<i>In Vitro</i>Survey of<i>α</i>-Glucosidase Inhibitory Food Components

Matsui, Toshiro; Yoshimoto, Chiho; Osajima, Katsuhiro; Oki, Tomoyuki; Osajima, Yutaka

doi:10.1271/bbb.60.2019

Cited by 198 publications

(134 citation statements)

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“…Diabetes mellitus (DM) is an endocrine system disease, characterised by chronic hyperglycaemia with impaired carbohydrate, fat and protein metabolism, which causes metabolic disorders resulting in multiple organ damage syndromes. Control of blood glucose levels remains the most effective therapeutic approach for DM (Matsui et al 1996;Yu et al 2012). Glycoside-trimming enzymes are important in the digestion of carbohydrates.…”

Section: In Vitro Antioxidant and α-Amylase Inhibitory Properties Of mentioning

confidence: 99%

In vitro antioxidant and α-amylase inhibitory properties of watermelon seed protein hydrolysates

Arise¹

2016

EEB

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Proteins from watermelon (Citrullus lanatus L.) seed were isolated using acid-induced precipitation method and then hydrolysed using pepsin, trypsin and alcalase. The hydrolysates were investigated for in vitro antioxidant and α-amylase inhibitory properties. The yield of peptic hydrolysis (68.9 ± 1.0%) was significantly higher than of tryptic (41.4 ± 1.1%) and alcalase (38.5 ± 0.5%) hydrolysis. Peptic hydrolysate showed the highest radical-scavenging ability whereas tryptic hydrolysate gave the highest reducing ability. In a concentrationdependent manner, the hydrolysates demonstrated potent α-amylase inhibitory ability with alcalase and tryptic hydrolysates exhibiting 86.0 ± 3.9 and 83.0 ± 3.5% α-amylase inhibition respectively (IC 50 0.149 to 0.234 mg mL -1). Kinetic analysis revealed that the three enzyme hydrolysates inhibited α-amylase activity via a non-competitive inhibition mechanism. The results therefore indicate that these multidirectional bioactivities of watermelon seed protein hydrolysates may serve as useful tools in the formulation of antidiabetic agents.

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Section: In Vitro Antioxidant and α-Amylase Inhibitory Properties Of mentioning

confidence: 99%

In vitro antioxidant and α-amylase inhibitory properties of watermelon seed protein hydrolysates

Arise¹

2016

EEB

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“…Test substances were dissolved in DMSO, and the assay was carried out according to a published procedure, with slight modifications (Matsui et al, 1996). a-Glucosidase from Saccharomyces cerevisiae and 4-nitrophenyl a-D-glucopyranoside (PNP-G) were purchased from Sigma-Aldrich, St. Louis, MO.…”

Section: Inhibition Of A-glucosidasementioning

confidence: 99%

α-Glucosidase inhibition, 15-lipoxygenase inhibition, and brine shrimp toxicity of extracts and isolated compounds fromTerminalia macropteraleaves

Pham

Malterud

Paulsen

et al. 2014

Pharmaceutical Biology

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Context: Terminalia macroptera Guill. & Perr. (Combretaceae), a tree that grows in West Africa, has been used in traditional medicine against a variety of diseases such as hepatitis, gonorrhea, skin diseases, and diabetes. Objective: To investigate enzyme inhibitory activity against a-glucosidase and 15-lipoxygenase (15-LO) and toxicity against brine shrimp of extracts and compounds from T. macroptera leaves. Materials and methods: Methanol extract, ethyl acetate, and butanol extracts obtained from the methanol extract, six isolated polyphenols (chebulagic acid, chebulic acid trimethyl ester, corilagin, methyl gallate, narcissin, and rutin), and shikimic acid were evaluated for enzyme inhibition and toxicity. Results: In enzyme inhibition assays, all extracts showed high or very high activity. Chebulagic acid showed an IC 50 value of 0.05 mM towards a-glucosidase and 24.9 ± 0.4 mM towards 15-LO, in contrast to positive controls (acarbose: IC 50 201 ± 28 mM towards a-glucosidase, quercetin: 93 ± 3 mM towards 15-LO). Corilagin and narcissin were good 15-LO and a-glucosidase inhibitors, as well, while shikimic acid, methyl gallate, and chebulic acid trimethyl ester were less active or inactive. Rutin was a good a-glucosidase inhibitor (IC 50 ca. 3 mM), but less active towards 15-LO. None of the extracts or the isolated compounds seemed to be very toxic in the brine shrimp assay compared with the positive control podophyllotoxin. Conclusion: Inhibition of a-glucosidase in the gastrointestinal tract may be a rationale for the medicinal use of T. macroptera leaves against diabetes in traditional medicine in Mali. The plant extracts and its constituents show strong inhibition of the peroxidative enzyme 15-LO.

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“…Compound had strongest inhibitory activity in these compounds, and IC 50 value of was 2-fold higher than those of and . Previously, a-glucosidase inhibitory activity of natural occurring flavan-3-ols has been reported [18][19][20] . IC 50…”

Section: Resultsmentioning

confidence: 99%

“…value of (+)-catechin 18) and ( )-epicatechin 19) were 12.8 and 0.18 mM, respectively. Compounds , and showed more potent inhibitory activity than those of catechins.…”

mentioning

confidence: 93%