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Activity and purification of ACE inhibitory peptides from animal by-products: in vitro and in vivo evaluation

Griet Herregods (UGent)
(2011)
Author
Promoter
Guy Smagghe and John Van Camp
Organization
Abstract
Hypertension or high blood pressure is a major risk factor for cardiovascular diseases, which are the leading cause of death in the Western world. Next to lifestyle modifications, including smoke cessation, exercise, stress management and a healthy diet, functional foods containing angiotensin I-converting enzyme (ACE)-inhibitory peptides can play a role in the prevention of hypertension. ACE (EC 3.4.15.1) plays a key role in different blood pressure-regulating mechanisms, including the renin-angiotensin-aldosteron-system (RAAS) and the kallikrein-kinin-system (KKS), where its action results in an overall increase in blood pressure. Thus, peptides or protein hydrolysates with ACE-inhibitory activity have a blood pressure-lowering effect. In this project, the potential of different protein hydrolysates for the development of an antihypertensive functional food was investigated. Two main sections can be distinguished, the ACE-inhibitory and antihypertensive activity of gelatin hydrolysates was evaluated on the one hand, and a peptic hydrolysate of an animal by-product and its derivatives were investigated for blood pressure-lowering properties on the other hand. In each section, antihypertensive activity was confirmed at three levels: in vitro, in vivo and in organ baths, and finally, bio-active peptides were identified. In addition, for the hydrolysate of an animal by-product, hydrolysis was optimized, starting from its crude source, and the active fraction was concentrated with ultrafiltration.
Keywords
animal by-product, gelatin, angiotensin converting enzyme (ACE), hypertension

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Citation

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Chicago
Herregods, Griet. 2011. “Activity and Purification of ACE Inhibitory Peptides from Animal By-products: In Vitro and in Vivo Evaluation”. Ghent, Belgium: Ghent University. Faculty of Bioscience Engineering.
APA
Herregods, G. (2011). Activity and purification of ACE inhibitory peptides from animal by-products: in vitro and in vivo evaluation. Ghent University. Faculty of Bioscience Engineering, Ghent, Belgium.
Vancouver
1.
Herregods G. Activity and purification of ACE inhibitory peptides from animal by-products: in vitro and in vivo evaluation. [Ghent, Belgium]: Ghent University. Faculty of Bioscience Engineering; 2011.
MLA
Herregods, Griet. “Activity and Purification of ACE Inhibitory Peptides from Animal By-products: In Vitro and in Vivo Evaluation.” 2011 : n. pag. Print.
@phdthesis{1900049,
  abstract     = {Hypertension or high blood pressure is a major risk factor for cardiovascular diseases, which are the leading cause of death in the Western world. Next to lifestyle modifications, including smoke cessation, exercise, stress management and a healthy diet, functional foods containing angiotensin I-converting enzyme (ACE)-inhibitory peptides can play a role in the prevention of hypertension. ACE (EC 3.4.15.1) plays a key role in different blood pressure-regulating mechanisms, including the renin-angiotensin-aldosteron-system (RAAS) and the kallikrein-kinin-system (KKS), where its action results in an overall increase in blood pressure. Thus, peptides or protein hydrolysates with ACE-inhibitory activity have a blood pressure-lowering effect.
In this project, the potential of different protein hydrolysates for the development of an antihypertensive functional food was investigated. Two main sections can be distinguished, the ACE-inhibitory and antihypertensive activity of gelatin hydrolysates was evaluated on the one hand, and a peptic hydrolysate of an animal by-product and its derivatives were investigated for blood pressure-lowering properties on the other hand. In each section, antihypertensive activity was confirmed at three levels: in vitro, in vivo and in organ baths, and finally, bio-active peptides were identified. In addition, for the hydrolysate of an animal by-product, hydrolysis was optimized, starting from its crude source, and the active fraction was concentrated with ultrafiltration.},
  author       = {Herregods, Griet},
  isbn         = {9789059894617},
  keyword      = {animal by-product,gelatin,angiotensin converting enzyme (ACE),hypertension},
  language     = {eng},
  pages        = {VII, 156},
  publisher    = {Ghent University. Faculty of Bioscience Engineering},
  school       = {Ghent University},
  title        = {Activity and purification of ACE inhibitory peptides from animal by-products: in vitro and in vivo evaluation},
  year         = {2011},
}