Angiotensin-I-converting enzyme inhibitory activities of gastric and pancreatic proteinase digests of whey proteins

Mullally, Margaret M.; Meisel, Hans; Fitzgerald, Richard J.

doi:10.1016/s0958-6946(97)00018-6

Cited by 195 publications

(161 citation statements)

References 14 publications

Supporting

Mentioning

136

Contrasting

Unclassified

Order By: Relevance

“…Hydrolysis simulating gastrointestinal tract Simulation of gastrointestinal linseed hydrolysis was performed according to the method of Pihlanto-Leppälä et al (1998) and Mullally et al (1997), with the modifications reported by Yoshie- . Methanolic extract was prepared for analysis of ACE inhibition, DPPH radical scavenging, copper reduction, LOX inhibitory activity, and bile acid binding capacity.…”

Section: Methodsmentioning

confidence: 99%

Functional Properties of Linseed Meal Fractions: Application as Nutraceutical Ingredient

Yoshie-Stark

Müller

Kawarada

et al. 2011

FSTR

View full text Add to dashboard Cite

Brown linseed (Linum ustatissimum) is pressed to produce oil, and the remaining linseed meal is rich in protein and soluble dietary fiber. To utilize the derivatives of linseed meal as food ingredients or additives, linseed meal was fractionated by controlling pH on a pilot-plant scale. Chemical composition, functional properties and health-related bioactivities, such as angiotensin-converting enzyme (ACE) inhibition and antioxidant activities, of the fractions were then analyzed. The alkaline soluble protein had the highest content of secoisolariciresinol diglucoside (SDG) and showed good emulsification activity, comparable to that of whole egg. The acid-soluble fraction showed the highest viscosity. ACE inhibition, antioxidant activities, and bile acid binding activity were observed in the soluble dietary fiber fraction. There was no correlation between SDG content and bioactivities. These findings indicate that the acid-soluble fraction is useful as a food ingredient to increase viscosity, while the soluble dietary fiber fraction has health-related features.Keywords: Linum ustatissimum, fractionation, functional properties, hydrolysis, ACE inhibition, DPPH radical scavenging, Cu reduction, bile acid binding, LOX inhibition *To whom correspondence should be addressed. E-mail: yumiko_y@toyo.jp IntroductionLinseed is useful for its oil, while the remaining material after oil extraction is rich in protein and viscous mucilage. Many researchers attempted to utilize whole linseed by fractionation; however, these purification methods are timeconsuming, expensive or decompose useful compounds such as phenolic acids (Chung et al., 2005, Oomah and Mazza, 1993, Oomah and Mazza, 1998. Interest in the use of whole linseed and its derivatives as functional foods or nutraceutical ingredients is still growing. Thus, we have attempted to fractionate de-oiled linseed using the simplest method possible. After establishing a simple fractionation method in preliminary experiments, it was necessary to further determine the functions and activities of each fraction in order to select the appropriate food application.Physicochemical properties such as emulsification capacity and viscosity have provided ideas on how to apply linseed fractions to food processing. As in the case of lupin fractions (Yoshie-Stark et al., 2004), a protein-rich fraction may express angiotensin-converting enzyme (ACE) inhibitory activity after being converted to a peptide by gastrointestinal hydrolysis. Dietary fiber binds bile acids; therefore, a dietary-fiber-rich, viscous linseed fraction may exhibit bile acid binding and affect cholesterol metabolism in the human body (Wang et al., 2001).In order to use linseed fractions for food applications, such fractions should not promote oxidation or induce spoliation. Therefore, the nonpromotion of lipid oxidation should be confirmed. It has been reported that lignans show certain health-related activities, and linseed is one of the richest sources of lignans (Westcott and Muir, 2003). The main et al. (2010), fra...

show abstract

Section: Methodsmentioning

confidence: 99%

Functional Properties of Linseed Meal Fractions: Application as Nutraceutical Ingredient

Yoshie-Stark

Müller

Kawarada

et al. 2011

FSTR

View full text Add to dashboard Cite

show abstract

“…Da mesma maneira, outros autores mencionam fato semelhante, porém utilizando métodos diferentes do presente estudo na determinação da atividade inibitória da ECA. Assim, Mullally et al (1997) encontraram baixos valores de AI para a α-lactalbumina (3,5%), WPC (7,1%) e β-lactoglobulina (9,6%), antes de se proceder a hidrólise por meio de várias enzimas proteolíticas. Nesse caso, nenhuma atividade inibitória foi observada para a β-lactoglobulina ovina e caprina, antes de serem hidrolisadas por diferentes proteases (HERNÁNDEZ-LEDESMA et al, 2002).…”

Section: Resultsunclassified

“…Assim, com relação ao WPC, Mullally et al (1997), empregando cinco diferentes proteases (tripsina, quimotripsina, elastase, PTN3.0S e pancreatina), obtiveram hidrolisados cuja AI variou de 35,0 a 88,6%, faixa essa que abrange a dos resultados encontrados no presente estudo. Ven et al (2002) utilizaram uma pancreatina na hidrólise de WPC 60, variando diversos parâmetros hidrolíticos, tendo observado que os valores de IC 50 de todos os hidrolisados variou entre 0,17 a 0,88 mg/mL, faixa essa que engloba alguns dos valores observados no presente trabalho.…”

Section: Resultsunclassified

“…Somente dois estudos foram encontrados na literatura abordando o efeito do tipo de enzima sobre a atividade inibitória da ECA de hidrolisados de WPC, sendo um do mesmo grupo de pesquisa do presente trabalho e um de outros pesquisadores (MULLALLY et al, 1997). Ressalta-se que em nenhum destes estudos foram utilizadas as enzimas do presente trabalho.…”

Section: Efeito Do Tipo De Enzimaunclassified

“…Com relação ao trabalho de outros pesquisadores, Mullally et al (1997) avaliaram o efeito de cinco enzimas, tendo mostrado que as mais eficientes foram a tripsina (88,6%) e a quimotripsina (87,7%), seguidas pela pancreatina (78,2%), PTN 3.0S (60,8%) e, por último, a elastase (35,5%). De acordo com estes autores, os menores valores de AI observados para esta última enzima relacionam-se ao fato que ela hidrolisa ligações peptídi-cas envolvendo aminoácidos com cadeias laterais não aromáticas e não carregadas, o que levaria a formação de peptídeos com baixa ação inibitória da ECA.…”

Section: Efeito Do Tipo De Enzimaunclassified

See 2 more Smart Citations

OBTENÇÃO DE HIDROLISADOS DE CONCENTRADO PROTEICO DE SORO DE LEITE COM ATIVIDADE INIBITÓRIA DA ENZIMA CONVERSORA DE ANGIOTENSINA: AÇÃO DAS PROTEASES DO Bacillus licheniformis E DO Aspergillus oryzae

SILVESTRE¹,

Morais²,

SILVA³

et al. 2011

Publ.Exatas

View full text Add to dashboard Cite

Lactokinins: Whey protein-derived ACE inhibitory peptides

Fitzgerald

Meisel²

1999

Nahrung

View full text Add to dashboard Cite

Angiotensin-I-converting enzyme (ACE) has been classically associated with the renin-angiotensin system which regulates peripheral blood pressure. Peptides derived from the major whey proteins, i.e. alpha-lactalbumin (alpha-la) and beta-lactoglobulin (beta-lg) in addition to bovine serum albumin (BSA), inhibit ACE. Some of these inhibitory peptides, i.e. alpha-lactorphin (alpha-la f(50-53)), beta-lactorphin (beta-lg f(102-105)), beta-lactotensin (beta-lg f(146-149) and albutensin A (BSA f(208-216)), have other bioactivities. The most potent lactokinin reported to date, (beta-lg f(142-148)), has an ACE IC50 of 42.6 mumol/l. While they do not have the inhibitory potency of synthetic drugs commonly used in the treatment of hypertension, these naturally occurring peptides may represent nutraceutical/functional food ingredients for the prevention/treatment of high blood pressure. Studies with gastric and pancreatic proteinase digests of whey proteins indicate that enzyme specificity rather than extent of hydrolysis dictates the ACE inhibitory potency of whey hydrolysates.

show abstract

Angiotensin-I-converting enzyme inhibitory activities of gastric and pancreatic proteinase digests of whey proteins

Cited by 195 publications

References 14 publications

Functional Properties of Linseed Meal Fractions: Application as Nutraceutical Ingredient

Functional Properties of Linseed Meal Fractions: Application as Nutraceutical Ingredient

OBTENÇÃO DE HIDROLISADOS DE CONCENTRADO PROTEICO DE SORO DE LEITE COM ATIVIDADE INIBITÓRIA DA ENZIMA CONVERSORA DE ANGIOTENSINA: AÇÃO DAS PROTEASES DO Bacillus licheniformis E DO Aspergillus oryzae

Lactokinins: Whey protein-derived ACE inhibitory peptides

Contact Info

Product

Resources

About