Production and identification of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from discarded cowhide collagen

He, Long; Wang, Xinyue; Wang, Yanru; Luo, Jianxun; Zhao, Yuhai; Han, Gencheng; Han, Ling; Yu, Qunli

doi:10.1016/j.foodchem.2022.134793

Cited by 17 publications

(14 citation statements)

References 38 publications

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“…Collagen without any treatment was designated as control (CK). Subsequently, the residual IL was removed as described previously 12 . After concentration (RE‐52‐864; Shanghai Yarong Biochemical Instrument Factory, Shanghai, China), collagen concentrate containing IL was mixed with ethanol.…”

Section: Methodsmentioning

confidence: 99%

“…Subsequently, the residual IL was removed as described previously. 12 After concentration (RE-52-864; Shanghai Yarong Biochemical Instrument Factory, Shanghai, China), collagen concentrate containing IL was mixed with ethanol. Subsequently, the solution was stirred at 25°C for 1 h, and then centrifuged at 4500 × g for 10 min.…”

Section: Pretreatment Of Collagen With Ultrasonic and Ilmentioning

confidence: 99%

“…Ultrasound has been reported to disrupt the compact protein structure, break down protein aggregates, and enhance mass transfer efficiency 7 . However, the effect of ultrasonic pretreatment alone on the release of collagen‐derived bioactive peptides is limited 12 . Ionic liquids are a class of organic salts consisting of cations and anions, which have been gradually applied to food processing as a result of their innovative function with respect to improving protein solubility and accelerating reaction rate.…”

Section: Introductionmentioning

confidence: 99%

“…7 However, the effect of ultrasonic pretreatment alone on the release of collagen-derived bioactive peptides is limited. 12 Ionic liquids are a class of organic salts consisting of cations and anions, which have been gradually applied to food processing as a result of their innovative function with respect to improving protein solubility and accelerating reaction rate. Research has shown that proteins pretreated with ionic liquid (IL) resulted in a stretched protein structure and loosened protein aggregates, resulting in an increased protein enzymatic efficiency.…”

Section: Introductionmentioning

confidence: 99%

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Synergistic modification of collagen structure using ionic liquid and ultrasound to promote the production of DPP‐IV inhibitory peptides

Cao

Wang

et al. 2023

J Sci Food Agric

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BACKGROUND Dual modification of collagen was performed using ionic liquid (IL) and ultrasound (US) to modulate the activity of collagen hydrolyzed peptides and reveal the production mechanism of cowhide‐derived dipeptidyl peptidase (DPP‐IV) inhibitory peptides. RESULTS The results revealed that dual modification (IL + US) significantly improved the hydrolytic degree of collagen (P < 0.05). Meanwhile, IL and US tended to promote the break of hydrogen bonds, but inhibit the crosslinking between collagens. The double modification reduced the thermal stability and accelerated the exposure of tyrosine and phenylalanine of collagen, and improved the proportion of small molecular (< 1 kDa) peptides in collagen hydrolysates. Interestingly, the hydrophobic amino acid residues and DPP‐IV inhibitory activity of collagen peptides with small molecular weight (< 1 kDa) was increased further under the combination of IL and US. CONCLUSION Enhanced hypoglycemic activity of collagen peptides can be attained through the dual modification of IL and US. © 2023 Society of Chemical Industry.

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Section: Methodsmentioning

confidence: 99%

Section: Pretreatment Of Collagen With Ultrasonic and Ilmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Synergistic modification of collagen structure using ionic liquid and ultrasound to promote the production of DPP‐IV inhibitory peptides

Cao

Wang

et al. 2023

J Sci Food Agric

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“…In summary, we speculated that the temperature and pH may be important factors in the production of enzymatic digests with DPP-IV inhibitory activity. Dai et al and He et al found that papain has great potential for preparing DPP-IV inhibitory peptides.…”

Section: Resultsmentioning

confidence: 99%

DPP-IV Inhibitory Peptides from Coix Seed Prolamins: Release, Identification, and Analysis of the Interaction between Key Residues and Enzyme Domains

Zhang,

Li,

Feng

et al. 2023

J. Agric. Food Chem.

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Dipeptidyl peptidase IV (DPP-IV) inhibitory peptides can regulate type 2 diabetes by inhibiting the cleavage of glucagon-like peptide-1 and prolonging its half-life. The development of DPP-IV inhibitory peptides is still a hot topic. The primary structure of coix seed prolamins contains peptide sequence fragments that potentially inhibit DPP-IV; however, limited information is available regarding the extraction of peptides from coix seeds and the analysis of their conformational relationships. In this study, novel coix seed prolamin-derived peptides were obtained through single hydrolysis and double-enzyme stepwise hydrolysis. The inhibitory activity of these peptides against DPP-IV was evaluated to explore new functional properties of coix seeds. The results evidenced that the step-by-step enzymolysis (papain and alcalase) compared to single enzymolysis promoted the secondary structure disruption of the hydrolysates, enhanced the β-turn structure, significantly increased the content of peptides below 1 kDa, and exhibited a substantial increase in DPP-IV inhibitory activity (97% inhibition). Three nontoxic DPP-IV inhibitory peptides, namely, LPFYPN, TFFPQ, and ATFFPQ (IC 50 = 70.24, 176.87, 268.31 μM), were isolated and identified. All three peptides exhibited strong interactions with DPP-IV (all K A values >10 3 ). LPFYPN exhibited competitive inhibition, while TFFPQ and ATFFPQ demonstrated mixed competitive−noncompetitive inhibition. Hydrogen bonding and hydrophobic interactions were the main contributors to the coix seed prolamin peptides binding to DPP-IV. The central residue was a key amino acid in the parent peptide sequence, forming a more stable π−π stacking with residues in the active pocket, which may facilitate peptide activity. This study provides theoretical support for the development of coix seed-derived hypoglycemic peptides.

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Effect of tremella polysaccharides on the quality of collagen jelly: insight into the improvement of the gel properties and the antioxidant activity of yak skin gelatin

Zhang,

Han,

Wang

et al. 2024

J Sci Food Agric

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BackgroundThe present study aimed to investigate the effects of tremella polysaccharides on the gel properties and antioxidant activity of yak skin gelatin with a view to improving the quality of collagen jellies. The preparation of composite gels were performed by yak skin gelatin (66.7 mg/mL) and tremella polysaccharides with different concentrations (0, 2, 4, 6, 8 mg/mL), and finally the collagen jelly was prepared by composite gel (yak skin gelatin: 66.7 mg/mL; tremella polysaccharides:6 mg/mL) with the best performance.ResultsTremella polysaccharides not only improved the hardness, springiness, gel strength, water holding capacity and melting temperature of yak skin gelatin, but also enhanced the composite gel's scavenging activity against ABTS radicals, DPPH radicals, O2 and OH radicals. The filling of tremella polysaccharides into the gelatin network increased the number of cross‐linking sites inside the gel, which resulted in that the gel network structure becomes dense and orderly. The gel particles became finer and more uniform, and the thermal stability was improved. Furthermore, the sensory score of commercially available gelatin jelly decreased more rapidly during storage compared to the composite gel jelly.ConclusionThe gel properties and antioxidant activity of yak skin gelatin were improved by adding tremella polysaccharides, and then the quality and storage properties of jelly were improved, which also provided technical reference for the development of functional gel food.This article is protected by copyright. All rights reserved.

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Production and identification of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from discarded cowhide collagen

Cited by 17 publications

References 38 publications

Synergistic modification of collagen structure using ionic liquid and ultrasound to promote the production of DPP‐IV inhibitory peptides

Synergistic modification of collagen structure using ionic liquid and ultrasound to promote the production of DPP‐IV inhibitory peptides

DPP-IV Inhibitory Peptides from Coix Seed Prolamins: Release, Identification, and Analysis of the Interaction between Key Residues and Enzyme Domains

Effect of tremella polysaccharides on the quality of collagen jelly: insight into the improvement of the gel properties and the antioxidant activity of yak skin gelatin

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