Optimisation of the angiotensin converting enzyme inhibition by whey protein hydrolysates using response surface methodology

Ven, C. van der; Gruppen, Harry; Bont, Dries B. A. De; Voragen, A.G.J.

doi:10.1016/s0958-6946(02)00077-8

Cited by 162 publications

(76 citation statements)

References 27 publications

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“…The model was further optimized (simplified model) by only taking into account the parameters which were significant (p < 0.1) as described by van der Ven, et al 20 . A response surface methodology (RSM) curve was plotted using the simplified model with Matlab.…”

Section: Discussionmentioning

confidence: 99%

Strategies for the release of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides in an enzymatic hydrolyzate of α-lactalbumin

et al. 2016

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Bovine α-lactalbumin (α-La) contains numerous dipeptidyl peptidase IV (DPP-IV) inhibitory peptides sequences within its primary structure. In silico analysis indicated that the targeted hydrolysis of α-La with elastase should release DPP-IV inhibitory peptide sequences. An α-La isolate was hydrolysed with elastase under different conditions using an experimental design approach incorporating 3 factors (temperature, pH and enzyme to substrate ratio (E:S) ratio) at 2 levels. The hydrolyzate generated at pH 8.5, 50C, E:S 2.0% (w/w) (H9) displayed the lowest half maximal DPP-IV inhibitory concentration (IC50 = 1.20 ± 0.12 mg mL -1). Five α-La-derived DPP-IV inhibitory peptides (GY, GL, GI, NY and WL) predicted to be released in silico were identified by liquid-chromatography tandem mass spectrometry (LC-MS/MS) within H9 and its simulated gastrointestinal digestion (SGID) sample. This proof of concept study demonstrated the benefit of using a targeted approach combined with an experimental design in the generation of dietary protein hydrolyzates with DPP-IV inhibitory properties. IntroductionDipeptidyl peptidase IV (DPP-IV) is an ubiquitous enzyme which is responsible for the cleavage and inactivation of the incretin hormones, glucose dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (GLP-1) 1 . In the context of type 2 diabetes management, DPP-IV inhibition may be used as a means to improve the regulation of serum glucose in humans. Various DPP-IV inhibitory drugs (gliptins), have been developed to maintain the insulinotropic activity of the incretins in the post-prandial phase 2 .Dietary components, including food protein-derived peptides, have been shown to play a role in the inhibition of DPP-IV in vitro and in certain instances in vivo, for reviews, see: 3,4,5 . In silico studies have shown that selected DPP-IV inhibitory peptide sequences may be found within a wide range of dietary proteins 6,7 . To date, milk proteins appear to be the most frequently studied substrate for the generation of DPP-IV inhibitory peptides. Depending on the enzymatic strategy employed, different milk proteins may appear to be more suitable substrates for the production of DPP-IV inhibitory peptides. For instance, it was recently predicted by Tulipano et al.8 using in silico digestion with gastrointestinal proteinases that -lactoglobulin (-Lg) should yield a higher number of previously identified DPP-IV inhibitory peptides than -La. This was further confirmed following in vitro digestion of -Lg and -La with gastrointestinal enzymes, yielding hydrolyzates with IC 50 values of 0.74 and 1.70 mg mL -1, respectively 8 . Other in silico analysis of the major milk proteins indicated that -lactalbumin (-La) displayed the highest level of sequence coverage (43.9%) for previously identified DPP-IV inhibitory peptides as well as the highest DPP-IV inhibitory potency index (i.e., 17.9 10 -6 µM -1 g -1 ) 7 . It has been suggested that discrepancies between studies to determine the most adequate substrate for the genera...

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Section: Discussionmentioning

confidence: 99%

Strategies for the release of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides in an enzymatic hydrolyzate of α-lactalbumin

et al. 2016

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“…Além da ação hipertensora, a angiotensina II estimula a produção do hormônio aldosterona que age diminuindo a excreção renal de fluido e de sais, aumentando a retenção de água e o volume de fluido extracelular. Vários peptídios com ação inibidora da ACE foram isolados e caracterizados a partir de hidrolisados da β-lactoglobulina e da ∝-lactalbumina [49][50][51][52] .…”

Section: Proteção Ao Sistema Cardiovascularunclassified

Propriedades fisiológicas-funcionais das proteínas do soro de leite

Sgarbieri

2004

Rev. Nutr.

106

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O presente artigo coloca em destaque as propriedades multifuncionais das proteínas presentes no soro de leite bovino, a começar pelo colostro que contém essas proteínas em concentrações muito elevadas e que tem por função garantir a proteção e a imunidade dos recém-nascidos. Essas mesmas proteínas continuam no leite, porém em concentrações bastante reduzidas. A utilização dessas proteínas nas formas de concentrados e isolados protéicos evidenciam propriedades muito favoráveis à saúde no sentido de diminuir o risco de doenças infecciosas e também as consideradas crônicas e/ou degenerativas. Enfatizou-se as propriedades das proteínas do soro de leite e de peptídios delas resultantes no estímulo ao sistema imunológico, na proteção contra microrganismos patogênicos e contra alguns tipos de vírus como o HIV e o vírus da hepatite C, na proteção contra vários tipos de câncer, particularmente de cólon, na proteção da mucosa gástrica contra agressão por agentes ulcerogênicos, evidenciou-se várias linhas de ação protetora das proteínas de soro contra agentes condicionadores de problemas cardiovasculares. Com base em várias propriedades funcionais das proteínas do soro de leite, discutiu-se a vantagem e os benefícios de seu uso como suplemento alimentar para atletas e esportistas em geral. Os possíveis benefícios de vários fatores de crescimento celular, presentes no soro de leite também foram discutidos.Termos de Indexação: proteínas do leite, leite, colostro, propriedades funcionais fisiológicas. A B S T R A C T

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“…Understanding of the impact of hydrolysis parameters on hydrolysate bioactivity has been systematically studied using multifactorial experimental design and response surface methodology (RSM) approaches. 89 In particular when a specic peptide sequence is being targeted for enzymatic release, RSM may be employed to determine the hydrolysis parameters giving an optimum yield of the peptide. For example, RSM has been applied to optimally release an ACE inhibitory peptide, His-Leu-Pro-Leu-Pro (b-casein f(134-138)), from casein using Corolase PP, an intestinal enzyme preparation.…”

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confidence: 99%

Learnings from quantitative structure–activity relationship (QSAR) studies with respect to food protein-derived bioactive peptides: a review

Nongonierma

Fitzgerald

2016

RSC Adv.

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Optimisation of the angiotensin converting enzyme inhibition by whey protein hydrolysates using response surface methodology

Cited by 162 publications

References 27 publications

Strategies for the release of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides in an enzymatic hydrolyzate of α-lactalbumin

Strategies for the release of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides in an enzymatic hydrolyzate of α-lactalbumin

Propriedades fisiológicas-funcionais das proteínas do soro de leite

Learnings from quantitative structure–activity relationship (QSAR) studies with respect to food protein-derived bioactive peptides: a review

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