Dipeptidyl-peptidase IV inhibitory activity of peptides derived from tuna cooking juice hydrolysates

Huang, Shih-Li; Jao, Chia-Ling; Ho, Kit-Pan; Hsu, Kuo‐Chiang

doi:10.1016/j.peptides.2012.03.006

Cited by 133 publications

(93 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The resulting biopeptides contained in the hydrolysates can be hydrolysed by T and C because these enzymes can cleave specific peptide bonds, namely, pepsin breaks peptides bonds in Tyr, Phe and Leu residues; trypsin in Arg and Lys residues; chymotrypsin in Trp, Phe, Tyr, Met and Leu residues. Huang et al (2012) observed that two peptides Fig. 4 Influence of a previous pH treatment (4 or 7) of peptide fractions (Alb1H103; GloH88 and GluH24) on ACEIA, ATA and DPPIVIA, followed by an in vitro gastrointestinal digestion.…”

Section: Stability Of Bioactivity Of Hydrolysates On An In Vitro Gastmentioning

confidence: 99%

“…During the simulated gastrointestinal digestion, the peptides were truncated into smaller fragments, some of which increased the DPPIV inhibitory potential. Huang et al (2012) suggest that the smaller peptides may have greater intestinal permeability than the original ones. They also found that the DPPIV inhibitory potential of other peptides isolated from tuna cooking juice hydrolysates was retained or improved.…”

Section: Stability Of Bioactivity Of Hydrolysates On An In Vitro Gastmentioning

confidence: 99%

See 1 more Smart Citation

Effects of heat and pH treatments and in vitro digestion on the biological activity of protein hydrolysates of Amaranthus hypochondriacus L. grain

et al. 2016

View full text Add to dashboard Cite

The aim of this work was to assess the effects of temperature (T), time (t) and pH treatments and an in vitro digestion on the stability of the angiotensin I-convertingenzyme-inhibitory activity (ACEIA) and antithrombotic activity (ATA; assessed as inhibition of platelet aggregation) of selected protein hydrolysates of amaranth named Alb1H103 and GloH88 and GluH24 with dipeptidyl peptidase IV inhibitory activity (DPPIVIA). Heat treatment (40-100°C) for 1 h showed no significant differences among ACEIA, DPPIVIA and ATA of the heated hydrolysates at pH 4 and 7. There was no statistically significant loss of any bioactivity under heat treatment for 3 h at pH 4.0. Alb1H103 and GluH24 maintained the inhibitory activity of ACE and ATA at pH 7.0 for 3 h, whereas GloH88 maintained ACEIA and ATA for 2.0 h at pH 7.0. The pH effect on hydrolysates bioactivity was assessed in the range of 2.0-12.0. This was negligible on ACEIA, ATA and DPPIVIA. The in vitro digestion was performed using pepsin, trypsin (T) and a-chymotrypsin (C). A previous treatment of hydrolysates with pepsin improved the proteolytic activities of T and C. The hydrolysates kept at 100°C for 1 h at pH 4.0, showed a significant increase in bioactivity. Conversely, a treatment at pH 7.0 showed no significant difference (p \ 0.05) in the hydrolysates bioactivities after their digestion. Thus, biological activity of hydrolysates may be preserved or enhanced, depending on their processing conditions.

show abstract

Section: Stability Of Bioactivity Of Hydrolysates On An In Vitro Gastmentioning

confidence: 99%

Section: Stability Of Bioactivity Of Hydrolysates On An In Vitro Gastmentioning

confidence: 99%

Effects of heat and pH treatments and in vitro digestion on the biological activity of protein hydrolysates of Amaranthus hypochondriacus L. grain

et al. 2016

View full text Add to dashboard Cite

show abstract

“…Hydrolysis of the East Asian azuki bean with proteolytic or microbial enzymes produced hydrolysates with Gly-Pro-Ala-Glu 41.9 Tuna cooking juice Pro-Gly-Val-Gly-Gly-Pro-Leu-Gly-Pro-Ile-Gly-Pro-Cys-Tyr-Glu 116 (62) Cys-Ala-Tyr-Gln-Trp-Gln-Arg-Pro-Val-Asp-Arg-Ile-Arg 78 Pro-Ala-Cys-Gly-Gly-Phe-Tyr-Ile-Ser-Gly-Arg-Pro-Gly 96.4…”

Section: Proceedings Of the Nutrition Societymentioning

confidence: 99%

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

2013

View full text Add to dashboard Cite

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.

show abstract

“…Similarly, milk protein hydrolysates have been evaluated for DPP-4 inhibitory activity, and five milk protein hydrolysates were shown to competitively inhibit DPP-4 (Nongonierma and Fitzgerald 2013). Interestingly, dosedependent inhibition of DPP-4 was recently demonstrated by peptides (>1422 Da) isolated from tuna cooking juice, which can actively pass through the digestive tract, retaining inhibitory potential (Huang et al 2008). A small number of studies have reported medicinal plant DPP-4 inhibitory activity (Lendeckel et al 2002;Parmar et al 2012).…”

mentioning

confidence: 99%

Lactobacilli possess inhibitory activity against dipeptidyl peptidase-4 (DPP-4)

et al. 2015

View full text Add to dashboard Cite

Dipeptidyl peptidase-4 (DPP-4) plays an important role in the enzymatic inactivation of incretin hormones. In this context, drugs that inhibit DPP-4 have been developed and clinically approved as therapies for type 2 diabetes. As the primary substrates of DPP-4 are produced in the intestinal lining, we investigated whether lactobacilli colonizing the gut could inhibit this enzyme. Fifteen Lactobacillus strains (Lb 1-15) from human infant faecal samples were isolated, identified, extracted and screened for inhibitory activity against DPP-4. Activity was compared against Lactobacillus reference strains (Ref 1-7), a Gram-positive control (Ctrl 1) and two Gram-negative controls (Ctrl 2-3). A range of DPP-4 inhibitory activity was observed (10-32 %; p<0.05-0.001). Strains of L. plantarum (12-25 %) and L. fermentum (14 %) had significant inhibitory activity. However, we noted that Escherichia coli (Ctrl 2) and Salmonella Typhimurium (Ctrl 3) had the greatest inhibitory activity (30-32 %). Contrastingly, some isolates (Lb 12-15) and reference cultures (Ref 1-4), instead of inhibiting DPP-4, actually enhanced it, perhaps indicating the presence of X-prolyldipeptidyl-amino-peptidase (PepX). This provides a future rationale for using probiotic bacteria or their components for management of type 2 diabetes via DPP-4 inhibition.

show abstract

Dipeptidyl-peptidase IV inhibitory activity of peptides derived from tuna cooking juice hydrolysates

Cited by 133 publications

References 23 publications

Effects of heat and pH treatments and in vitro digestion on the biological activity of protein hydrolysates of Amaranthus hypochondriacus L. grain

Effects of heat and pH treatments and in vitro digestion on the biological activity of protein hydrolysates of Amaranthus hypochondriacus L. grain

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

Lactobacilli possess inhibitory activity against dipeptidyl peptidase-4 (DPP-4)

Contact Info

Product

Resources

About