Purification and characterisation of antioxidative peptides from enzymatic hydrolysates of venison protein

Kim, Min Jung; Lee, Seung-Jae; Jeon, Byong-Tae; Moon, Sang Ho; Kim, Bo Kyung; Park, Tae Kyu; Han, Jiarui; Park, Pyo Jam

doi:10.1016/j.foodchem.2008.11.035

Cited by 89 publications

(62 citation statements)

References 26 publications

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“…It is generally accepted that short peptides are relatively stable 25 to gastrointestinal digestion. The intestinal stability of Trp containing dipeptides was predicted using the model developed by Foltz et al 35 It was shown that Trp-Val was moderately stable to intestinal digestion (between 25 to 75 % of intact peptide remaining after 60 min simulated intestinal digestion), whereas 30 other Trp containing dipeptides (Arg-Trp, Lys-Trp, Val-Trp and Ile-Trp) were not predicted to be stable.…”

Section: Discussionmentioning

confidence: 99%

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Inhibition of dipeptidyl peptidase IV (DPP-IV) by tryptophan containing dipeptides

Nongonierma

Fitzgerald

2013

Food Funct.

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Twenty seven Trp containing dipeptides were evaluated for their ability to inhibit dipeptidyl peptidase IV (DPP-IV), a key enzyme involved in incretin hormone processing. Novel DPP-IV inhibitors were identified comprising of three potent dipeptides (Trp-Arg, Trp-Lys and Trp-Leu) with half maximum inhibitory concentration (IC 50 values) <45 mM. With the exception of Leu-Trp which was $20 times less potent than Trp-Leu, their reverse peptide did not inhibit DPP-IV. Trp-Asp was the only peptide studied herein with an N terminal Trp residue which was not a DPP-IV inhibitor. Phosphorylation resulted in an increase in DPP-IV IC 50 , giving values of 482.1 AE 12.9 and >11 000 mM for Trp-Thr and Trp-pThr, respectively. The mode of inhibition of these peptides was studied using Lineweaver and Burk kinetic analysis, which showed both competitive and non-competitive modes of inhibition depending on the peptide sequence. This suggested binding of the peptide inhibitors to different locations on DPP-IV. In silico analysis of the milk proteome revealed that some of the DPP-IV inhibitors identified herein may be released from milk proteins following enzymatic digestion. The results are relevant to understanding the mechanism(s) involved in DPP-IV inhibition by short peptides. This in turn may dictate a more targeted approach for the release of potent peptides from milk proteins with the view of developing biofunctional hydrolysates for the management of type 2 diabetes.

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Section: Discussionmentioning

confidence: 99%

“…Inhibition of dipeptidyl peptidase IV (DDP-IV) by food derived 25 constituents may represent a dietary related approach for the management/control of Type 2 diabetes (T2D). DPP-IV is an enzyme which can be found in different locations of the body including on the surface of various cells and in the circulation.…”

Section: Introductionmentioning

confidence: 99%

Inhibition of dipeptidyl peptidase IV (DPP-IV) by tryptophan containing dipeptides

Nongonierma

Fitzgerald

2013

Food Funct.

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“…Degree of hydrolysis The effect of hydrolysis time on DH was estimated using the method introduced by Kim et al (1996). At the end of each hydrolysis time of 0, 0.5, 1 and 2 h at 37°C, an aliquot of 10 mL of the aqueous suspension of enzyme-treated fractions was removed and mixed with 10 mL of 20% trichloroacetic acid (TCA) to obtain 10% TCA-soluble nitrogen and 10% TCA-insoluble nitrogen and then centrifuged at 15,770×g for 15 min at 4°C.…”

Section: Methodsmentioning

confidence: 99%

Kinetic characterization of Channa striatus muscle sarcoplasmic and myofibrillar protein hydrolysates

et al. 2011

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This study was conducted to evaluate the kinetic characteristics of proteolytic activity of proteases on Channa striatus protein fractions. Degree of hydrolysis (DH), amino acid composition and kinetic parameters of sarcoplasmic and myofibrillar proteins were investigated when incubated with proteinase K and thermolysin, separately. After 30 min incubation with proteases, a decrease in DH of sarcoplasmic protein was observed whereas, hydrolysis of myofibrillar protein with proteases took 2 h with an increase in DH. The major amino acids were glutamic acid (16.6%) in thermolysin-myofibrillar hydrolysate followed by aspartic acid (11.1%) in sarcoplasmic protein fraction with no enzyme treatment and lysine (10%) in thermolysinmyofibrillar hydrolysate. The apparent Michaelis constant of proteinase K was lower than thermolysin for both sarcoplasmic and myofibrillar proteins. However, rate of turnover and enzyme efficiency suggested that sarcoplasmic and myofibrillar proteins are suitable substrates for proteinase K and thermolysin hydrolytic reaction, respectively.

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“…These peptides are very valuable because they have variety of functions and they are easily absorbed in the body and therefore, they can potentially be considered a great alternative for the synthetic antihypertensive drugs (Lee et al, 2010). Although a huge body of research has been dedicated to antihypertensive effect of bioactive peptides from plant (Motoi and Kodama, 2003;Chen et al, 2003;Motoi and Kodama, 2003;Nakano et al, 2006;Kodera and Nio, 2006;Kodera and Nio, 2006;Lee et al, 2006a, b;Zhu et al, 2006;OsegueraToledo et al, 2011;Gonz alez-Garc ıa et al, 2014;OsegueraToledo et al, 2015;Capriotti et al, 2015;Esteve et al, 2015;Coscueta et al, 2016;Da Silva Vaz et al, 2016), terrestrial animals (Morimatsu et al, 1996;Arihara et al, 2001;Nakashima et al, 2002;Saiga et al, 2003;Vercruysse et al, 2005;Arihara, 2006;Yu et al, 2006;Sentandreu and Toldra, 2007;Li et al, 2007;Chang et al, 2007;Wang et al, 2008a;Xu et al, 2009;Shimizu et al, 2009;Kim et al, 2009;Liu et al, 2010;Bernardini et al, 2012;Escudero et al, 2013), seafood (Jeon et al, 1999;Byun and Kim, 2001;Morimura et al, 2002;…”

Section: Ace Inhibitory and Antihypertensive Effectmentioning

confidence: 99%

Peptides: Production, bioactivity, functionality, and applications

Hajfathalian

Ghelichi

Moreno

et al. 2017

Critical Reviews in Food Science and Nutrition

133

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Production of peptides with various effects from proteins of different sources continues to receive academic attention. Researchers of different disciplines are putting increasing efforts to produce bioactive and functional peptides from different sources such as plants, animals, and food industry by-products. The aim of this review is to introduce production methods of hydrolysates and peptides and provide a comprehensive overview of their bioactivity in terms of their effects on immune, cardiovascular, nervous, and gastrointestinal systems. Moreover, functional and antioxidant properties of hydrolysates and isolated peptides are reviewed. Finally, industrial and commercial applications of bioactive peptides including their use in nutrition and production of pharmaceuticals and nutraceuticals are discussed.

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Purification and characterisation of antioxidative peptides from enzymatic hydrolysates of venison protein

Cited by 89 publications

References 26 publications

Inhibition of dipeptidyl peptidase IV (DPP-IV) by tryptophan containing dipeptides

Inhibition of dipeptidyl peptidase IV (DPP-IV) by tryptophan containing dipeptides

Kinetic characterization of Channa striatus muscle sarcoplasmic and myofibrillar protein hydrolysates

Peptides: Production, bioactivity, functionality, and applications

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