Production of dipeptidyl peptidase IV inhibitory peptides from defatted rice bran

Hatanaka, Tadashi; Inoue, Yosikazu; Arima, Jiro; Kumagai, Yuya; Usuki, Hirokazu; Kawakami, Kayoko; Kimura, Masayo; Mukaihara, Takafumi

doi:10.1016/j.foodchem.2012.02.183

Cited by 215 publications

(158 citation statements)

References 27 publications

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“…Similar findings as those for Val-Trp and its reverse peptide have been mentioned in another study, with Ile-Pro (IC 50 0.41 ± 0.07 M) inhibiting DPP-IV whereas its reverse peptide Pro-Ile did not [11]. This result was explained by the fact the N terminal residue of the peptide plays an important role in the inhibition of DPP-IV [11].…”

Section: Discussionsupporting

confidence: 86%

“…The DPP-IV IC 50 values observed for the milk protein hydrolysates described herein are of the same order as values reported in the literature. IC 50 values ranging from 0.075 to 6.4 ± 2.3 mg.mL -1 have previously been reported for various food protein-derived hydrolysates [11,17,19]. It is interesting to note that the milk protein hydrolysates were less potent on a weight basis than the dipeptides (Table 3).…”

Section: Discussionmentioning

confidence: 64%

“…This result was explained by the fact the N terminal residue of the peptide plays an important role in the inhibition of DPP-IV [11]. Different milk protein hydrolysates have been reported for their DPP-IV inhibitory potential including hydrolysates of-lactoglobulin [17,43].…”

Section: Discussionmentioning

confidence: 99%

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Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk protein-derived dipeptides and hydrolysates

2013

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Selected synthetic dipeptides and milk protein hydrolysates were evaluated for their dipeptidyl peptidase IV (DPP-IV) inhibitory properties, and their superoxide (SO) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activities. DPP-IV inhibition was seen with eight out of the twelve dipeptides and 5 of the twelve hydrolysates studied. Trp-Val inhibited DPP-IV, however, inhibition was not observed with the reverse peptide Val-Trp. The most potent hydrolysate inhibitors were generated from casein (CasH2) and lactoferrin (LFH1). Two Trp containing dipeptides, Trp-Val and Val-Trp, and three lactoferrin hydrolysates scavenged DPPH. The dipeptides had higher SO EC 50 values compared to the milk protein hydrolysates (arising from three lactoferrin and one whey protein hydrolysates). Higher molecular mass fractions of the milk protein hydrolysates were associated with the SO scavenging activity. Trp-Val and one lactoferrin hydrolysate (LFH1) were multifunctional displaying both DPP-IV inhibitory and antioxidant (SO and DPPH scavenging) activities. These compounds may have potential as dietary ingredients in the management of type 2 diabetes by virtue of their ability to scavenge reactive oxygen species and to extend the half-life of incretin molecules.

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Section: Discussionsupporting

confidence: 86%

Section: Discussionmentioning

confidence: 64%

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Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk protein-derived dipeptides and hydrolysates

2013

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“…1·5 v. 0·4 mg/ml) for lysozyme hydrolysates. Japanese rice bran has also been used to generate peptides with DPP-IV inhibitory properties (53) . Two hydrolysates were prepared using fungal and bacterial enzyme preparations (Umanizyme G ® and Bioprase SP) and had IC 50 values of 2·3 and 26·4 mg/ml, respectively.…”

Section: Gouda Cheesementioning

confidence: 99%

“…For example, the dipeptides Ile-Pro and Trp-Val had DPP-IV inhibitory activity (Table 1) whereas the reverse peptides Pro-Ile and Val-Trp, respectively had no inhibitory activity (13,53) . In addition, the N-terminal residue of Pro containing dipeptides (Xaa-Pro) was shown to influence the DPP-IV inhibitory activity (53) . The dipeptide Leu-Pro had a fivefold higher IC 50 value than Ile-Pro (2·37 v. 0·41 mM).…”

Section: Structure-activity Relationship Of Peptide Inhibitorsmentioning

confidence: 99%

Food protein hydrolysates as a source of dipeptidyl peptidase IV inhibitory peptides for the management of type 2 diabetes

2013

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The prevalence of type 2 diabetes mellitus (T2DM) is increasing and it is estimated that by 2030 approximately 366 million people will be diagnosed with this condition. The use of dipeptidyl peptidase IV (DPP-IV) inhibitors is an emerging strategy for the treatment of T2DM. DPP-IV is a ubiquitous aminodipeptidase that cleaves incretins such as glucagon like peptide 1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), resulting in a loss in their insulinotropic activity. Synthetic DPP-IV drug inhibitors are being used to increase the half-life of the active GLP-1 and GIP. Dietary intervention is accepted as a key component in the prevention and management of T2DM. Therefore, identification of natural food protein-derived DPP-IV inhibitors is desirable. Peptides with DPP-IV inhibitory activity have been identified in a variety of food proteins. This review aims to provide an overview of food protein hydrolysates as a source of the DPP-IV inhibitory peptides with particular focus on milk proteins. In addition, the proposed modes of inhibition and structure–activity relationship of peptide inhibitors are discussed. Milk proteins and associated peptides also display insulinotropic activity and help regulate blood glucose in healthy and diabetic subjects. Therefore, milk protein derived peptide inhibitors may be a unique multifunctional peptide approach for the management of T2DM.

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Cereal Proteins: Potential Health Applications and Allergenicities

Bleakley

2018

Novel Proteins for Food, Pharmaceuticals and Agriculture

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Production of dipeptidyl peptidase IV inhibitory peptides from defatted rice bran

Cited by 215 publications

References 27 publications

Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk protein-derived dipeptides and hydrolysates

Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk protein-derived dipeptides and hydrolysates

Food protein hydrolysates as a source of dipeptidyl peptidase IV inhibitory peptides for the management of type 2 diabetes

Cereal Proteins: Potential Health Applications and Allergenicities

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