The proportion–ratio on <i>dipeptidyl aminopeptidase</i>-4 (DP-4) inhibition by gelatin compared to synthetic sitagliptin

Atma, Yoni; Lioe, Hanifah Nuryani; Prangdimurti, Endang; Seftiono, Hermawan; Taufik, Moh.; Fitriani, Dita; Mustopa, Apon Zaenal

doi:10.1080/15321819.2019.1613243

Cited by 2 publications

(8 citation statements)

References 26 publications

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“…The gelatin solution from bone of Pangasius catfish (Pangsius sutchi) which was extracted on our previous study [15]. The Hydroxyproline Colorimetric Assay Kit (containing 10 mL Oxidation buffer, 0.6 mL Chloramin T concentrate, 5 mL Perchloric acid/Isopropanol solution, 5 mL p-dimethylaminobenzaldehyde (DMAB) concentrate (in DMSO) and 0.1 mL Hydroxyproline standard) was purchased from Biovision Inc. (Milpitas, CA, USA).…”

Section: A Materials and Reagentsmentioning

confidence: 99%

“…It was performed using microplate reader (Multiscan Ex, Champaign, IL, USA) mated with 96-well microplate and interpreted by the color amplification of reacted solution absorbance at visible wavelength [5]. The procedure of analysis is according to our previous study [15]. In this quantification, Sitagiliptin in concentration of 0.1 ng/mL (diluted with 100 mM buffer Tris, pH 8) and 10 μg/mL Diprotin A were used as standard.…”

Section: F Determination Of Dpp-iv Inhibitory Activitymentioning

confidence: 99%

“…The Ministry of Marine Affairs and Fisheries of Indonesia was targeted the Pangasius catfish production in 2018 reaching 604.587 ton [23], it would inflicted to they waste especially bones, which is contribute about 12.44% for total fish weight. In addition, our previous study also shown that the gelatin from bone of Indonesia Pangasius catfish has DPP-IV inhibitory activiy, and it was above of bovine and fish skin gelatin activities [15]. Consequently, it is required to further analysis of this gelatin hydrolysate in order to discover a superior and sustainable source of bioactive peptide with DPP-IV inhibitory activity.…”

Section: Introductionmentioning

confidence: 99%

“…Almost all type of gelatin sources have shown inhibitory activity against DPP-IV covering traditional and alternative origin [14], [15], [16]. Even though, most of gelatin or derivates is from mammalians, such as cow and pig [17], but some research were used gelatin from alternative source in order to seeking a bioactive peptide for DPP-IV inhibitor [15], [16], [18], [19]. It is caused by socio-religion and cultural aspects, where are gelatin derived from porcine is unacceptable in Muslim and Jewish communities, whereas bovine or cow gelatin is not accepted by Hindu community [20].…”

Section: Introductionmentioning

confidence: 99%

“…The gelatin from alternative sources which has been tested for generating bioactive peptide as DPP-IV inhibitor monopolized by fish gelatin. They were involved gelatin from skin of salmon [18], [19] hake, halibut, milkfish, nila tilapia [16] and pangasius catfish [15]. Bioactive peptide derived from warm-water fish were higher than other in order to inhibit DPP-IV action [16].…”

Section: Introductionmentioning

confidence: 99%

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Dipeptidyl Peptidase IV (DPP-IV) Inhibitory Activity of Ultrafiltration and Gel Filtration Fraction of Gelatin Hydrolyaste Derived from Bone of Fish for Antidiabetes

Atma¹,

Lioe²,

Prangdimurti³

et al. 2019

Int. J. Adv. Sci. Eng. Inf. Technol.

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Bioactive peptides have been investigated largely for many biofunctional properties. The aim of this research was to determine the inhibitory activity of ultrafiltration (UF) and gel filtration (GF) fractions of gelatin derived from bone of Pangasius catfish against dipeptidyl peptidase IV (DPP-IV). Previous studies have shown that gelatin from skins of salmon, hake, halibut, milkfish, tilapia and bone of pangasius catfish have the activity in DPP-IV inhibition. While, as inhibitor, most of previous and recent studies shown that separation and fractination of gelatin hydrolysate increase their activity. This research was conducted in three stages including gelatin hydrolysates fractination by ultrafiltration (UF), UF fraction loaded into gel filtration (GF) and DPP-IV inhibition measurement. The fish bone gelatin was hydrolyzed using flavourzyme at three enzyme/substrate ratios (E/S of 3%, 6% and 9%) with incubation times 4, 6, and 8 h. Then, the hydrolysates fractioned by ultrafiltration with 3 kDa cutoff membrane continued with Superfine G-25 sephadex column (65 cm x 3 cm, flow rate 1 mL/min). The result shown that both group of fractions i.e UF and GF have inhibitory activity regarding their capacity to inhibit DPP-IV. The UF fraction >3 kDa derived from 9% (E/S) ratio for hdyrolysis were superb as DPP-IV inhibitor than other fractions, the highest one also has bioactivity higher than other previous fish gelatin fractions.

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Section: A Materials and Reagentsmentioning

confidence: 99%

Section: F Determination Of Dpp-iv Inhibitory Activitymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Dipeptidyl Peptidase IV (DPP-IV) Inhibitory Activity of Ultrafiltration and Gel Filtration Fraction of Gelatin Hydrolyaste Derived from Bone of Fish for Antidiabetes

Atma¹,

Lioe²,

Prangdimurti³

et al. 2019

Int. J. Adv. Sci. Eng. Inf. Technol.

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Characterization of DPP-IV Inhibitory Peptides Using an In Vitro Cell Culture Model of the Intestine

Jin

Shang

Teng

et al. 2021

J. Agric. Food Chem.

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Here, we characterize the activities of two depeptidyl peptidase-IV (DPP-IV) inhibitory peptides, VLATSGPG and LDKVFER, using the Caco-2 monolayer model for the intestine. VLATSGPG and LDKVFR inhibited the DPP-IV in the cells via a mixed-type inhibition mode, with in situ IC50 values of 207.3 and 148.5 μM, respectively. Furthermore, VLATSGPG and LDKVFR were transported intact across the cells, with P app values of 2.41 ± 0.16 and 4.23 ± 0.29 × 10–7 cm/s, respectively. Fragmented peptides were identified in the basolateral side of the membrane. Two of these, GPG and VLA, exhibited high inhibitory activities of 83.6 ± 3.3 and 58.5 ± 2.5%, respectively, at 100 μM concentration. Although 3 mM VLATSGPG and LDKVFR were transported across the epithelium in a concentration-dependent manner, their transport did not damage the tight junction proteins, ZO-1 and occludin. This study demonstrates that the two peptides potentially regulate DPP-IV activity in the intestine.

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The proportion–ratio on dipeptidyl aminopeptidase-4 (DP-4) inhibition by gelatin compared to synthetic sitagliptin

Cited by 2 publications

References 26 publications

Dipeptidyl Peptidase IV (DPP-IV) Inhibitory Activity of Ultrafiltration and Gel Filtration Fraction of Gelatin Hydrolyaste Derived from Bone of Fish for Antidiabetes

Dipeptidyl Peptidase IV (DPP-IV) Inhibitory Activity of Ultrafiltration and Gel Filtration Fraction of Gelatin Hydrolyaste Derived from Bone of Fish for Antidiabetes

Characterization of DPP-IV Inhibitory Peptides Using an In Vitro Cell Culture Model of the Intestine

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