as the synthetic ones. We also determined the stability of the peptides under simulated gastrointestinal condition. IQW, IRW and LKP were then successfully purified from crude ovotransferrin hydrolysate through multi-step chromatographic purification comprising of cation exchange chromatography followed by three-step reverse-phase high performance liquid chromatography (RP-HPLC), and their sequences were analysed by UPLC-MS/MS. Our results showed that their activities were comparable to the synthetic ones. Simulated gastrointestinal incubation showed that IRW was degraded into a dipeptide of IR and a free amino acid of W by pancreatin, LKP was degraded into a dipeptide of KP and a free amino acid of L by mucosal peptidase, while IQW was stable against the digestive enzymes.

AB - Three novel peptides, IQW, IRW and LKP, were predicted in our previous study in the thermolysin-pepsin ovotransferrin hydrolysate. The aims of the present study were to purify the peptides, and determine if the predicted peptides purified from the hydrolysate would have the same activity as the synthetic ones. We also determined the stability of the peptides under simulated gastrointestinal condition. IQW, IRW and LKP were then successfully purified from crude ovotransferrin hydrolysate through multi-step chromatographic purification comprising of cation exchange chromatography followed by three-step reverse-phase high performance liquid chromatography (RP-HPLC), and their sequences were analysed by UPLC-MS/MS. Our results showed that their activities were comparable to the synthetic ones. Simulated gastrointestinal incubation showed that IRW was degraded into a dipeptide of IR and a free amino acid of W by pancreatin, LKP was degraded into a dipeptide of KP and a free amino acid of L by mucosal peptidase, while IQW was stable against the digestive enzymes.

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KW - Purification

KW - Stability

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Purification and characterisation of angiotensin i converting enzyme (ACE) inhibitory peptides derived from enzymatic hydrolysate of ovotransferrin

Abstract

Keywords

ASJC Scopus subject areas

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