Cloning and characterization of a recombinant α-glucosidase from Ensifer adhaerens NBRC 100388 and evaluation of its glucosyl transfer activity

Suzuki, Tatsuya; Fukaya, Miyu; Takahashi, Kuniyuki; Takeuchi, Mitsuaki; Hara, Ryoichi; Ogawa, Jun; Ueda, Makoto

doi:10.1016/j.bcab.2020.101837

Cited by 3 publications

(2 citation statements)

References 24 publications

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“…Among the metal ions, the CuSO 4 (32.36%) inhibited the activity of the PersiAlpha‐GL1. Similar decrease of the α‐glucosidase activity in the presence of the Cu 2+ was reported by the recombinant α‐glucosidase from Ensiferadhaerens (Suzuki et al., 2020). The metal‐chelating, EDTA showed negligible reduction on the activity of enzyme (87%).…”

Section: Resultssupporting

confidence: 82%

The novel homologue of the human α‐glucosidase inhibited by the non‐germinated and germinated quinoa protein hydrolysates after in vitro gastrointestinal digestion

Salami

Motahar

Ariaeenejad

et al. 2021

Journal of Food Biochemistry

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Quinoa (Chenopodium quinoa Willd) is a potential source of protein with ideal amino acid profiles which its bioactive compounds can be improved during germination and gastrointestinal digestion. The present investigation studies the impact of germination for 24 hr and simulated gastrointestinal digestion on α‐glucosidase inhibitory activity of the quinoa protein and bioactive peptides against the novel homologue of human α‐glucosidase, PersiAlpha‐GL1. The sprouted quinoa after gastroduodenal digestion was the most effective α‐glucosidase inhibitor showing 81.10% α‐glucosidase inhibition at concentration 4 mg/ml with the half inhibition rate (IC50) of 0.07 mg/ml. Based on the kinetic analysis, both the germinated and non‐germinated samples before and after digestion were competitive‐type inhibitors of α‐glucosidase. Results of this study showed the improved α‐glucosidase inhibitory activity of the quinoa bioactive peptides after germination and gastrointestinal digestion and highlighted the potential of metagenome‐derived PersiAlpha‐GL1 as a novel homologue of the human α‐glucosidase for developing the future anti‐diabetic drugs. Practical applications This study aimed to evaluate the effect of germination and gastrointestinal digestion of the quinoa protein and bioactive peptides on α‐glucosidase inhibitory activity against the novel PersiAlpha‐GL1. Metagenomic data were used to identify the novel α‐glucosidase structurally and functionally homologue of human intestinal. The results showed the highest inhibition on PersiAlpha‐GL1 by a germinated quinoa after gastroduodenal digestion and confirmed the potential of PersiAlpha‐GL1 to enhance the effectiveness of the anti‐diabetic drugs for industrial application.

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Section: Resultssupporting

confidence: 82%

The novel homologue of the human α‐glucosidase inhibited by the non‐germinated and germinated quinoa protein hydrolysates after in vitro gastrointestinal digestion

Salami

Motahar

Ariaeenejad

et al. 2021

Journal of Food Biochemistry

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show abstract

“…The supernatant containing the α-glucosidase was stored at −20 °C for further analysis. The α-glucosidase activity was determined by measuring the amount of glucose released during the enzymatic hydrolysis of maltose ( Suzuki et al, 2020 ). Briefly, A reaction mixture (1.0 mL) consisting of an appropriate centration of enzyme, 0.5 M maltose, and 0.4 mL PBS (pH 6.8) was incubated at 37 °C for 20 min.…”

Section: Methodsmentioning

confidence: 99%

Hypoglycemic activity in vivo and in vitro of the Lotus (Nelumbo nucifera Gaertn.) seed skin (testa) phenolic-rich extracts

Xu,

Wang,

Gong

2024

Food Chemistry: X

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Characterization of regioselective glycosyltransferase of Rhizobium pusense JCM 16209T useful for resveratrol 4′-O-α-d-glucoside production

Kimoto

Takeuchi

Kishino

et al. 2022

Journal of Bioscience and Bioengineering

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Cloning and characterization of a recombinant α-glucosidase from Ensifer adhaerens NBRC 100388 and evaluation of its glucosyl transfer activity

Cited by 3 publications

References 24 publications

The novel homologue of the human α‐glucosidase inhibited by the non‐germinated and germinated quinoa protein hydrolysates after in vitro gastrointestinal digestion

The novel homologue of the human α‐glucosidase inhibited by the non‐germinated and germinated quinoa protein hydrolysates after in vitro gastrointestinal digestion

Hypoglycemic activity in vivo and in vitro of the Lotus (Nelumbo nucifera Gaertn.) seed skin (testa) phenolic-rich extracts

Characterization of regioselective glycosyltransferase of Rhizobium pusense JCM 16209T useful for resveratrol 4′-O-α-d-glucoside production

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